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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: TEM22 (uPARAP)

	TEM domain structure

	TEM Sequence Analysis

name	from	to	source/E	description
SignalP	1	30
Ricin_B_lectin	41	161	Pfam,E = 2.1e-05	The domain has a possible function in carbohydrate-recognition. The ricin B lectin, also (QxW)3,domain is composed of three homologous subdomains of 40 amino acids (alpha, beta and gamma) and a linker peptide of around 15 residues (lambda).
FN2	187	228	Pfam, E = 1.8e-27	The fibronectin2 domain contains four conserved cysteines involved in disulfide bonds and is part of the collagen-binding region of fibronectin.
lectin_c	264	359	Pfam, E =2.8e-28	CRD1 shows high conservation of key residues for Ca 2+ -dependent carbohydrate binding although there is a loss of conservation in Ca 2+ site 2.
lectin_c	408	504	Pfam, E =1.7e-34	CRD2 has a strong consensus binding site including the critical Ca 2+ /carbohydrate binding site residues, correctly spaced cysteine residues and 26/28 of the remaining conserved amino acids found in functional CRDs.
lectin_c	547	644	Pfam, E =1e-21	CRD3 is most likely not involved in carbohydrate binding as key residues required for Ca 2+ and sugar co-ordination are not conserved.(apolar=613-633)
lectin_c	702	808	Pfam, E =6.7e-10	CRD4 is most likely not involved in carbohydrate binding. Four cysteine residues required for carbohydrate binding are retained but key residues required for Ca 2+ and sugar co-ordination are not conserved.
lectin_c	851	950	Pfam, E =	CRD5 is most likely not involved in carbohydrate binding.
lectin_c	1002	1107	Pfam, E =1.6e+02	CRD6 is most likely not involved in carbohydrate binding.
	1113	1126	SEG	LCR(P)
lectin_c	1151	1243	Pfam, E =4e-09	CRD7 most likely not involved in carbohydrate binding.
lectin_c	1293	1393	Pfam, E =6.1e-05	CRD8 most likely not involved in carbohydrate binding.
TM	1413	1433	SEG	LCR(LV)
cytoplasmic	1433	1479		Two putative endocytosis motifs are present in the cytoplasmic Endo180 sequence. The first one is a weekly perserved tyrosine-based endocytosis motif (FxNxxY) FEGARY-1452. This type of signal is found in the vast majority of endocytic receptors. Although Y1452 is conserved in the macrophage mannose receptor family, human Endo180 has G in position 3 of the motif and mouse Endo180 has F3. The second one is a di-hydrophobic motifs (LV), with an upstream acidic residue has been shown to be important for targeting to endocytic vesicles EXXXLV-1469.
1479

	Remarks

• CLASSIFICATION: TEM22 was previously obtained in three independent experiments:
  • as KIAA0709, in a screen for large brain proteins
  • as Endo180 while looking for fibroblast cell surface receptor
  • as uPARAP urokinase receptor-associated protein
  It belongs to the family of macrophage mannose receptor proteins with the ability to be endocytosed. Three members are known to belong to this family besides TEM22. This are the macrophage mannose receptor, the phospholipase A(2) receptor and the DEC-205/MR6 receptor. Macrophage mannose receptor represents a particularly unusual group of type C lectins. While most of the members of the type C lectin group contain only a single carbohydrate recognition domain (CRD), macrophage mannose receptors contain 8.

• DOMAIN ARCHITECTURE: The large extracellular region contains the following domains a cysteine rich Ricin_B_lectin domain, a fibronectin type 2 domain, eight CRD (type C lectin). The single transmembrane domain is followed by a short cytoplasmic region. The protein shares this overall predicted protein domain structure with the other three members of the macrophage mannose receptor protein family.

• LOCALIZATION: 10-30% of TEM22/uPARAP co-localizes with clathrin to plasma membrane coated pits and 70-90% to intracellular endosomes. The protein is a proposed constitutively recycled receptor.

• FUNCTION: TEM22/uPARAP is part of a tri-molecular complex included the urokinase receptor, pro-urokinase. It proved capable of binding strongly to a single type of collagen, collagen V. This collagen binding reaction at the exact site of plasminogen activation on the cell may lead to adhesive functions as well as a contribution to cellular degradation of collagen matrices.

  LIGAND BINDING: uPARAP has been previously shown to bind collagen V and N-acetylglucosamine.
     The N-terminal cysteine-rich domain of TEM22/uPARAP might be involved in Ca 2+ -independent carbohydrate binding as has been shown for the macrophage mannose receptor.
     The macrophage mannose receptor protein family shows diversity in ligand binding which is partially contributed by differences in the CRD domains. Phospholipase A2 receptor and DEC-205/MR6 receptor lack key amino-acids for Ca 2+ -dependent carbohydrate binding in their type C lectins and are, thus, involved in protein-protein interactions. By contrast, uPARAP and the macrophage mannose receptor contain key amino-acids in CRD2 and CRD4. Both these receptors can mediate Ca 2+ -dependent carbohydrate binding and bind N-acetylglucosamine and mannose, fucose, N-acetylglucosamine respectively. This difference in carbohydrate binding specifity is paralleled by differences in the CRD2, CRD4 site conservation. Mannose receptor binds mainly by its CRD4, while uPARAP is proposed to bind mainly via its CRD2 domain.
     Within CRD4, carbohydrate binding requires four cysteine residues to create nested disulphide bonds plus other key residues for the formation of two Ca 2+ binding sites and the packing and formation of the hydrophobic cores. The uPARAP CRD4 has retained the four cysteine residues at equivalent spacing but key residues required for Ca 2+ and sugar co-ordination are not conserved. However, CRD2 in both mouse and human uPARAP has a strong consensus binding site including the critical Ca 2+ /sugar binding site residues, correctly spaced cysteine residues and 26/28 of the remaining conserved amino acids found in functional CRDs. Additionally, many of these residues are also conserved in uPARAP CRD1 although there is a loss of conservation in Ca 2+ site 2.

  ENDOCYTOSIS: The ability of receptors to be recruited into clathrin coated pits and subsequently endocytosed, requires that their cytoplasmic domains can interact with intracellular adaptin complexes. Two putative endocytosis motifs are present in the uPARAP sequence.
     The first one is a weekly perserved tyrosine-based endocytosis motif (FxNxxY) FEGARY-1452. This type of signal is found in the vast majority of endocytic receptors. Although Y1452 is conserved in the macrophage mannose receptor family, human uPARAP has G in position 3 of the motif and mouse uPARAP has F3.
     The second one is a di-hydrophobic motifs (LV), with an upstream acidic residue has been shown to be important for targeting to endocytic vesicles EXXXLV-1469.
     The WIGL domain is conserved in seven out of the eight C-lectin domains (altered in domain3). REGULATION OF RECEPTOR-CYCLING: uPARAP is serine-phosphorylated after phorbol esters treatment, potentially by protein kinase C. Receptor phosphorylation could be an important modulator of intracellular trafficking.

• DISTRIBUTION OF THE MOUSE ORTHOLOGUE: The relatively widespread transcription in adult tissues is consistent with endothelial expression, and the in situ hybridization analysis also supports this contention. The high level of expression of the protein in matrix-depositing chondrocytes,and its detection in regions of mineralization, such as the sternal and tooth regions, as well as sites of cartilage deposition, such as the layrnx suggest that the lectin might be involved with the synthesis of cartilage or other types of extracellular matrix produced by the chondrocytes. Based on this observation is has been hypothesized that the protein might be involved in the uptake of highly glycosylated precursor proteins that are degraded and utilized for extracellular matrix production, or contrastingly might be involved in remodeling of the extracellular matrix by the endocytosis of highly glycosylated proteins.

	Sequence Information

TEM	TEM22
Reliability of Gen2Tag mapping	Cid->tag (Hs.7835) frequency: tem22: CATG-GCCCTTTCTCT=54/55 (EST oriented) tem22: CATG-GCCCTTTCTCT=2/4 (cDNA)
Analysis	BlastP against nr Output Created by a Suite of Single Sequence Analysis Techniques
Protein Description	SEQ.SOURCE: gi|3327232|dbj|BAA31684.1| KIAA0709 protein REMARKS: TEM22 was obtained in three independent experiments: as KIAA0709, in a screen for large brain proteins as Endo180 while looking for fibroblast cell surface receptor as uPARAP urokinase receptor-associated protein
Protein Sequence	MGPGRPAPAPWPRHLLRCVLLLGCLHLGRPGAPGDAALPEPNVFLIFSHGLQGCLEAQGGQVRVTPACNT SLPAQRWKWVSRNRLFNLGTMQCLGTGWPGTNTTASLGMYECDREALNLRWHCRTLGDQLSLLLGARTSN ISKPGTLERGDQTRSGQWRIYGSEEDLCALPYHEVYTIQGNSHGKPCTIPFKYDNQWFHGCTSTGREDGH LWCATTQDYGKDERWGFCPIKSNDCETFWDKDQLTDSCYQFNFQSTLSWREAWASCEQQGADLLSITEIH EQTYINGLLTGYSSTLWIGLNDLDTSGGWQWSDNSPLKYLNWESDQPDNPSEENCGVIRTESSGGWQNRD CSIALPYVCKKKPNATAEPTPPDRWANVKVECEPSWQPFQGHCYRLQAEKRSWQESKKACLRGGGDLVSI HSMAELEFITKQIKQEVEELWIGLNDLKLQMNFEWSDGSLVSFTHWHPFEPNNFRDSLEDCVTIWGPEGR WNDSPCNQSLPSICKKAGQLSQGAAEEDHGCRKGWTWHSPSCYWLGEDQVTYSEARRLCTDHGSQLVTIT NRFEQAFVSSLIYNWEGEYFWTALQDLNSTGSFFWLSGDEVMYTHWNRDQPGYSRGGCVALATGSAMGLW EVKNCTSFRARYICRQSLGTPVTPELPGPDPTPSLTGSCPQGWASDTKLRYCYKVFSSERLQDKKSWVQA QGACQELGAQLLSLASYEEEHFVANMLNKIFGESEPEIHEQHWFWIGLNRRDPRGGQSWRWSDGVGFSYH NFDRSRHDDDDIRGCAVLDLASLQWVAMQCDTQLDWICKIPRGTDVREPDDSPQGRREWLRFQEAEYKFF EHHSTWAQAQRICTWFQAELTSVHSQAELDFLSHNLQKFSRAQEQHWWIGLHTSESDGRFRWTDGSIINF ISWAPGKPRPVGKDKKCVYMTASREDWGDQRCLTALPYICKRSNVTKETQPPDLPTTALGGCPSDWIQFL NKCFQVQGQEPQSRVKWSEAQFSCEQQEAQLVTITNPLEQAFITASLPNVTFDLWIGLHASQRDFQWVEQ EPLMYANWAPGEPSGPSPAPSGNKPTSCAVVLHSPSAHFTGRWDDRSCTEETHGFICQKGTDPSLSPSPA ALPPAPGTELSYLNGTFRLLQKPLRWHDALLLCESHNASLAYVPDPYTQAFLTQAARGLRTPLWIGLAGE EGSRRYSWVSEEPLNYVGWQDGEPQQPGGCTYVDVDGAWRTTSCDTKLQGAVCGVSSGPPPPRRISYHGS CPQGLADSAWIPFREHCYSFHMELLLGHKEARQRCQRAGGAVLSILDEMENVFVWEHLQSYEGQSRGAWL GMNFNPKGGTLVWQDNTAVNYSNWGPPGLGPSMLSHNSCYWIQSNSGLWRPGACTNITMGVVCKLPRAEQ SSFSPSALPENPAALVVVLMAVLLLLALLTAALILYRRRQSIERGAFEGARYSRSSSSPTEATEKNILVS DMEMNEQQE
SAGE-Tag	CATG-GCCCTTTCTCT
EST/cluster Description	UNIGEN CLUSTER: Hs.7835 : endocytic receptor SEQ.SOURCE: gi|3327231|dbj|AB014609.1|AB014609 mRNA for KIAA0709 protein MARKINGS: TEM22 Tag in red
EST/cluster Sequence	CGGAGGAGGACGCGAGCCCCTTGCGGGCGGTCATCACAGCCCAGCCTCGGGGCTGCCACAGCGCGTTGCG CCTGTGCGCCCTCGGTCCCCGCGTCCACTGAGCGCCGCGCTCGGGGATGGGGCCCGGCCGGCCGGCCCCC GCGCCCTGGCCTCGTCACCTGCTGCGCTGCGTCCTGCTCCTCGGGTGCCTGCACCTCGGCCGTCCCGGCG CCCCTGGGGACGCCGCCCTCCCGGAACCCAACGTCTTCCTCATCTTCAGCCATGGACTGCAGGGCTGCCT GGAGGCCCAGGGCGGGCAGGTCAGAGTCACCCCGGCTTGCAATACCAGCCTCCCTGCCCAGCGCTGGAAG TGGGTCTCCCGAAACCGGCTATTCAACCTGGGTACCATGCAGTGCCTGGGCACAGGCTGGCCAGGCACCA ACACCACGGCCTCCCTGGGCATGTATGAGTGTGACCGGGAAGCACTGAATCTTCGCTGGCATTGTCGTAC ACTGGGTGACCAGCTGTCCTTGCTCCTGGGGGCCCGCACCAGCAACATATCCAAGCCTGGCACCCTTGAG CGTGGTGACCAGACCCGCAGTGGCCAGTGGCGCATCTACGGCAGCGAGGAGGACCTATGTGCTCTGCCCT ACCACGAGGTCTACACCATCCAGGGAAACTCCCACGGAAAGCCGTGCACCATCCCCTTCAAATATGACAA CCAGTGGTTCCACGGCTGCACCAGCACGGGCCGCGAGGATGGTCACCTGTGGTGTGCCACCACCCAGGAC TACGGCAAAGACGAGCGCTGGGGCTTCTGCCCCATCAAGAGTAACGACTGCGAGACCTTCTGGGACAAGG ACCAGCTGACTGACAGCTGCTACCAGTTTAACTTCCAGTCCACGCTGTCGTGGAGGGAGGCCTGGGCCAG CTGCGAGCAGCAGGGTGCGGATCTGCTGAGCATCACGGAGATCCACGAGCAGACCTACATCAACGGCCTC CTCACTGGGTACAGCTCCACCCTGTGGATCGGCTTGAATGACTTGGACACGAGCGGAGGCTGGCAGTGGT CGGACAACTCGCCCCTCAAGTACCTCAACTGGGAGAGTGACCAGCCGGACAACCCCAGTGAGGAGAACTG TGGAGTGATCCGCACTGAGTCCTCGGGCGGCTGGCAGAACCGTGACTGCAGCATCGCGCTGCCCTATGTG TGCAAGAAGAAGCCCAACGCCACGGCCGAGCCCACCCCTCCAGACAGGTGGGCCAATGTGAAGGTGGAGT GCGAGCCGAGCTGGCAGCCCTTCCAGGGCCACTGCTACCGCCTGCAGGCCGAGAAGCGCAGCTGGCAGGA GTCCAAGAAGGCATGTCTACGGGGCGGTGGCGACCTGGTCAGCATCCACAGCATGGCGGAGCTGGAATTC ATCACCAAGCAGATCAAGCAAGAGGTGGAGGAGCTGTGGATCGGCCTCAACGATTTGAAACTGCAGATGA ATTTTGAGTGGTCTGACGGGAGCCTTGTGAGCTTCACCCACTGGCACCCCTTTGAGCCCAACAACTTCCG GGACAGTCTGGAGGACTGTGTCACCATCTGGGGCCCGGAAGGCCGCTGGAACGACAGTCCCTGTAACCAG TCCTTGCCATCCATCTGCAAGAAGGCAGGCCAGCTGAGCCAGGGGGCCGCCGAGGAGGACCATGGCTGCC GGAAGGGTTGGACGTGGCACAGCCCATCCTGCTACTGGCTGGGAGAAGACCAAGTGACCTACAGTGAGGC CCGGCGCCTGTGCACTGACCATGGCTCTCAGCTGGTCACCATCACCAACAGGTTCGAGCAGGCCTTCGTC AGCAGCCTCATCTACAACTGGGAGGGCGAGTACTTCTGGACGGCCCTGCAGGACCTCAACAGCACCGGCT CCTTCTTCTGGCTCAGTGGGGATGAAGTCATGTACACCCACTGGAACCGGGACCAGCCCGGGTACAGCCG TGGGGGCTGCGTGGCGCTGGCCACTGGCAGCGCCATGGGGCTGTGGGAGGTGAAGAACTGTACCTCGTTC CGGGCCCGCTACATCTGCCGGCAGAGCCTGGGCACTCCAGTGACGCCGGAGCTGCCGGGGCCAGATCCCA CGCCCAGCCTCACTGGCTCCTGTCCCCAGGGCTGGGCCTCGGACACCAAACTCCGGTATTGCTATAAGGT GTTCAGCTCAGAGCGGCTGCAGGACAAGAAGAGCTGGGTCCAGGCCCAGGGGGCCTGCCAGGAGCTGGGG GCCCAGCTGCTGAGCCTGGCCAGCTACGAGGAGGAGCACTTTGTGGCCAACATGCTCAACAAGATCTTCG GTGAATCAGAACCCGAGATCCACGAGCAGCACTGGTTCTGGATCGGCCTGAACCGTCGGGATCCCAGAGG GGGTCAGAGTTGGCGCTGGAGCGACGGCGTAGGGTTCTCTTACCACAATTTCGACCGGAGCCGGCACGAC GACGACGACATCCGAGGCTGTGCGGTGCTGGACCTGGCCTCCCTGCAGTGGGTGGCCATGCAGTGCGACA CACAGCTGGACTGGATCTGCAAGATCCCCAGAGGTACGGACGTGCGGGAGCCCGACGACAGCCCTCAAGG CCGACGGGAATGGCTGCGCTTCCAGGAGGCCGAGTACAAGTTCTTTGAGCACCACTCCACGTGGGCGCAG GCGCAGCGCATCTGCACGTGGTTCCAGGCCGAGCTGACCTCCGTGCACAGCCAGGCAGAGCTAGACTTCC TGAGCCACAACTTGCAGAAGTTCTCCCGGGCCCAGGAGCAGCACTGGTGGATCGGCCTGCACACCTCTGA GAGCGATGGGCGCTTCAGATGGACAGATGGTTCCATTATAAACTTCATCTCCTGGGCACCAGGCAAACCT CGGCCTGTCGGCAAGGACAAGAAGTGCGTGTACATGACAGCCAGCCGAGAGGACTGGGGGGACCAGAGGT GCCTGACAGCCTTGCCCTACATCTGCAAGCGCAGCAACGTCACCAAAGAAACGCAGCCCCCAGACCTGCC AACTACAGCCCTGGGGGGCTGCCCCTCTGACTGGATCCAGTTCCTCAACAAGTGTTTTCAGGTCCAGGGC CAGGAACCCCAGAGCCGGGTGAAGTGGTCAGAGGCACAGTTCTCCTGTGAACAGCAAGAGGCCCAGCTGG TCACCATCACAAACCCCTTAGAGCAAGCATTCATCACAGCCAGCCTGCCCAATGTGACCTTTGACCTTTG GATTGGCCTCCATGCCTCGCAGAGGGACTTCCAGTGGGTGGAGCAGGAGCCTTTGATGTATGCCAACTGG GCACCTGGGGAGCCCTCTGGCCCTAGCCCTGCTCCCAGTGGCAACAAACCGACCAGCTGTGCGGTGGTCC TGCACAGCCCCTCAGCCCACTTCACTGGCCGCTGGGACGATCGGAGCTGCACGGAGGAGACCCATGGCTT CATCTGCCAGAAGGGCACGGACCCCTCCCTGAGCCCGTCCCCAGCAGCGCTGCCCCCCGCCCCGGGCACT GAGCTCTCCTACCTCAACGGCACCTTCCGGCTGCTTCAGAAGCCGCTGCGCTGGCACGATGCCCTCCTGC TGTGTGAGAGCCACAATGCCAGCCTGGCCTACGTGCCCGACCCCTACACCCAGGCCTTCCTCACGCAGGC TGCCCGAGGGCTGCGCACGCCGCTCTGGATTGGGCTGGCTGGCGAGGAGGGCTCTCGGCGGTACTCCTGG GTCTCAGAGGAGCCGCTGAACTACGTGGGCTGGCAGGACGGGGAGCCGCAGCAGCCGGGGGGCTGTACCT ACGTAGATGTGGACGGGGCCTGGCGCACCACCAGCTGTGACACCAAGCTGCAGGGGGCTGTGTGTGGGGT TAGCAGTGGGCCCCCTCCTCCCCGAAGAATAAGCTACCATGGCAGCTGTCCCCAGGGACTGGCAGACTCC GCGTGGATTCCCTTCCGGGAGCACTGCTATTCTTTCCACATGGAGCTGCTGCTGGGCCACAAGGAGGCGC GACAGCGCTGCCAGAGAGCGGGTGGGGCCGTCCTGTCTATCCTGGATGAGATGGAGAATGTGTTTGTCTG GGAGCACCTGCAGAGCTATGAGGGCCAGAGTCGGGGCGCCTGGCTGGGCATGAACTTCAACCCCAAAGGA GGCACTCTGGTCTGGCAGGACAACACAGCTGTGAACTACTCCAACTGGGGGCCCCCGGGCTTGGGCCCCA GCATGCTGAGCCACAACAGCTGCTACTGGATTCAGAGCAACAGCGGGCTATGGCGCCCCGGCGCTTGCAC CAACATCACCATGGGTGTCGTCTGCAAGCTTCCTCGTGCTGAGCAGAGCAGCTTCTCCCCATCAGCGCTT CCAGAGAACCCAGCGGCCCTGGTGGTGGTGCTGATGGCGGTGCTGCTGCTCCTGGCCTTGCTGACCGCAG CCCTCATCCTTTACCGGAGGCGCCAGAGCATCGAGCGCGGGGCCTTTGAGGGTGCCCGCTACAGCCGCAG CAGCTCCAGCCCCACCGAGGCCACTGAGAAGAACATCCTGGTGTCAGACATGGAAATGAATGAGCAACAA GAATAGAGCCAGGCGCGTGGGCAGGGCCAGGGCGGGAGGAGCTGGGGAGCTGGGGCCCTGGGTCAGTCTG GCCCCCCACCAGCTGCCTGTCCAGTTGGCCTATGGAAGGGTGCCCTTGGGAGTCGCTGTTGGGAGCCGGA GCTGGGCAGAGCCTGGGCTGGTGGGGTGCCACCCTCCCACAAGGGCTGGGCTGAGACCCAGCTGAGTGCA GCGTGGCGTTTCCCTTTCTGGGGGGGCCTGAGGTCTTGTCACCTGGTCCTGTGCCCCCACAGGAACCAGA GGTAGGATGGGAGGGGGAACGAGAGCCTCTTTCTCCCCAGAGCCCCCGGCCCAGGCCTGTTGATCCGCGC CCCAGGACCCCCTTCTTTGCAGAGCCCGAGGAGCCTCCCCTGTCCCCTCGGGCAGATCTGTTGTGTCTCT CTTCCCACCTGGCAGCCTCAGCTCTGTGCCCCTCACCCTGCTCCCTCTCGCCCCTTCTCTCCCACCCCTT CCTTCTGAGCCGGGCCCTGGGGATTGGGGAGCCCTCTTGTTCCTGATGAGGGTCAGCTGAGGGGGCTGAG CATCCATCACTCCTGTGCCTGCTGGGGTGGCTGTGGGGCGTGGCAGGAGGGGCCTAGGTGGGTTGGGCCT GAGAACCAGGGCACGGGTGTGGTGTCTGCTGGGCTGGAGATAAGACTGGGGAGAGACACCCCAACCTCCC AGGGTGGGAGCTGGGCCGGGCTGGGATGTCATCTCCTGCCGGGCGGGGGAGGGCTCTGCCCCTGGAAGAG TCCCCTGTGGGGACCAAAATAAGTTCCCTAACATCTCCAGCTCCTGGCTCTGGTTTGGAGCAAGGGGAAG GGTTGCCAGAGTCCTGGGGGCCCCAGAGGAGCAGGAGTCTGGGAGGGCCCAGAGTTCACCCTCTAGTGGA TCCAGGAGGAGCAGCACCCGAGCCCTGGAGTGGCCCAGTACCCTTCCAAGAGGCCACAGTCCCAGCCAGG ACAAAGTATGCGGCCCATCCTGGTGCGACAGCGTGGGACAATGTGAACATGGACTCGAAGACATGGCCCT TTCTCTGTAGTTGATTTTTTAAATGTGCCATTATTGTTTTT
Genomic Sequence Description	SEQ.SOURCE: gi|5867237|ref|NT_000839.1|Hs17_1442| Homo sapiens chr.17 invers REMARKS: The first exon separated by a >32kb intron.
Genomic Sequence

	Literature

PubMed: 1063690	A urokinase receptor-associated protein with specific collagen binding properties. Behrendt N, Jensen ON, Engelholm LH, Mortz E, Mann M, Dano K. J Biol Chem 2000 Jan 21;275(3):1993-2002.
PubMed: 1068315	Endo180, an endocytic recycling glycoprotein related to the macrophage mannose receptor is expressed on fibroblasts, endothelial cells and macrophages and functions as a lectin receptor. Sheikh H, Yarwood H, Ashworth A, Isacke CM. J Cell Sci. 2000 Mar;113 ( Pt 6):1021-32.
PubMed: 9677372	Mechanism of N-acetylgalactosamine binding to a C-type animal lectin carbohydrate-recognition domain. Kolatkar AR, Leung AK, Isecke R, Brossmer R, Drickamer K, Weis WI. J Biol Chem. 1998 Jul 31;273(31):19502-8.
PubMed: 8702911	Characterization of a novel member of the macrophage mannose receptor type C lectin family. Wu K, Yuan J, Lasky LA. J Biol Chem. 1996 Aug 30;271(35):21323-30.
PubMed: 7650016	A role for acidic residues in di-leucine motif-based targeting to the endocytic pathway. Pond L, Kuhn LA, Teyton L, Schutze MP, Tainer JA, Jackson MR, Peterson PA. J Biol Chem 1995 Aug 25;270(34):19989-97.
PubMed: 8408022	YTRF is the conserved internalization signal of the transferrin receptor, and a second YTRF signal at position 31-34 enhances endocytosis. Collawn JF, Lai A, Domingo D, Fitch M, Hatton S, Trowbridge IS. J Biol Chem. 1993 Oct 15;268(29):21686-92.
PubMed: 2188094	p180, a novel recycling transmembrane glycoprotein with restricted cell type expression. Isacke CM, van der Geer P, Hunter T, Trowbridge IS. Mol Cell Biol. 1990 Jun;10(6):2606-18.