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Angiogenesis

List of -TEMs -PEMs -NEMs

TEMs TEM1 TEM2 TEM3 TEM4 TEM5 TEM6 TEM7 TEM8 TEM9 TEM10 TEM11 TEM12 TEM13 TEM14 TEM15 TEM16 TEM17 TEM18 TEM19 TEM20 TEM21_1 TEM21_2 TEM22 TEM23 TEM24 TEM25 TEM26 TEM27 TEM28 TEM29 TEM30 TEM31_1 TEM31_2 TEM32 TEM33 TEM34 TEM35 TEM36 TEM37 TEM38 TEM39 TEM40 TEM41 TEM42 TEM43 TEM44 TEM45 TEM46

Summary -Overview of TEMs -extracellular TEMs -intrac. & membrane TEMs -TEM tissue distribution

Supplementary -SAGE -Seq.analysis Methods

FAQ

Tumor Endothelial Marker Report: TEM9 (7tm_2 receptor)

	TEM domain structure

	TEM Sequence Analysis

name	from	to	source/E	description
Signalp	1	27	SignalP
LRRNT	29	72	Pfam, E= 44	The LLRNT domain is a cystein-rich domain that is found to border LRR-repeats. Due to the cystein conservation the hit is considered despite of the unreliable scoring.
LRR	75	99	PfamFrag, E=0.69	LRRs are usually involved in protein-protein interactions.
LRR	100	123	Pfam, E=309e+02	LRRs are usually involved in protein-protein interactions and cellular adhesion.
LRR	124	147	Pfam, E=0.0037	LRRs are usually involved in protein-protein interactions and cellular adhesion.
LRR	148	171	Pfam, E=0.032	LRRs are usually involved in protein-protein interactions and cellular adhesion.
LRRCT	183	233	Pfam, E=1.9e-08	The LLRCT domain is a cystein-rich domain that is found to border LRR-repeats.
ig	246	339	PfamFrag, E=0.77 SMART, E=3.49e-03	Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.
HormR	342	419	SMART, E=4.57e-02	The HormR domain is found in peptide hormone receptors and is a proposed ligand binding domain.
unknown	419	510	predator	The region is highly helical (>85 %) and contains a apolar span
unknown	510	699	predator	The region is predicted to be mostly unstructured (71 % coil), contains a LCR(P) from 556 to 580. Two apolar regions are predicted by toppred2 to be certain TM spans. The prediction of TM regions is not considered due to missing helix predictions in this region, the fact that the following GPS domain is supposed to be extracellular in proteins with various membrane topology (1-, 7-, 10TM), and due to known topology of proteins of the secretin family homologous in this region (PsiBlast, TEM9: HormR-GPS-7tm_2).
GPS	699	751	PFAM, E = 0.004	The GPS domain can be found N-terminally of the 7 tm region in various secretin receptors. The domain in TEM9 contains one of the two putative di-S bridges found in most of the GPS domains. Functionally it could be a ligand binding and/or cleavage domain based on its similarity to G-protein-coupled receptor proteolytic site domain.
7tm_2	762	1069	PFAMsanger, E = 0.01	The 7tm region defines TEM9 as a secretin family proteins. Characteristic residues were found to be conserved in TM segments, with the exception of TM6 (eg GxP motif in TM4). Most characterized receptors of the secretin family are coupled to G-proteins which activate both adenylyl cyclase and the phosphatidylinositol-calcium pathway.
cytoplasmic	1069	1331		The cytoplasmic sequence contains two vicinal cysteins typical for the GPCR-palmitoylation site. It is longer than in other G-protein-coupled receptors and shows no significant homologies. The composition is notable, as the region is highly LCR -rich: proline-, alanine-rich, and LCR with a positively charged cluster. Highly proline-rich regions usually serve as binding sites for Src homology (SH3) domains and other protein modules. A class II consensus-SH3 binding motif (XPpXPXR, p proline-preferred, X non-conserved residue) can be found (PHAPPR).
1331

	Remarks

• THE PROTEIN SEQUENCE IS PRESUMPTIVE: A CHIMERA containing N-terminal most of the sequence predicted from the Ensemble genomic sequence and continued in the C-terminal by KIAA1531, which is EST derived and thus potentially more reliable.

• CLASSIFICATION: Secretin family G-protein-coupled receptors (GPCRs). Seven-span transmembrane (7-TM) receptors form the largest superfamily of transmembrane proteins in nature with nearly 2000 members.

• DOMAIN ARCHITECTURE: The N-terminal extracellular part functions in ligand binding and consists of a LRR region followed by an Ig, a peptide hormone receptor domain (HormR) and a GPCR proteolytic site (GPS) domain. The transmembrane region is homologous to the transmembrane region of other secretin-family serpentine receptors. The region including the HormR, GPS, seven-pass transmembrane domain combination is weekly conserved in a subfamily of G-protein-coupled receptors (GPCRs) including the latrophilin-like receptors, protocadherin and BAI. The beginning of the cytoplasmic region contains two vicinal cysteins (1234, 1235) typical for the GPCR-palmitoylation site. The cytoplasmatic sequence is longer than in other G-protein-coupled receptors and shows no significant homology, but shows LCR accumulation. Highly proline-rich regions usually serve as binding sites for Src homology (SH3) domains and other protein modules. A class II consensus-SH3 binding motif(XPpXPXR, p proline-preferred, X non-conserved residue) also found in dynamin can be observed at position 1267-1273 (XPXXPXR). P2, P5 and R7 of this motif have been shown to contribute to SH3 binding affinity. Whether SH3-containing proteins interact with TEM9 remains uncertain.

• HOMOLOGUES:
  Drosophila CG15744 [AAF48247.1] (Identity = 22%). Homology in parts of the extracellular region and down to the seventransmembrane region.
  Further homologs in the extracellular region are clustering in two regions:
  • TEM9: 1-339aa containing LRR+LRR+LRR+LRRCT+Ig. View the PsiBlast (E=0.002) search to get an overview of proteins with similarities in this region.
    
  • TEM9: 342-1069aa containing HormR-GPS-7tm_2. View the PsiBlast (E=0.002) search to get an overview of proteins with similarities in this region.
    

• FUNCTION: The unusual structure of the TEM9 protein suggests it could function in both cell adhesion and/or cell signaling pathways.

  RESIDUE 1-339 LIGAND-BINDING DOMAIN:
  

     For a support of the following speculations view the PsiBlast search (E=0.002) performed with the TEM9 region 1-625aa that contains the following domains: LRR-LRR-LRR-LRRCT-Ig.
     The region 1-339 containing LRR+LRR+LRR+LRRCT+Ig is most likely to interact with glycoprotein ligands. In a variety of organisms from yeast to humans, members of the leucine-rich repeat (LRR) family, in which one repeat consists of 24 amino acids and leucine residues appear regularly, have been shown to be involved in protein-protein interactions. As the sequence prediction based on the genomic sequence has not been verified by EST analysis it has to be analyzed with caution.
     Over the length from this region a distant similarity to the extracellular N-terminus of mouse LIG-1 (ref|NP_032403.1), a region containing 15 leucine-rich repeats, can be observed. A function of LIG-1 as a cell type-specific adhesion molecule or receptor at the glial cell surface, has been proposed.

  RESIDUE 342-1069 LIGAND-BINDING AND RECEPTOR REGULATION BY SIMILARITY: The region is composed of HormR-linker-GPS-7tm_2.
  

  For a support of the following speculations view the PsiBlast search (E=0.002) performed with the TEM9 region 501-1300aa that contains the following domains: HormR-GPS-7tm_2.
     The arrangment of HormR-linker-GPS-7tm_2 seems to characterize a subfamily of secretin GPCRs, containing several proteins with otherwise divergent domainarchitecture in the distal N-terminal region.
     The HormR motif is also found in "classical" secretin receptors (vasoactive intestinal peptide receptor, secretin receptor, glucagon-like peptide receptor) but in close proximity to the transmembrane core and a GPS domain being absent.
     The GPS domain has been implicated in receptor regulation in latrophilin/CL-1 proteins as the receptor is cleaved at the Leu-Thr peptide bond of the HLTN site. The motif can also be found in other plasma-membrane independently of the HormR domain, where it is again found in membrane proximity (PKD1,PKDREJ).
     The subfamily of secretin GPCRs characterized by the arrangment of HormR-linker-GPS-7tm_2 can be further subdivided by the domains found in the distal N-terminus:
  • Latrohpilin-like receptors with an N-terminally located Olfactomedin domain.
  • Protocadherin adhesion molecules with N-terminally located multiple cadherin, EGF, lamG domains.
  • TEM9 with N-terminally located LRR and Ig domains is most closely related to the protocadherins for which it is known that the ectodomains of each member of the protocadherin gene clusters are present in one large exon.
  • BAI (brain-specific angiogenesis inhibitor)-like with N-terminally located Thrombospondin type 1 repeats for TGF-beta binding.
     The HormR/GPS combination of TEM9, latrophilin-like receptors, protocadherin and BAI have a common origin as can be seen by the PsiBlast sarch preformed with Tem9 501-1300aa.

  GPS AS A CLEAVAGE SITE: The cleavage site in the GPS domain has been alocated in latrophilin CL-1,with the region around the putative cleavage site (HLGN) being most highly conserved. Several proteins containing this cystein-rich region have been shown to be cleaved :CL-1, 2, 3, CD97, making it likely that TEM9 could be processed as well. The subunits resulting from the CL-1 cleavage have been shown to remain associated. From the four conserved cystein residues mostly found in GPS domains only two cysteins are conserved in Tem9, human PKD1 and in C.elegans F31D5.4, F31D5.5.

  • SIGNALING: It can be hypothesized that TEM9 functions as a receptor or coreceptor. No mechanism of action has been shown for closely related receptors. Flamingo studies in drosophila md neurons raised the possibility that the receptor signaling pathway might involve or interact with RhoA. Many proteins of the secretin receptor family have been shown to increase the intracellular levels of cAMP and/or inositol phosphates upon ligand binding.

  • SIDE-INFO ON HOMOLOGS:
    • Drosophila Stan(Flamingo) protein shows a similar domain organization regarding the HormR-GPS-7tm_2 region but differs in the distal N-terminus where it has a typical nine cadherin motifs, four EGF-like motifs, and two laminin G motifs. Thus, it is proposed to be a seven-transmembrane cell-adhesion molecule, being localized to cell-cell boundaries in both the SOPs and their surrounding epithelial cells. Stan controls planar cellular polarity. It has been suggested that in tissue polarity Stan functions primarily in signaling/signal transduction. Flamingo studies in Drosophila neurons raised the possibility that the receptor signaling pathway might involve or interact with RhoA.
    • BAI1 interacts via its C-terminus with BAIAP2 BAI-associated proteins. And the formation of a GTP-Rho-mDia1-BAIAP2 termary complex has been shown recently. The cytoplasmic domain of BAI1 that is involved in BAIAP2 binding is not conserved among latrophilins, BAI, protocadherins and TEM9, but has common general features as it is unusually long for GPCRs and rich in LCRs.

	Sequence Information

TEM	TEM9
Reliability of Gen2Tag mapping	Cid->tag (Hs.17270) frequency: tem9: CATG-TTTTTAAGAA=67/74 (EST: oriented)
Analysis	BlastP against nr Output Created by a Suite of Single Sequence Analysis Techniques
Protein Description	SEQ.SOURCE: gi|17511205|ref|NP_116166.6| tumor endothelial marker 5 precursor REMARKS: The KIAA1531 protein was elongated N-terminally by the predicted protein sequence AP000501.00001.82992.
Protein Sequence	MRGAPARLLLPLLPWLLLLLAPEARGAPGCPLSIRSCKCSGERPKGLSGGVPGPARRRVVCSGGDLPEPP EPGLLPNGTVTLLLSNNKITGLRNGSFLGLSLLEKLDLRNNIISTVQPGAFLGLGELKRLDLSNNRIGCL TSETFQGLPRLLRLNISGNIFSSLQPGVFDELPALKVVDLGTEFLTCDCHLRWLLPWAQNRSLQLSEHTL CAYPSALHAQALGSLQEAQLCCEGALELHTHHLIPSLRQVVFQGDRLPFQCSASYLGNDTRIRWYHNRAP VEGDEQAGILLAESLIHDCTFITSELTLSHIGVWASGEWECTVSMAQGNASKKVEIVVLETSASYCPAER VANNRGDFRWPRTLAGITAYQSCLQYPFTSVPLGGGAPGTRASRRCDRAGRWEPGDYSHCLYTNDITRVL YTFVLMPINASNALTLAHQLRVYTAEAASFSDMMDVVYVAQMIQKFLGYVDQIKELVEVMVDMASNLMLV DEHLLWLAQREDKACSRIVGALERIGGAALSPHAQHISVNARNVALEAYLIKPHSYVGLTCTAFQRREGG VPGTRPGSPGQNPPPEPEPPADQQLRFRCTTGRPNVSLSSFHIKNSVALASIQLPPSLFSSLPAALAPPV PPDCTLQLLVFRNGRLFHSHSNTSRPGAAGPGKRRGVATPVIFAGTSGCGVGNLTEPVAVSLRHWAEGAE PVAAWWSQEGPGEAGGWTSEGCQLRSSQPNVSALHCQHLGNVAVLMELSAFPREVGGAGAGLHPVVYPCT ALLLLCLFATIITYILNHSSIRVSRKGWHMLLNLCFHIAMTSAVFAGGITLTNYQMVCQAVGITLHYSSL STLLWMGVKARVLHKELTWRAPPPQEGDPALPTPSPMLRFYLIAGGIPLIICGITAAVNIHNYRDHSPYC WLVWRPSLGAFYIPVALILLITWIYFLCAGLRLRGPLAQNPKAGNSRASLEAGEELRGSTRLRGSGPLLS DSGSLLATGSARVGTPGPPEDGDSLYSPGVQLGALVTTHFLYLAMWACGALAVSQRWLPRVVCSCLYGVA ASALGLFVFTHHCARRRDVRASWRACCPPASPAAPHAPPRALPAAAEDGSPVFGEGPPSLKSSPSGSSGH PLALGPCKLTNLQLAQSQVCEAGAAAGGEGEPEPAGTRGNLAHRHPNNVHHGRRAHKSRAKGHRAGEACG KNRLKALRGGAAGALELLSSESGSLHNSPTDSYLGSSRNSPGAGLQLEGEPMLTPSEGSDTSAAPLSEAG RAGQRRSASRDSLKGGGALEKESHRRSYPLNAASLNGAPKGGKYDDVTLMGAEVASGGCMKTGLWKSETT V
SAGE-Tag	CATG-TTTTTAAGAAC
EST/cluster Description	UNIGEN CLUSTER: Hs.17270 : DKFZP434C211 protein SEQ.SOURCE: gi|7959328|dbj|AB040964.1|AB040964 Homo sapiens mRNA for KIAA1531 protein, partial cds MARKINGS: TEM9 Tag in red first Poly-A-signal following the Tag in bold
EST/cluster Sequence	ACCACCTCATCCCGTCCCTACGCCAAGTGGTGTTCCAGGGGGATCGGCTGCCCTTCCAGTGCTCTGCCAG CTACCTGGGCAACGACACCCGCATCCGCTGGTACCACAACCGAGCCCCTGTGGAGGGTGATGAGCAGGCG GGCATCCTCCTGGCCGAGAGCCTCATCCACGACTGCACCTTCATCACCAGTGAGCTGACGCTGTCTCACA TCGGCGTGTGGGCCTCAGGCGAGTGGGAGTGCACCGTGTCCATGGCCCAAGGCAACGCCAGCAAGAAGGT GGAGATCGTGGTGCTGGAGACCTCTGCCTCCTACTGCCCCGCCGAGCGTGTTGCCAACAACCGCGGGGAC TTCAGGTGGCCCCGAACTCTGGCTGGCATCACAGCCTACCAGTCCTGCCTGCAGTATCCCTTCACCTCAG TGCCCCTGGGCGGGGGTGCCCCGGGCACCCGAGCCTCCCGCCGGTGTGACCGTGCCGGCCGCTGGGAGCC AGGGGACTACTCCCACTGTCTCTACACCAACGACATCACCAGGGTGCTGTACACCTTCGTGCTGATGCCC ATCAATGCCTCCAATGCGCTGACCCTGGCTCACCAGCTGCGCGTGTACACAGCCGAGGCCGCTAGCTTTT CAGACATGATGGATGTAGTCTATGTGGCTCAGATGATCCAGAAATTTTTGGGTTATGTCGACCAGATCAA AGAGCTGGTAGAGGTGATGGTGGACATGGCCAGCAACCTGATGCTGGTGGACGAGCACCTGCTGTGGCTG GCCCAGCGCGAGGACAAGGCCTGCAGCCGCATCGTGGGTGCCCTGGAGCGCATTGGGGGGGCCGCCCTCA GCCCCCATGCCCAGCACATCTCAGTGAATGCGAGGAACGTGGCATTGGAGGCCTACCTCATCAAGCCGCA CAGCTACGTGGGCCTGACCTGCACAGCCTTCCAGAGGAGGGAGGGAGGGGTGCCGGGCACACGGCCAGGA AGCCCTGGCCAGAACCCCCCACCTGAGCCCGAGCCCCCAGCTGACCAGCAGCTCCGCTTCCGCTGCACCA CCGGGAGGCCCAATGTTTCTCTGTCGTCCTTCCACATCAAGAACAGCGTGGCCCTGGCCTCCATCCAGCT GCCCCCGAGTCTATTCTCATCCCTTCCGGCTGCCCTGGCTCCCCCGGTGCCCCCAGACTGCACCCTGCAA CTGCTCGTCTTCCGAAATGGCCGCCTCTTCCACAGCCACAGCAACACCTCCCGCCCTGGAGCTGCTGGGC CTGGCAAGAGGCGTGGCGTGGCCACCCCCGTCATCTTCGCAGGAACCAGTGGCTGTGGCGTGGGAAACCT GACAGAGCCAGTGGCCGTTTCGCTGCGGCACTGGGCTGAGGGAGCCGAACCTGTGGCCGCTTGGTGGAGC CAGGAGGGGCCCGGGGAGGCTGGGGGCTGGACCTCGGAGGGCTGCCAGCTCCGCTCCAGCCAGCCCAATG TCAGCGCCCTGCACTGCCAGCACTTGGGCAATGTGGCCGTGCTCATGGAGCTGAGCGCCTTTCCCAGGGA GGTGGGGGGCGCCGGGGCAGGGCTGCACCCCGTGGTATACCCCTGCACGGCCTTGCTGCTGCTCTGCCTC TTCGCCACCATCATCACCTACATCCTCAACCACAGCTCCATCCGTGTGTCCCGGAAAGGCTGGCACATGC TGCTGAACTTGTGCTTCCACATAGCCATGACCTCTGCTGTCTTTGCGGGGGGCATCACACTCACCAACTA CCAGATGGTCTGCCAGGCGGTGGGCATCACCCTGCACTACTCCTCCCTATCCACGCTGCTCTGGATGGGC GTGAAGGCGCGAGTGCTCCATAAGGAGCTCACCTGGAGGGCACCCCCTCCGCAAGAAGGGGACCCCGCTC TGCCTACTCCCAGTCCTATGCTCCGCTGCTGGCTGGTGTGGCGTCCAAGCCTTGGCGCCTTCTACATCCC TGTGGCTTTGATTCTGCTCATCACCTGGATCTATTTCCTGTGCGCCGGGCTACGCTTACGGGGTCCTCTG GCACAGAACCCCAAGGCGGGCAACAGCAGGGCCTCCCTGGAGGCAGGGGAGGAGCTGAGGGGTTCCACCA GGCTCAGGGGCAGCGGCCCCCTCCTGAGTGACTCAGGTTCCCTTCTTGCTACTGGGAGCGCGCGAGTGGG GACGCCCGGGCCCCCGGAGGATGGTGACAGCCTCTATTCTCCGGGAGTCCAGCTAGGGGCGCTGGTGACC ACGCACTTCCTGTACTTGGCCATGTGGGCCTGCGGGGCTCTGGCAGTGTCCCAGCGCTGGCTGCCCCGGG TGGTGTGCAGCTGCTTGTACGGGGTGGCAGCCTCCGCCCTGGGCCTCTTCGTCTTCACTCACCACTGTGC CAGGCGGAGGGACGTGAGAGCCTCGTGGCGCGCCTGCTGCCCCCCTGCCTCTCCCGCGGCCCCCCATGCC CCGCCCCGGGCCCTGCCCGCCGCCGCAGAGGACGGTTCCCCGGTGTTCGGGGAGGGGCCCCCCTCCCTCA AGTCCTCCCCAAGCGGCAGCAGCGGCCATCCGCTGGCTCTGGGCCCCTGCAAGCTCACCAACCTGCAGCT GGCCCAGAGTCAGGTGTGCGAGGCGGGGGCGGCGGCCGGCGGGGAAGGAGAGCCGGAGCCGGCGGGCACC CGGGGAAACCTCGCCCACCGCCACCCCAACAACGTGCACCACGGGCGTCGGGCGCACAAGAGCCGGGCCA AGGGACACCGCGCGGGGGAGGCCTGCGGCAAGAACCGGCTCAAGGCCCTGCGCGGGGGCGCGGCGGGGGC GCTGGAGCTGCTGTCCAGCGAGAGCGGTAGTCTGCACAACAGCCCCACCGACAGCTACCTGGGCAGCAGC CGCAACAGCCCGGGCGCCGGCCTGCAGCTGGAAGGCGAGCCCATGCTCACGCCGTCCGAGGGCAGCGACA CCAGCGCCGCGCCGCTTTCTGAGGCGGGCCGGGCAGGCCAGCGCCGCAGCGCCAGCCGCGACAGTCTCAA GGGCGGCGGCGCGCTGGAGAAGGAGAGCCATCGCCGCTCGTACCCGCTCAACGCCGCCAGCCTAAACGGC GCCCCCAAGGGGGGCAAGTACGACGACGTCACCCTGATGGGCGCGGAGGTAGCCAGCGGCGGCTGCATGA AGACCGGACTCTGGAAGAGCGAAACTACCGTCTAAGGTGGGGCGGGCGACGCGGTAGACGGGCTGGCCAC GCGGCTCGTTCCCCCGCTCCTCGGGGCCCTCCAAGGTGTCTCCGTAGTCAGCAGGTTGGAGGCAGAGGAG CCGATGGCTGGAGGAAGCCCACAGGCGGATGTTCCCCACTTGCCTAGAGGGCATCCCTCTGGGGTAGCGA CAGACAATCCCAGAAACACGCATAATACATTTCCGTCCAGCCCGGGGCAGTCTGACTGTCGGTGCCCTCC CAGGAACGGGGAAGGCCTCCGTCTGTGTGAAAGGGCACAGCACATCCCAGGTGCACCCTCCCCAAGTACT CCCACCCCGCCTACTGTCCATGCGGCCTCACTGGGGGCCATCAGCCTCACCAGCAAAGCAGAGATGAGAG CGTGGGAACTGTGTTCTTTCCTCCCTGCCCTCTACTGATTTCAGCCCAGCCCCTGCCTAGATCCTAGGTC CCTTTTCCTCCCGAGTTTGGCTGGCACGAGAGCTAGCCCAGCACATGAAGCAGGTGATGTTAAGTCACAA GGTGCTGCTTTTCAGATCCACTATGCAAGAGGGGAGGGTGGGGCCACGTGAAAGGCAGCTCTAGACATCA ACCAGTCCTGGGGGAGGGGAGTGGGAACCGGGCACAACTAGGAACAATGCCACCATTCCCACAGGAGTGG TACTTAAACCAGACAGCAGGGTTCAGAGGTGGCACACCGGGACAAAGCTGAGGCCCTGCACCTCAACAGC TGACTGCCAGGTGCCTGTGGGTGAACTGAGGGGAGTAGAGGGAGAGGGCAGGTGGAACTGGGGCAGAATC TAGTCATGCCCTAAAGCTAGTCCTGTAAACAATGGTGCCCCAGAAAGCTGCAGGTGGTGTTTGGAGAAGC AGTTACTTTTCAGTTACAAGACCCATCTCCCTAGTCTCAGCCTTACAACACCACGGGACTAAGGAAGAGC ACTTCCTTGCCTCCGTAAGGCCAGAGGAAGAACCATCCCAATCATTTGATCTCCAGCTCCACAGTAGAGA GAAACCTACAAAATGTCAAACCAGCTTCCCGACTCCCAGGAGCTCAAGCCAAGCCCAGAGGCAGTGGCTG GGGTCCCTGCAGGTCATGAGGGGCCTATGCCTTTACTCCTTTTAAACACCAGCACCCGTCTTTTCCCCAA CCTAAAACCAACCACCAGCATTTCACTACAGGACCAAATGGAAACCGAGGGAACCCTGGGTCTTGGGAAG AACAACAGGAAACCAAGGTCTGACCTAGGGTTCCCTCCCAGTCTTCACATCACTCTGGCCTCATCACCAA GGTGACAGAGGACACAGGGGAGGGGGAAAACCCACACACACTCCTTGGAATGGGTCCTGTTATTTATGCT TGCTGCACAGACATATTAGAAGAAAAAAAAAAGCTTTGTATTATTCTTCCACATATGCTGGCTGCTGTTT ACACACCCTGCCAATGCCTTAGCACTGGAGAGCTTTTTGCAATATGCTGGGGAAAGGGGAGGGAGGGAAT GAAAGTGCCAAAGAAAACATGTTTTTAAGAACTCGGGTTTTATACAATAGAATGTTTTCTAGCAGATGCC TCTTGTTTTAATATATTAAAATTTTGCAAAGCCCTTTG
Genomic Sequence Description	SEQ.SOURCE: gi|5926688|dbj|AP000501.1|AP000501 Homo sapiens genomic DNA, chromosome 8p11.2
Genomic Sequence

	Literature

PubMed:99121098	Structural requirements for alpha-latrotoxin binding and alpha-latrotoxin-stimulated secretion. A study with calcium-independent receptor of alpha-latrotoxin (CIRL) deletion mutants. Krasnoperov V, Bittner MA, Holz RW, Chepurny O, Petrenko AG. J Biol Chem 1999 Feb 5;274(6):3590-6
PubMed:9904765	alpha-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual family of ubiquitous G-protein-linked receptors. G-protein coupling not required for triggering exocytosis. Sugita S, Ichtchenko K, Khvotchev M, Sudhof TC. J Biol Chem 1998 Dec 4;273(49):32715-24
PubMed:10469603	A latrophilin/CL-1-like GPS domain in polycystin-1. Ponting CP, Hofmann K, Bork P. Curr Biol. 1999 Aug 26;9(16):R585-8.
PubMed:11086986	Control of dendritic field formation in Drosophila: the roles of flamingo and competition between homologous neurons. Gao FB, Kohwi M, Brenman JE, Jan LY, Jan YN. Neuron. 2000 Oct;28(1):91-101.
PubMed:10556066	The Drosophila tissue polarity gene starry night encodes a member of the protocadherin family. Chae J, Kim MJ, Goo JH, Collier S, Gubb D, Charlton J, Adler PN, Park WJ. Development. 1999 Dec;126(23):5421-9.
PubMed:20202599	Large exons encoding multiple ectodomains are a characteristic feature of protocadherin genes. Wu Q, Maniatis T Proc Natl Acad Sci U S A 2000 Mar 28;97(7):3124-9
PubMed:7526465	Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Feng S, Chen JK, Yu H, Simon JA, Schreiber SL. Science. 1994 Nov 18;266(5188):1241-7.