Tumor Endothelial Marker Report: TEM27 (slit-3)

TEM domain structure

	TEM domain structure

TEM Sequence Analysis

name from to source/E description

Signalp 1 33

LRRNT 33 60 Pfam, E = 5e-09 This domain belongs to the cysteine rich domains nkown to flank LRR.

LRR 62 85 Pfam, E = 1.3 LRR are proposed to be involved in protein-protein interactions.

LRR 86 109 Pfam, E = 0.005 LRR are proposed to be involved in protein-protein interactions.

LRR 110 133 Pfam, E = 0.21 LRR are proposed to be involved in protein-protein interactions.

LRR 134 157 Pfam, E = 0.0041 LRR are proposed to be involved in protein-protein interactions.

LRR 158 181 Pfam, E= 0.5 LRR are proposed to be involved in protein-protein interactions.

LRR 182 205 Pfam, E= 0.75 LRR are proposed to be involved in protein-protein interactions.

LRR 206 227 Pfam, E= 9.3e+02 LRR are proposed to be involved in protein-protein interactions.

LRRCT 215 264 Pfam, E= 5e-17 This domain belongs to the cysteine rich domains nkown to flank LRR.

LRRNT 279 306 Pfam, E= 8.9e-07 This domain belongs to the cysteine rich domains nkown to flank LRR.

LRR 308 331 PfamFrag, E= 4.2 LRR are proposed to be involved in protein-protein interactions.

LRR 332 355 Pfam, E= 0.0012 LRR are proposed to be involved in protein-protein interactions.

LRR 356 379 Pfam, E= 0.046 LRR are proposed to be involved in protein-protein interactions.

LRR 380 403 PfamFrag, E= 3 LRR are proposed to be involved in protein-protein interactions.

LRR 404 427 Pfam, E= 0.15 involved in protein-protein interaction

LRRCT 437 486 Pfam, E= 3.3e-13 This domain belongs to the cysteine rich domains nkown to flank LRR.

LRRNT 504 531 Pfam, E= 9.7e-06 LRR flanking cysteine rich domains

LRR 558 581 Pfam, E= 0.064 LRR are proposed to be involved in protein-protein interactions.

LRR 582 605 Pfam, E= 0.62 LRR are proposed to be involved in protein-protein interactions.

LRR 606 629 Pfam, E= 2.5 LRR are proposed to be involved in protein-protein interactions.

LRR 630 653 Pfam, E= 0.67 LRR are proposed to be involved in protein-protein interactions.

LRRCT 663 712 Pfam, E= 2.5e-14 This domain belongs to the cysteine rich domains nkown to flank LRR.

LRRNT 724 751 Pfam, E= 1.1e-06 This domain belongs to the cysteine rich domains nkown to flank LRR.

LRR 753 775 Pfam, E= 3.4 LRR are proposed to be involved in protein-protein interactions.

LRR 776 799 Pfam, E= 0.074 LRR are proposed to be involved in protein-protein interactions.

LRR 800 823 Pfam, E= 0.014 LRR are proposed to be involved in protein-protein interactions.

LRR 824 847 Pfam, E= 0.00081 LRR are proposed to be involved in protein-protein interactions.

LRRCT 857 906 Pfam, E= 2.5e-16 This domain belongs to the cysteine rich domains nkown to flank LRR.

EGF
EGFCa 920 952 Pfam, E= 0.00019 The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.

EGF
EGFCa 959 993 Pfam, E= 4.5e-06 The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.

EGF
EGFCa 1000 1031 Pfam, E= 2.4e-08 The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.

EGF
EGFCa 1038 1071 Pfam, E= 4.8e-07 The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.

EGF
EGFCa 1078 1109 Pfam, E= 1e-07 The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.

EGF
EGFCa 1123 1154 Pfam, E= 3.1e-07 The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.

laminin_G 1186 1317 Pfam, E= 4.2e-24 The domain also known as ALPS domain is responsible for protein-protein interactions and self-aggregation of agrin, laminin, and perlecan.

EGF
EGFCa 1332 1364 Pfam, E= 0.0062 The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.

EGF
EGFCa 1372 1402 Pfam, E= 1.5e-05 The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.

EGF
EGFCa 1412 1443 Pfam, E= 0.00027 The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.

Cys_knot 1464 1522 Pfam, E= 0.00099 The Cys-knot is a dimerization motif building the C-terminus of various extracellular proteins.

1522

	TEM Sequence Analysis

name	from	to	source/E	description
Signalp	1	33
LRRNT	33	60	Pfam, E = 5e-09	This domain belongs to the cysteine rich domains nkown to flank LRR.
LRR	62	85	Pfam, E = 1.3	LRR are proposed to be involved in protein-protein interactions.
LRR	86	109	Pfam, E = 0.005	LRR are proposed to be involved in protein-protein interactions.
LRR	110	133	Pfam, E = 0.21	LRR are proposed to be involved in protein-protein interactions.
LRR	134	157	Pfam, E = 0.0041	LRR are proposed to be involved in protein-protein interactions.
LRR	158	181	Pfam, E= 0.5	LRR are proposed to be involved in protein-protein interactions.
LRR	182	205	Pfam, E= 0.75	LRR are proposed to be involved in protein-protein interactions.
LRR	206	227	Pfam, E= 9.3e+02	LRR are proposed to be involved in protein-protein interactions.
LRRCT	215	264	Pfam, E= 5e-17	This domain belongs to the cysteine rich domains nkown to flank LRR.
LRRNT	279	306	Pfam, E= 8.9e-07	This domain belongs to the cysteine rich domains nkown to flank LRR.
LRR	308	331	PfamFrag, E= 4.2	LRR are proposed to be involved in protein-protein interactions.
LRR	332	355	Pfam, E= 0.0012	LRR are proposed to be involved in protein-protein interactions.
LRR	356	379	Pfam, E= 0.046	LRR are proposed to be involved in protein-protein interactions.
LRR	380	403	PfamFrag, E= 3	LRR are proposed to be involved in protein-protein interactions.
LRR	404	427	Pfam, E= 0.15	involved in protein-protein interaction
LRRCT	437	486	Pfam, E= 3.3e-13	This domain belongs to the cysteine rich domains nkown to flank LRR.
LRRNT	504	531	Pfam, E= 9.7e-06	LRR flanking cysteine rich domains
LRR	558	581	Pfam, E= 0.064	LRR are proposed to be involved in protein-protein interactions.
LRR	582	605	Pfam, E= 0.62	LRR are proposed to be involved in protein-protein interactions.
LRR	606	629	Pfam, E= 2.5	LRR are proposed to be involved in protein-protein interactions.
LRR	630	653	Pfam, E= 0.67	LRR are proposed to be involved in protein-protein interactions.
LRRCT	663	712	Pfam, E= 2.5e-14	This domain belongs to the cysteine rich domains nkown to flank LRR.
LRRNT	724	751	Pfam, E= 1.1e-06	This domain belongs to the cysteine rich domains nkown to flank LRR.
LRR	753	775	Pfam, E= 3.4	LRR are proposed to be involved in protein-protein interactions.
LRR	776	799	Pfam, E= 0.074	LRR are proposed to be involved in protein-protein interactions.
LRR	800	823	Pfam, E= 0.014	LRR are proposed to be involved in protein-protein interactions.
LRR	824	847	Pfam, E= 0.00081	LRR are proposed to be involved in protein-protein interactions.
LRRCT	857	906	Pfam, E= 2.5e-16	This domain belongs to the cysteine rich domains nkown to flank LRR.
EGF EGFCa	920	952	Pfam, E= 0.00019	The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.
EGF EGFCa	959	993	Pfam, E= 4.5e-06	The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.
EGF EGFCa	1000	1031	Pfam, E= 2.4e-08	The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.
EGF EGFCa	1038	1071	Pfam, E= 4.8e-07	The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.
EGF EGFCa	1078	1109	Pfam, E= 1e-07	The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.
EGF EGFCa	1123	1154	Pfam, E= 3.1e-07	The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.
laminin_G	1186	1317	Pfam, E= 4.2e-24	The domain also known as ALPS domain is responsible for protein-protein interactions and self-aggregation of agrin, laminin, and perlecan.
EGF EGFCa	1332	1364	Pfam, E= 0.0062	The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.
EGF EGFCa	1372	1402	Pfam, E= 1.5e-05	The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.
EGF EGFCa	1412	1443	Pfam, E= 0.00027	The domain includes six cysteine residues which have been shown (in EGF) to be involved in disulfide bonds.
Cys_knot	1464	1522	Pfam, E= 0.00099	The Cys-knot is a dimerization motif building the C-terminus of various extracellular proteins.
1522

Remarks

	Remarks

CLASSIFICATION: Slit family (repellent axon guidance molecules).
DOMAIN ARCHITECTURE: A N-terminal signal peptide is followed by a four fold duplicated region each consisting of an amino flanking region, leucine rich repeats and a carboxyl flanking region (flank-LRR-flank domain). This is followed by 9 EGF motifs probably participating in extracellular protein-protein interactions. An laminin related sequence is separating the sixth and seventh EGF-like domains. The C terminal segment contains a cysteine-rich domain found in other secreted proteins.
FUNCTION: Slit proteins are known to provide a matrix for the migration axons, link multiple ligands and thereby mediate cell interactions and to be involved in differentiation processes (gut, heart). By similarity to Drosophila slit and by domain composition vertebrate slit proteins are proposed to be involved in mediating protein-protein and ECM-protein interactions in cell migration. As Northern blot analysis shows that human Slit-3 mRNAs is expressed predominantly in the thyroid, suggesting that the protein may participate in the formation and maintenance of the endocrine system.

Sequence Information

TEM TEM27

Reliability of Gen2Tag mapping

Cid->tag (Hs.57929) frequency(EST: 3 oriented):
: CATG-AAGGAAATGA=13/27
tem27: CATG-ACTACCATAA=6/27
Cid->tag (Hs.57929) frequency(EST: unoriented):
tem27: CATG-ACTACCATAA=11/22
: CATG-AAGGAAATGA=3/22

Analysis
BlastP against nr

Output Created by a Suite of Single Sequence Analysis Techniques

Protein Description

SEQ.SOURCE: gi|4049589|dbj|BAA35186.1| Slit-3 protein [Homo sapiens]

Protein Sequence

MAPGWAGVGAAVRARLALALALASVLSGPPAVACPTKCTCSAASVDCHGLGLRAVPRGIPRNAERLDLDR NNITRITKMDFAGLKNLRVLHLEDNQVSVIERGAFQDLKQLERLRLNKNKLQVLPELLFQSTPKLTRLDL SENQIQGIPRKAFRGITDVKNLQLDNNHISCIEDGAFRALRDLEILTLNNNNISRILVTSFNHMPKIRTL RLHSNHLYCDCHLAWLSDWLRQRRTVGQFTLCMAPVHLRGFNVADVQKKEYVCPAPHSEPPSCNANSISC PSPCTCSNNIVDCRGKGLMEIPANLPEGIVEIRLEQNSIKAIPAGAFTQYKKLKRIDISKNQISDIAPDA FQGLKSLTSLVLYGNKITEIAKGLFDGLVSLQLLLLNANKINCLRVNTFQDLQNLNLLSLYDNKLQTISK GLFAPLQSIQTLHLAQNPFVCDCHLKWLADYLQDNPIETSGARCSSPRRLANKRISQIKSKKFRCSGSED YRSRFSSECFMDLVCPEKCRCEGTIVDCSNQKLVRIPSHLPEYVTDLRLNDNEVSVLEATGIFKKLPNLR KINLSNNKIKEVREGAFDGAASVQELMLTGNQLETVHGRVFRGLSGLKTLMLRSNLIGCVSNDTFAGLSS VRLLSLYDNRITTITPGAFTTLVSLSTINLLSNPFNCNCHLAWLGKWLRKRRIVSGNPRCQKPFFLKEIP IQDVAIQDFTCDGNEESSCQLSPRCPEQCTCMETVVRCSNKGLRALPRGMPKDVTELYLEGNHLTAVPRE LSALRHLTLIDLSNNSISMLTNYTFSNMSHLSTLILSYNRLRCIPVHAFNGLRSLRVLTLHGNDISSVPE GSFNDLTSLSHLALGTNPLHCDCSLRWLSEWVKAGYKEPGIARCSSPEPMADRLLLTTPTHRFQCKGPVD INIVAKCNACLSSPCKNNGTCTQDPVELYRCACPYSYKGKDCTVPINTCIQNPCQHGGTCHLSDSHKDGF SCSCPLGFEGQRCEINPDDCEDNDCENNATCVDGINNYVCICPPNYTGELCDEVIDHCVPELNLCQHEAK CIPLDKGFSCECVPGYSGKLCETDNDDCVAHKCRHGAQCVDTINGYTCTCPQGFSGPFCEHPPPMVLLQT SPCDQYECQNGAQCIVVQQEPTCRCPPGFAGPRCEKLITVNFVGKDSYVELASAKVRPQANISLQVATDK DNGILLYKGDNDPLALELYQGHVRLVYDSLSSPPTTVYSVETVNDGQFHSVELVTLNQTLNLVVDKGTPK SLGKLQKQPAVGINSPLYLGGIPTSTGLSALRQGTDRPLGGFHGCIHEVRINNELQDFKALPPQSLGVSP GCKSCTVCKHGLCRSVEKDSVVCECRPGWTGPLCDQEARDPCLGHRCHHGKCVATGTSYMCKCAEGYGGD LCDNKNDSANACSAFKCHHGQCHISDQGEPYCLCQPGFSGEHCQQENPCLGQVVREVIRRQKGYASCATA SKVPIMECRGGCGPQCCQPTRSKRRKYVFQCTDGSSFVEEVERHLECGCLACS

SAGE-Tag CATG-ACTACCATAAC

EST/cluster Description

UNIGEN CLUSTER: Hs.57929 : slit (Drosophila) homolog 3

SEQ.SOURCE: continuos sequence based on gi|4049588|dbj|AB017169.1|AB017169 Slit-3 protein and
gi|3449301|dbj|AB011538.1|AB011538 partial MEGF5
MEGF5 mRNA extends the 3 UTR of Slit-3 mRNA

ANALYSIS: Blastn gen against Human dbEST
shows EST distribution along the TEM27.
Blastn gen against nr legitimates the contig formation from Slit-3 and MEGF5

REMARKS: From the position of the TEM27 tag relative to the proposed CDS end
it can be assumed that the TEM27 tag is corresponding to the CDS.
Usage of the alternative tag would result in < 200 bp UTR, which is unlikely.

MARKINGS: tem27 Tag in red
second frequent Hs.57929 Tag in darkmagenta
last nucleotides of the CDS marked in bold

EST/cluster Sequence

1 GCGCTCCGCACCTGGGCACTCCCAGCGATGCGCAGCGGGGCAGCGCCGGCCCCGCCGATG 61 GAGCTGCTGTTGCTGCCGCCGCCGCCGCCCGGAGCGCCCCGCTCCGCCCGCGCCCCGTGC 121 GCCTGAGCACCGAGCTCGCCCCTCCTCCGCGCTAACTCCGCCGCCCGCTCCCCAGGCCGC 181 CCGCGCTCCCCGCGCGCCTCCTCGGGCTCCACGCGTCTTGCCCCGCAGAGGCAGCCTCCT 241 CCAGGAGCGGGGCCCTGCACACCATGGCCCCCGGGTGGGCAGGGGTCGGCGCCGCCGTGC 301 GCGCCCGCCTGGCGCTGGCCTTGGCGCTGGCGAGCGTCCTGAGTGGGCCTCCAGCCGTCG 361 CCTGCCCCACCAAGTGTACCTGCTCCGCTGCCAGCGTGGACTGCCACGGGCTGGGCCTCC 421 GCGCGGTTCCTCGGGGCATCCCCCGCAACGCTGAGCGCCTTGACCTGGACAGAAATAATA 481 TCACCAGGATCACCAAGATGGACTTCGCTGGGCTCAAGAACCTCCGAGTCTTGCATCTGG 541 AAGACAACCAGGTCAGCGTCATCGAGAGAGGCGCCTTCCAGGACCTGAAGCAGCTAGAGC 601 GACTGCGCCTGAACAAGAATAAGCTGCAAGTCCTTCCAGAATTGCTTTTCCAGAGCACGC 661 CGAAGCTCACCAGACTAGATTTGAGTGAAAACCAGATCCAGGGGATCCCGAGGAAGGCGT 721 TCCGCGGCATCACCGATGTGAAGAACCTGCAACTGGACAACAACCACATCAGCTGCATTG 781 AAGATGGAGCCTTCCGAGCGCTGCGCGATTTGGAGATCCTTACCCTCAACAACAACAACA 841 TCAGTCGCATCCTGGTCACCAGCTTCAACCACATGCCGAAGATCCGAACTCTGCGCCTCC 901 ACTCCAACCACCTGTACTGCGACTGCCACCTGGCCTGGCTCTCGGATTGGCTGCGACAGC 961 GACGGACAGTTGGCCAGTTCACACTCTGCATGGCTCCTGTGCATTTGAGGGGCTTCAACG 1021 TGGCGGATGTGCAGAAGAAGGAGTACGTGTGCCCAGCCCCCCACTCGGAGCCCCCATCCT 1081 GCAATGCCAACTCCATCTCCTGCCCTTCGCCCTGCACGTGCAGCAATAACATCGTGGACT 1141 GTCGAGGAAAGGGCTTGATGGAGATTCCTGCCAACTTGCCGGAGGGCATCGTCGAAATAC 1201 GCCTAGAACAGAACTCCATCAAAGCCATCCCTGCAGGAGCCTTCACCCAGTACAAGAAAC 1261 TGAAGCGAATAGACATCAGCAAGAATCAGATATCGGATATTGCTCCAGATGCCTTCCAGG 1321 GCCTGAAATCACTCACATCGCTGGTCCTGTATGGGAACAAGATCACCGAGATTGCCAAGG 1381 GACTGTTTGATGGGCTGGTGTCCCTACAGCTGCTCCTCCTCAATGCCAACAAGATCAACT 1441 GCCTGCGGGTGAACACGTTTCAGGACCTGCAGAACCTCAACTTGCTCTCCCTGTATGACA 1501 ACAAGCTGCAGACCATCAGCAAGGGGCTCTTCGCCCCTCTGCAGTCCATCCAGACACTCC 1561 ACTTAGCCCAAAACCCATTTGTGTGCGACTGCCACTTGAAGTGGCTGGCCGACTACCTCC 1621 AGGACAACCCCATCGAGACAAGCGGGGCCCGCTGCAGCAGCCCGCGCCGACTCGCCAACA 1681 AGCGCATCAGCCAGATCAAGAGCAAGAAGTTCCGCTGCTCAGGCTCCGAGGATTACCGCA 1741 GCAGGTTCAGCAGCGAGTGCTTCATGGACCTCGTGTGCCCCGAGAAGTGTCGCTGTGAGG 1801 GCACGATTGTGGACTGCTCCAACCAGAAGCTGGTCCGCATCCCAAGCCACCTCCCTGAAT 1861 ATGTCACCGACCTGCGACTGAATGACAATGAGGTATCTGTTCTGGAGGCCACTGGCATCT 1921 TCAAGAAGTTGCCCAACCTGCGGAAAATAAATCTGAGTAACAATAAGATCAAGGAGGTGC 1981 GAGAGGGAGCTTTCGATGGAGCAGCCAGCGTGCAGGAGCTGATGCTGACAGGGAACCAGC 2041 TGGAGACCGTGCACGGGCGCGTGTTCCGTGGCCTCAGTGGCCTCAAAACCTTGATGCTGA 2101 GGAGTAACTTGATCGGCTGTGTGAGTAATGACACCTTTGCCGGCCTGAGTTCGGTGAGAC 2161 TGCTGTCCCTCTATGACAATCGGATCACCACCATCACCCCTGGGGCCTTCACCACGCTTG 2221 TCTCCCTGTCCACCATAAACCTCCTGTCCAACCCCTTCAACTGCAACTGCCACCTGGCCT 2281 GGCTCGGCAAGTGGTTGAGGAAGAGGCGGATCGTCAGTGGGAACCCTAGGTGCCAGAAGC 2341 CATTTTTCCTCAAGGAGATTCCCATCCAGGATGTGGCCATCCAGGACTTCACCTGTGATG 2401 GCAACGAGGAGAGTAGCTGCCAGCTGAGCCCGCGCTGCCCGGAGCAGTGCACCTGTATGG 2461 AGACAGTGGTGCGATGCAGCAACAAGGGGCTCCGCGCCCTCCCCAGAGGCATGCCCAAGG 2521 ATGTGACCGAGCTGTACCTGGAAGGAAACCACCTAACAGCCGTGCCCAGAGAGCTGTCCG 2581 CCCTCCGACACCTGACGCTTATTGACCTGAGCAACAACAGCATCAGCATGCTGACCAATT 2641 ACACCTTCAGTAACATGTCTCACCTCTCCACTCTGATCCTGAGCTACAACCGGCTGAGGT 2701 GCATCCCCGTCCACGCCTTCAACGGGCTGCGGTCCCTGCGAGTGCTAACCCTCCATGGCA 2761 ATGACATTTCCAGCGTTCCTGAAGGCTCCTTCAACGACCTCACATCTCTTTCCCATCTGG 2821 CGCTGGGAACCAACCCACTCCACTGTGACTGCAGTCTTCGGTGGCTGTCGGAGTGGGTGA 2881 AGGCGGGGTACAAGGAGCCTGGCATCGCCCGCTGCAGTAGCCCTGAGCCCATGGCTGACA 2941 GGCTCCTGCTCACCACCCCAACCCACCGCTTCCAGTGCAAAGGGCCAGTGGACATCAACA 3001 TTGTGGCCAAATGCAATGCCTGCCTCTCCAGCCCGTGCAAGAATAACGGGACATGCACCC 3061 AGGACCCTGTGGAGCTGTACCGCTGTGCCTGCCCCTACAGCTACAAGGGCAAGGACTGCA 3121 CTGTGCCCATCAACACCTGCATCCAGAACCCCTGTCAGCATGGAGGCACCTGCCACCTGA 3181 GTGACAGCCACAAGGATGGGTTCAGCTGCTCCTGCCCTCTGGGCTTTGAGGGGCAGCGGT 3241 GTGAGATCAACCCAGATGACTGTGAGGACAACGACTGCGAAAACAATGCCACCTGCGTGG 3301 ACGGGATCAACAACTACGTGTGTATCTGTCCGCCTAACTACACAGGTGAGCTATGCGACG 3361 AGGTGATTGACCACTGTGTGCCTGAGCTGAACCTCTGTCAGCATGAGGCCAAGTGCATCC 3421 CCCTGGACAAAGGATTCAGCTGCGAGTGTGTCCCTGGCTACAGCGGGAAGCTCTGTGAGA 3481 CAGACAATGATGACTGTGTGGCCCACAAGTGCCGCCACGGGGCCCAGTGCGTGGACACAA 3541 TCAATGGCTACACATGCACCTGCCCCCAGGGCTTCAGTGGACCCTTCTGTGAACACCCCC 3601 CACCCATGGTCCTACTGCAGACCAGCCCATGCGACCAGTACGAGTGCCAGAACGGGGCCC 3661 AGTGCATCGTGGTGCAGCAGGAGCCCACCTGCCGCTGCCCACCAGGTTTCGCCGGCCCCA 3721 GATGCGAGAAGCTCATCACTGTCAACTTCGTGGGCAAAGACTCCTACGTGGAACTGGCCT 3781 CCGCCAAGGTCCGACCCCAGGCCAACATCTCCCTGCAGGTGGCCACTGACAAGGACAACG 3841 GCATCCTTCTCTACAAAGGAGACAATGACCCCCTGGCACTGGAGCTGTACCAGGGCCACG 3901 TGCGGCTGGTCTATGACAGCCTGAGTTCCCCTCCAACCACAGTGTACAGTGTGGAGACAG 3961 TGAATGATGGGCAGTTTCACAGTGTGGAGCTGGTGACGCTAAACCAGACCCTGAACCTAG 4021 TAGTGGACAAAGGAACTCCAAAGAGCCTGGGGAAGCTCCAGAAGCAGCCAGCAGTGGGCA 4081 TCAACAGCCCCCTCTACCTTGGAGGCATCCCCACCTCCACCGGCCTCTCCGCCTTGCGCC 4141 AGGGCACGGACCGGCCTCTAGGCGGCTTCCACGGATGCATCCATGAGGTGCGCATCAACA 4201 ACGAGCTGCAGGACTTCAAGGCCCTCCCACCACAGTCCCTGGGGGTGTCACCAGGCTGCA 4261 AGTCCTGCACCGTGTGCAAGCACGGCCTGTGCCGCTCCGTGGAGAAGGACAGCGTGGTGT 4321 GCGAGTGCCGCCCAGGCTGGACCGGCCCACTCTGCGATCAGGAGGCCCGGGACCCCTGCC 4381 TCGGCCACAGATGCCACCATGGAAAATGTGTGGCAACTGGGACCTCATACATGTGCAAGT 4441 GTGCCGAGGGCTATGGAGGGGACTTGTGTGACAACAAGAATGACTCTGCCAATGCCTGCT 4501 CAGCCTTCAAGTGTCACCATGGGCAGTGCCACATCTCAGACCAAGGGGAGCCCTACTGCC 4561 TGTGCCAGCCCGGCTTTAGCGGCGAGCACTGCCAACAAGAGAATCCGTGCCTGGGACAAG 4621 TAGTCCGAGAGGTGATCCGCCGCCAGAAAGGTTATGCATCATGTGCCACAGCCTCCAAGG 4681 TGCCCATCATGGAATGTCGTGGGGGCTGTGGGCCCCAGTGCTGCCAGCCCACCCGCAGCA 4741 AGCGGCGGAAATACGTCTTCCAGTGCACGGACGGCTCCTCGTTTGTAGAAGAGGTGGAGA 4801 GACACTTAGAGTGCGGCTGCCTCGCGTGTTCCTAAGCCCCTGCCCGCCTGCCTGCCACCT 4861 CTCGGACTCCAGCTTGATGGAGTTGGGACAGCCATGTGGGACCCCCTGGTGATTCAGCAT 4921 GAAGGAAATGAAGCTGGAGAGGAAGGTAAAGAAGAAGAGAATATTAAGTATATTGTAAAA 4981 TAAACAAAAAATAGAACTTATTTTTATTATGGAAAGTGACTATTTTCATCTTTTATTATA 5041 TAAATATATTACACCATCTGCGTATATGTACCATATAGTGAGTTATTTTTACCAAGTTTT 5101 GTGTTGTGTATTTGTTGTGTTTTTAAAAATAGCTGTTTAAAAATTTAAGAAAAAAATAGA 5161 CTAATAAAAATGCTTTAAAACAAAAGGATAAGAATAAAGAATGATAGCCTGTCTGAGGAA 5221 GGAGGAAGATGTTTTCATGTTTATGAAACGGTATTATGTCGGCAGTAGACCAAGAGCTGC 5281 TCATTGAGATCAGAAAAAGGAATAAGAGGAAGAGAGAGAAGGAAAAGACCTTTGTTTCTT 5341 GTTTTTTAACTCCCTTTTATTTTTCCTCCCCTAAAATTACCCAGCTTTTCGGAGTCCTGG 5401 ATGTCAGTGCCCAAAATGCCCAGTTCTTCCAGGAAAAGCTGCTGAGCCCTGGCCTTCTCA 5461 GTCTCACTGCCACTCAAAAATATTGCTGTCCCTGTCTGTCCCAGACCCCCCTTCAGGGTA 5521 TCTGAACCCACTGGGGGACCCCTCTTCTCCTTCCTGGGTGGCCCTGGCTTCCGTATCTGA 5581 ACCCACTGGGGGACCCCTCTTCTCCTTCCTGGCTGGCCCTGGCTTCCAATCGAGGACTGA 5641 CTATTGAAGTCTGCTACAGGTGTCATTTGGAACTGTCTTACCAAATTTTAAAACAGCTGC 5701 TATTTTTCCTGCTCCTCCCCAGGAGAGGGGTCTTCCTAGAGGAGGCGAGGGAAGAGAATA 5761 TCATGGTGTCTCCTCAGGACCCATGCACTGGCCCTCTCTCCTCCTTCCAGGTAATTTTTC 5821 ATTGGAATGTATCCCAGTAGAGAAGGTAGTCAGCCCTTCTTGGAAGCGGAAGGCTGGGAG 5881 CCAAGTCAAGTCTGCCCACAGCGCTAGATGTCCAACTCTGGAAGGTTCTTGGAGGCTCTT 5941 GTTGTAAGACAGGCCTCTGCCACCTGATCCTCCAGGTCACCAGCATGACGATAGAGACTC 6001 CTTGCCCATCTGTGACACTTTCCAATGCATATCCAAACTTTACCTTATTTTATCTATGCA 6061 ACCCCTGCCTCCCTGGGAAGGATAAGGGAGTAGAGCTGGGTTCACTAAGAAGGAAGTTTA 6121 GGCCCTCACAGGCTCTGGAACTTGCCTTAAGCCACACACCAGATAAGTGGAGGAGCCAGA 6181 CCAGAAGTCCAGACCCAAAGCTTGAGATTCTTCCTCTAGAATGGGTGAGCACAGGTGATT 6241 CAGGCGGCTTAAATCCATCAGAGCAGCCCTGCCGGAAAAGGAAATAATATGATGTTTTTT 6301 CCTGCTCTTGTTCTGCCTTGCTCACTCCTTCTCCCTCCGCAGTATCTGGAAAGATTCTGG 6361 AGACCAGGGCTTATGCATCTAGGGAAAGTGACCAAGGGCAGCCTATCCAGCCTCTGCCTC 6421 CATTCCTGAAGGGGACTTCCCTGCCCCTGTTTCTTTCCATGTCTCTCCCTCCCTCACTCC 6481 CATTTGCCCCCTTCCACCCCATCAGGTTAGCCACATATCTTCCAGGGCTCAGCTGTTCAC 6541 ACCAACTCCCTGGCTCTTATCATCCATCCCTCCTTCCCCCAGGAGCTTCCACTGTAGGAG 6601 TTTCAGGGAGAAGAGTTTGGAATTCATTGGACCTTTCAGCCCTCAGGTTCCCTAGAGGAG 6661 CCTAGTTGATCTGTGAGTACCAATGGTGGGCCAAAGACGCAGGGAATAATGAAGGGAGAA 6721 AGAAAAGAAAGGAAGATGGAGGAAAACGAAGCAACTGGAAGAAGAAGGAAGGGATGGAGG 6781 GGATGAAGAGAAGGGAGAGAGGGATATAGCTGAGGAATTTATCTAAAAATGTGCATGTAA 6841 ATCTCCATTATGTTCCAGGTACTGTGCCTTATGATGGCTTTGTTTTTTGTTGTCATTAGA 6901 GACAAGGTCTTGCTTTGTCACCCAGGCTGGAGTAGAGTGGTTCGATCATAGCTCACCACA 6961 GCCTCAACCTCCTAGGCTCAAGCCATCTTCCTGCCTCAGTCTCCCAAAATGCTGGGATTA 7021 CAGGTGTGAGCCACTATGCTCAGCCTGTTTCAAACATTATTATAATAGCAGATTTATTTA 7081 GTACTTTATTATACATCAGATACCACTCTAATTGTGAAATAGATATATATTCATTTAATT 7141 ATTGAAACAACCATGTAGTTAAAACACTATTAACTCATTTTACAGTTGAGTAGACTGAGA 7201 CACAGAGAAGTTAAAGAACTTGCCCAAGAGTAAATGTCTAATAAACCGTAGAGCCAGGAT 7261 CTGGGCCCAGGCTGTCTGACTCCAGAACTTGCTCACTCAACCACTAAACCATCCTGCTTC 7321 TCATGGGAAAGAAACACATCCTGCCTTTGAGGATCCTACAGCCTGTGACAAAAACAGTCA 7381 TAAAAATGGACAATTGCCTTATTACACAAGGAGCTCTTAAGTGGCAATACAAGCAATGGA 7441 AGTGGCTGTCCAGAGGAGGGAACTTCTAGTCCTAGGTCTTTAAGGATGAATAGGAGTTTG 7501 CCAGAGTGAGAAAGGGAATTGAACTTTCCTGGGAGTGGCCTTTTAAAAAGCAATGAGATA 7561 TGGCCAGGCCTGGCTTGTTTGGGGAAGAGTCAAAATCTAGGGTGGCAAGAGTATGGGAAG 7621 CACACTGAGGAGCAGAGAGAAATGGGGTAGGTAGGAAGGTAGGGTTTTGACCACAAAGAG 7681 CTGTGCATGCTAAACTGGGCCACAGGTGCCAGCAGGGTTGTTTGAGGAAGGGAAGAGCAA 7741 GACAAGCTCTGGTTTAGGAAGAGAGCTGTGGCAGCATAAAGGCCTGAAAGAGGAGACAGA 7801 GCTGTCACCCAAAATGGACTTGAGAGCTCCCTGTGGTTTACTCTGTGGCTAGAAAACACT 7861 GCCGGCCAGATGGATCACAAATGTCTATGGTAGCTTAGAAGCTCTGCTCTTGAAGAGGAT 7921 CCTGGGATCTGCCCAACACCCTTCCCAACCTCCATTTCCCCATCCCCACCTCCATTGCCC 7981 CATCCCCCCTCTCCCCCTAGGCAGGTGGATCTGAGCCTTATCCCACCACCAATGCCCCTG 8041 CTAGCCTCTCCCCACCCAGCCCAGAGCCTACTCAGCCTGCCATCTCAAGAGCCCCACCGA 8101 GGGTCACTGGCTTCCTGGGAGGAGTCACCAGGCTGCCAGCTTTCCCTCTGCCTCCCCAAG 8161 GAACCTGAGACCTCCCTCTGCTCATCACCCTGGGCCCAATCCTGAATCCAGCCCCCATCA 8221 ACCAAGACAGCAAAAGGGCCAGGTCTGTCCCTTATAATTTTGAGCCTTCTCCCTCAAGTT 8281 TGGAAGCCCTGACTTTAAGAAATGCCAAATGCAAGGACCATTAAGAAAATTCTCCCCGAA 8341 ATGAGGCTCCTCTAACAAATGATGATTAAAACGCTCTCTCCTTGAGCAGTCACATTCTAG 8401 AAACAGGACATTCCATGAGGCAGGAAGAGTTCAGTTAATTTGCTCCTGAAAAAGTGTGGT 8461 TCAGTGTTTGTGTGGCAATGTACGTGGGCAGAAGAGGCCGCTCAAGCTGTGTCCCCCCTG 8521 AGCAGGATTCAGGAAAGGGAAAAGAAGTTCTCTTCAACTCAGCCAAGGGGCCGTACGATG 8581 GCCGATGAGATTATGTATTTAAAAGTTCTTTGTAAAGTGTAAACTAAAAACCTTAAATGT 8641 AAGATGCTGTTGTTATTATTACTGTTGTTGTTGCTGTTATGGACATGCCAAAAGGCCCTT 8701 GTTAGAAGACAGTTTTGCCTTTTCAATCTCATAGCAAGGAACTCAAGTCTGATGCTTCAA 8761 AAAGATGAGAAGAAGGGCAAGAAGAGGGATAACTCCCAAGCTCAGAGGGAAAAAAAAGGC 8821 GGGGGAAAAGAGCCCCAGGGTGACCTTCAGGAAAGGCCAGGACCAGGATGATCTAACCTT 8881 TCCCTTCACCAGAAACAAAGCTATTGCCAGACTGAACCCTAAAGTCAAGCAGTCACCCAC 8941 TGCCTTTGCTGGGAGCAGAAGCCCATAGCAACAAGTGACCTGCCCCTCAGACTCAAGATC 9001 CCAGATACCAGAGCTGGAGGAGTCATAGGGCATTACTGGTAGGCAGGAAAACTGAGGGTC 9061 GAACAAATGGAAGAATGCGGTGATCATAGACCAAAGACACACAGATAATTAACCCCATGT 9121 GTCCACCCAGGCCAAAGTTCTTCCTGCTACCCCACAGTGGATGTCCAGGCAGATGGTCCC 9181 CACATGATGGGGAAGCAGAGGGCATAGTGTGGTTTTGTGGGACTTGTTCATGTTTTGTAG 9241 TGTGGGCTCAACAGTGCCAAAGGAAACACTAGGGAAAAGTTGGTGAAACATGCCAGCTAG 9301 CAGGACCAGTAAAGGCATAATCAGGCATTTGGCAAAGCTTGCTTTTCTAATTCAATGATA 9361 GGTTCTAATAGGAAATTTTTGAAGATTTTTTAAAACAATGTTATAGTGGCACTTCCCCAG 9421 TATGGAATAAATAACATGCATTCTTTTTTCAATATACTGTCATATTCAGATGTCATTAAA 9481 ATAAATGGATGAGTCACAGAGGAGCTATCAGATGCTCTCATGACTACCATAACTC

Genomic Sequence Description

Genomic Sequence

	Sequence Information

Literature

	Literature

Pubmed: 10864956
J Neurosci: 20/13/4983 Slit inhibition of retinal axon growth and its role in retinal axon pathfinding and innervation patterns in the diencephalon.
Ringstedt T, Braisted JE, Brose K, Kidd T, Goodman C, Tessier-Lavigne M, OLeary DD.
J Neurosci. 2000 Jul 1;20(13):4983-91.

Pubmed: 10842075
Mechanisms of Development94/1-2 Expression of the vertebrate Slit gene family and their putative receptors, the Robo genes, in the developing murine kidney.
Piper M, Georgas K, Yamada T, Little M.
Mech Dev. 2000 Jun;94(1-2):213-7.

Pubmed: 9813312 Cloning and expressions of three mammalian homologues of Drosophila slit suggest possible roles for Slit in the formation andmaintenance of the nervous system.
Itoh A, Miyabayashi T, Ohno M, Sakano S.
Brain Res Mol Brain Res. 1998 Nov 20;62(2):175-86.

PubMed: 9432001 Localization of heparin binding activity in recombinant laminin G domain.
Sung U, ORear JJ, Yurchenco PD.
Eur J Biochem. 1997 Nov 15;250(1):138-43.

Pubmed: 8490958 A structural superfamily of growth factors containing a cystine knot motif.
McDonald NQ, Hendrickson WA
Cell 1993 May 7;73(3):421-4

FAQ

Pubmed: 10864956 J Neurosci: 20/13/4983	Slit inhibition of retinal axon growth and its role in retinal axon pathfinding and innervation patterns in the diencephalon. Ringstedt T, Braisted JE, Brose K, Kidd T, Goodman C, Tessier-Lavigne M, OLeary DD. J Neurosci. 2000 Jul 1;20(13):4983-91.
Pubmed: 10842075 Mechanisms of Development94/1-2	Expression of the vertebrate Slit gene family and their putative receptors, the Robo genes, in the developing murine kidney. Piper M, Georgas K, Yamada T, Little M. Mech Dev. 2000 Jun;94(1-2):213-7.
Pubmed: 9813312	Cloning and expressions of three mammalian homologues of Drosophila slit suggest possible roles for Slit in the formation andmaintenance of the nervous system. Itoh A, Miyabayashi T, Ohno M, Sakano S. Brain Res Mol Brain Res. 1998 Nov 20;62(2):175-86.
PubMed: 9432001	Localization of heparin binding activity in recombinant laminin G domain. Sung U, ORear JJ, Yurchenco PD. Eur J Biochem. 1997 Nov 15;250(1):138-43.
Pubmed: 8490958	A structural superfamily of growth factors containing a cystine knot motif. McDonald NQ, Hendrickson WA Cell 1993 May 7;73(3):421-4