ID CD166_HUMAN Reviewed; 583 AA. AC Q13740; B2RNS3; B4DTU0; O60892; Q1HGM8; Q1HGM9; Q6PEY4; Q6ZS95; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 27-MAR-2024, entry version 208. DE RecName: Full=CD166 antigen; DE AltName: Full=Activated leukocyte cell adhesion molecule; DE AltName: CD_antigen=CD166; DE Flags: Precursor; GN Name=ALCAM; Synonyms=MEMD {ECO:0000303|PubMed:9502422}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-301, PARTIAL PROTEIN RP SEQUENCE, INTERACTION WITH CD6, SUBUNIT, SUBCELLULAR LOCATION, FUNCTION, RP AND TISSUE SPECIFICITY. RX PubMed=7760007; DOI=10.1084/jem.181.6.2213; RA Bowen M.A., Patel D.D., Li X., Modrell B., Malacko A.R., Wang W.-C., RA Marquardt H., Neubauer M., Pesando J.M., Francke U., Haynes B.F., RA Aruffo A.; RT "Cloning, mapping, and characterization of activated leukocyte-cell RT adhesion molecule (ALCAM), a CD6 ligand."; RL J. Exp. Med. 181:2213-2220(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 3), RP FUNCTION (ISOFORMS 1 AND 3), GLYCOSYLATION, AND TISSUE SPECIFICITY. RX PubMed=15496415; DOI=10.1074/jbc.m407776200; RA Ikeda K., Quertermous T.; RT "Molecular isolation and characterization of a soluble isoform of activated RT leukocyte cell adhesion molecule that modulates endothelial cell RT function."; RL J. Biol. Chem. 279:55315-55323(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RA Abe Y., Bui-Thanh N.-A., Smith C.W., Ballantyne C.M., Burns A.R.; RT "A novel alternatively spliced variant of activated leukocyte cell adhesion RT molecule (ALCAM/CD166) resulting from a deletion in the extracellular RT membrane proximal stem."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Lung, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Brain, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-583 (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=9502422; RA Degen W.G., van Kempen L.C., Gijzen E.G., van Groningen J.J., van Kooyk Y., RA Bloemers H.P.J., Swart G.W.; RT "MEMD, a new cell adhesion molecule in metastasizing human melanoma cell RT lines, is identical to ALCAM (activated leukocyte cell adhesion RT molecule)."; RL Am. J. Pathol. 152:805-813(1998). RN [8] RP DOMAIN CD6 BINDING, AND INTERACTION WITH CD6. RX PubMed=8823162; DOI=10.1021/bi961038k; RA Skonier J.E., Bowen M.A., Emswiler J., Aruffo A., Bajorath J.; RT "Recognition of diverse proteins by members of the immunoglobulin RT superfamily: delineation of the receptor binding site in the human CD6 RT ligand ALCAM."; RL Biochemistry 35:12287-12291(1996). RN [9] RP GLYCOSYLATION AT ASN-91; ASN-167; ASN-480 AND ASN-499. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [10] RP FUNCTION, INTERACTION WITH CD6, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=15048703; DOI=10.1002/eji.200424856; RA Hassan N.J., Barclay A.N., Brown M.H.; RT "Frontline: Optimal T cell activation requires the engagement of CD6 and RT CD166."; RL Eur. J. Immunol. 34:930-940(2004). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=15294938; DOI=10.4049/jimmunol.173.4.2262; RA Gimferrer I., Calvo M., Mittelbrunn M., Farnos M., Sarrias M.R., Enrich C., RA Vives J., Sanchez-Madrid F., Lozano F.; RT "Relevance of CD6-mediated interactions in T cell activation and RT proliferation."; RL J. Immunol. 173:2262-2270(2004). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95; ASN-265 AND ASN-499. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CD6, SUBUNIT, AND TISSUE RP SPECIFICITY. RX PubMed=16352806; DOI=10.1182/blood-2005-09-3881; RA Zimmerman A.W., Joosten B., Torensma R., Parnes J.R., van Leeuwen F.N., RA Figdor C.G.; RT "Long-term engagement of CD6 and ALCAM is essential for T-cell RT proliferation induced by dendritic cells."; RL Blood 107:3212-3220(2006). RN [14] RP INTERACTION WITH CD6. RX PubMed=16914752; DOI=10.1128/mcb.00688-06; RA Hassan N.J., Simmonds S.J., Clarkson N.G., Hanrahan S., Puklavec M.J., RA Bomb M., Barclay A.N., Brown M.H.; RT "CD6 regulates T-cell responses through activation-dependent recruitment of RT the positive regulator SLP-76."; RL Mol. Cell. Biol. 26:6727-6738(2006). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-91; ASN-95; ASN-457 AND RP ASN-480. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-457. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION BY TNF RP AND IFNG. RX PubMed=23169771; DOI=10.1096/fj.12-217844; RA Iolyeva M., Karaman S., Willrodt A.H., Weingartner S., Vigl B., Halin C.; RT "Novel role for ALCAM in lymphatic network formation and function."; RL FASEB J. 27:978-990(2013). RN [19] RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=24740813; DOI=10.1182/blood-2014-03-565721; RA Chitteti B.R., Kobayashi M., Cheng Y., Zhang H., Poteat B.A., RA Broxmeyer H.E., Pelus L.M., Hanenberg H., Zollman A., Kamocka M.M., RA Carlesso N., Cardoso A.A., Kacena M.A., Srour E.F.; RT "CD166 regulates human and murine hematopoietic stem cells and the RT hematopoietic niche."; RL Blood 124:519-529(2014). RN [20] RP INTERACTION WITH CD6; LGALS1 AND LGALS3, GLYCOSYLATION, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=24945728; DOI=10.1016/j.febslet.2014.05.064; RA Escoda-Ferran C., Carrasco E., Caballero-Banos M., Miro-Julia C., RA Martinez-Florensa M., Consuegra-Fernandez M., Martinez V.G., Liu F.T., RA Lozano F.; RT "Modulation of CD6 function through interaction with galectin-1 and -3."; RL FEBS Lett. 588:2805-2813(2014). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [23] RP FUNCTION. RX PubMed=29263213; DOI=10.4049/jimmunol.1700553; RA Xu Z., Chang C.C., Li M., Zhang Q.Y., Vasilescu E.M., D'Agati V., RA Floratos A., Vlad G., Suciu-Foca N.; RT "ILT3.Fc-CD166 Interaction Induces Inactivation of p70 S6 Kinase and RT Inhibits Tumor Cell Growth."; RL J. Immunol. 200:1207-1219(2018). RN [24] RP 3D-STRUCTURE MODELING OF 28-133. RX PubMed=8520490; DOI=10.1002/pro.5560040822; RA Bajorath J., Bowen M.A., Aruffo A.; RT "Molecular model of the N-terminal receptor-binding domain of the human CD6 RT ligand ALCAM."; RL Protein Sci. 4:1644-1647(1995). RN [25] RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS), DISULFIDE BONDS, INTERACTION WITH RP CD6, AND SUBUNIT. RX PubMed=26146185; DOI=10.1016/j.str.2015.05.019; RA Chappell P.E., Garner L.I., Yan J., Metcalfe C., Hatherley D., Johnson S., RA Robinson C.V., Lea S.M., Brown M.H.; RT "Structures of CD6 and its ligand CD166 give insight into their RT interaction."; RL Structure 23:1426-1436(2015). CC -!- FUNCTION: Cell adhesion molecule that mediates both heterotypic cell- CC cell contacts via its interaction with CD6, as well as homotypic cell- CC cell contacts (PubMed:7760007, PubMed:15496415, PubMed:15048703, CC PubMed:16352806, PubMed:23169771, PubMed:24945728). Promotes T-cell CC activation and proliferation via its interactions with CD6 CC (PubMed:15048703, PubMed:16352806, PubMed:24945728). Contributes to the CC formation and maturation of the immunological synapse via its CC interactions with CD6 (PubMed:15294938, PubMed:16352806). Mediates CC homotypic interactions with cells that express ALCAM (PubMed:15496415, CC PubMed:16352806). Acts as a ligand for the LILRB4 receptor, enhancing CC LILRB4-mediated inhibition of T cell proliferation (PubMed:29263213). CC Required for normal hematopoietic stem cell engraftment in the bone CC marrow (PubMed:24740813). Mediates attachment of dendritic cells onto CC endothelial cells via homotypic interaction (PubMed:23169771). Inhibits CC endothelial cell migration and promotes endothelial tube formation via CC homotypic interactions (PubMed:15496415, PubMed:23169771). Required for CC normal organization of the lymph vessel network. Required for normal CC hematopoietic stem cell engraftment in the bone marrow. Plays a role in CC hematopoiesis; required for normal numbers of hematopoietic stem cells CC in bone marrow. Promotes in vitro osteoblast proliferation and CC differentiation (By similarity). Promotes neurite extension, axon CC growth and axon guidance; axons grow preferentially on surfaces that CC contain ALCAM. Mediates outgrowth and pathfinding for retinal ganglion CC cell axons (By similarity). {ECO:0000250|UniProtKB:P42292, CC ECO:0000269|PubMed:15048703, ECO:0000269|PubMed:15294938, CC ECO:0000269|PubMed:15496415, ECO:0000269|PubMed:16352806, CC ECO:0000269|PubMed:24945728, ECO:0000269|PubMed:29263213, CC ECO:0000269|PubMed:7760007}. CC -!- FUNCTION: [Isoform 3]: Inhibits activities of membrane-bound isoforms CC by competing for the same interaction partners. Inhibits cell CC attachment via homotypic interactions. Promotes endothelial cell CC migration. Inhibits endothelial cell tube formation. CC {ECO:0000269|PubMed:15496415}. CC -!- SUBUNIT: Homodimer (PubMed:7760007, PubMed:16352806, PubMed:15048703, CC PubMed:26146185). Interacts (via extracellular domain) with CD6 (via CC extracellular domain) (PubMed:7760007, PubMed:8823162, PubMed:15048703, CC PubMed:16914752, PubMed:24945728, PubMed:26146185). Homodimerization CC and interaction with CD6 involve the same region and cannot occur CC simultaneously. The affinity for CD6 is much higher than the affinity CC for self-association (PubMed:15048703). Interacts (via glycosylated CC extracellular domain) with LGALS1 and LGALS3 (PubMed:24945728). CC Interaction with LGALS1 or LGALS3 inhibits interaction with CD6 CC (PubMed:24945728). {ECO:0000269|PubMed:15048703, CC ECO:0000269|PubMed:16352806, ECO:0000269|PubMed:16914752, CC ECO:0000269|PubMed:24945728, ECO:0000269|PubMed:26146185, CC ECO:0000269|PubMed:7760007, ECO:0000269|PubMed:8823162}. CC -!- INTERACTION: CC Q13740; Q13740: ALCAM; NbExp=3; IntAct=EBI-1188108, EBI-1188108; CC Q13740; P30203: CD6; NbExp=5; IntAct=EBI-1188108, EBI-2873748; CC Q13740; P09382: LGALS1; NbExp=3; IntAct=EBI-1188108, EBI-1048875; CC Q13740; P17931: LGALS3; NbExp=3; IntAct=EBI-1188108, EBI-1170392; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15048703, CC ECO:0000269|PubMed:15294938, ECO:0000269|PubMed:16352806, CC ECO:0000269|PubMed:23169771, ECO:0000269|PubMed:24740813, CC ECO:0000269|PubMed:24945728, ECO:0000269|PubMed:7760007}; Single-pass CC type I membrane protein {ECO:0000305}. Cell projection, axon CC {ECO:0000250|UniProtKB:Q61490}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:Q61490}. Note=Detected at the immunological CC synapse, i.e, at the contact zone between antigen-presenting dendritic CC cells and T-cells (PubMed:15294938, PubMed:16352806). Colocalizes with CC CD6 and the TCR/CD3 complex at the immunological synapse CC (PubMed:15294938). {ECO:0000269|PubMed:15294938, CC ECO:0000269|PubMed:16352806}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted CC {ECO:0000269|PubMed:15496415}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q13740-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13740-2; Sequence=VSP_021797; CC Name=3; Synonyms=sALCAM; CC IsoId=Q13740-3; Sequence=VSP_053530, VSP_053531; CC Name=4; CC IsoId=Q13740-4; Sequence=VSP_053529, VSP_053532; CC -!- TISSUE SPECIFICITY: Detected on hematopoietic stem cells derived from CC umbilical cord blood (PubMed:24740813). Detected on lymph vessel CC endothelial cells, skin and tonsil (PubMed:23169771). Detected on CC peripheral blood monocytes (PubMed:15048703). Detected on monocyte- CC derived dendritic cells (at protein level) (PubMed:16352806). Detected CC at low levels in spleen, placenta, liver (PubMed:9502422). Expressed by CC activated T-cells, B-cells, monocytes and thymic epithelial cells CC (PubMed:7760007). Isoform 1 and isoform 3 are detected in vein and CC artery endothelial cells, astrocytes, keratinocytes and artery smooth CC muscle cells (PubMed:15496415). Expressed by neurons in the brain. CC Restricted expression in tumor cell lines. Detected in highly CC metastasizing melanoma cell lines (PubMed:9502422). CC {ECO:0000269|PubMed:15048703, ECO:0000269|PubMed:24740813, CC ECO:0000269|PubMed:7760007, ECO:0000269|PubMed:9502422}. CC -!- INDUCTION: Up-regulated by TNF and IFNG (at protein level). CC {ECO:0000269|PubMed:23169771}. CC -!- DOMAIN: The CD6 binding site is located in the N-terminal Ig-like CC domain. {ECO:0000269|PubMed:8823162}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15496415, CC ECO:0000305|PubMed:24945728}. CC -!- MISCELLANEOUS: [Isoform 3]: Secreted form, inhibits isoform 1 CC homophilic interaction. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L38608; AAB59499.1; -; mRNA. DR EMBL; AY644765; AAV28819.1; -; mRNA. DR EMBL; DQ486139; ABF48405.1; -; mRNA. DR EMBL; DQ486140; ABF48406.1; -; mRNA. DR EMBL; AK127617; BAC87059.1; -; mRNA. DR EMBL; AK300362; BAG62102.1; -; mRNA. DR EMBL; AK316113; BAH14484.1; -; mRNA. DR EMBL; AC023602; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC078806; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC133476; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC057809; AAH57809.1; -; mRNA. DR EMBL; BC137096; AAI37097.1; -; mRNA. DR EMBL; BC137097; AAI37098.1; -; mRNA. DR EMBL; Y10183; CAA71256.1; -; mRNA. DR CCDS; CCDS33810.1; -. [Q13740-1] DR CCDS; CCDS58841.1; -. [Q13740-2] DR PIR; I39428; I39428. DR RefSeq; NP_001230209.1; NM_001243280.1. [Q13740-2] DR RefSeq; NP_001230212.1; NM_001243283.1. [Q13740-3] DR RefSeq; NP_001618.2; NM_001627.3. [Q13740-1] DR PDB; 5A2F; X-ray; 1.86 A; A=1-583. DR PDBsum; 5A2F; -. DR AlphaFoldDB; Q13740; -. DR SMR; Q13740; -. DR BioGRID; 106716; 112. DR DIP; DIP-39093N; -. DR IntAct; Q13740; 22. DR MINT; Q13740; -. DR STRING; 9606.ENSP00000305988; -. DR ChEMBL; CHEMBL4665584; -. DR TCDB; 8.A.23.1.10; the basigin (basigin) family. DR GlyConnect; 1085; 66 N-Linked glycans (8 sites). DR GlyCosmos; Q13740; 9 sites, 73 glycans. DR GlyGen; Q13740; 11 sites, 73 N-linked glycans (7 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q13740; -. DR MetOSite; Q13740; -. DR PhosphoSitePlus; Q13740; -. DR SwissPalm; Q13740; -. DR BioMuta; ALCAM; -. DR DMDM; 118572629; -. DR CPTAC; CPTAC-1502; -. DR CPTAC; CPTAC-1503; -. DR EPD; Q13740; -. DR jPOST; Q13740; -. DR MassIVE; Q13740; -. DR MaxQB; Q13740; -. DR PaxDb; 9606-ENSP00000305988; -. DR PeptideAtlas; Q13740; -. DR ProteomicsDB; 5128; -. DR ProteomicsDB; 59670; -. [Q13740-1] DR ProteomicsDB; 59671; -. [Q13740-2] DR ProteomicsDB; 68208; -. DR Pumba; Q13740; -. DR ABCD; Q13740; 25 sequenced antibodies. DR Antibodypedia; 2625; 952 antibodies from 40 providers. DR CPTC; Q13740; 2 antibodies. DR DNASU; 214; -. DR Ensembl; ENST00000306107.9; ENSP00000305988.5; ENSG00000170017.12. [Q13740-1] DR Ensembl; ENST00000472644.6; ENSP00000419236.2; ENSG00000170017.12. [Q13740-2] DR GeneID; 214; -. DR KEGG; hsa:214; -. DR MANE-Select; ENST00000306107.9; ENSP00000305988.5; NM_001627.4; NP_001618.2. DR UCSC; uc003dvx.4; human. [Q13740-1] DR AGR; HGNC:400; -. DR CTD; 214; -. DR DisGeNET; 214; -. DR GeneCards; ALCAM; -. DR HGNC; HGNC:400; ALCAM. DR HPA; ENSG00000170017; Tissue enriched (parathyroid). DR MIM; 601662; gene. DR neXtProt; NX_Q13740; -. DR OpenTargets; ENSG00000170017; -. DR PharmGKB; PA24691; -. DR VEuPathDB; HostDB:ENSG00000170017; -. DR eggNOG; ENOG502RMQM; Eukaryota. DR GeneTree; ENSGT00940000156881; -. DR InParanoid; Q13740; -. DR OMA; SLNVSAX; -. DR OrthoDB; 5351031at2759; -. DR PhylomeDB; Q13740; -. DR TreeFam; TF321859; -. DR PathwayCommons; Q13740; -. DR Reactome; R-HSA-373760; L1CAM interactions. DR SignaLink; Q13740; -. DR SIGNOR; Q13740; -. DR BioGRID-ORCS; 214; 13 hits in 1162 CRISPR screens. DR ChiTaRS; ALCAM; human. DR GeneWiki; ALCAM; -. DR GenomeRNAi; 214; -. DR Pharos; Q13740; Tbio. DR PRO; PR:Q13740; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q13740; Protein. DR Bgee; ENSG00000170017; Expressed in bronchial epithelial cell and 205 other cell types or tissues. DR ExpressionAtlas; Q13740; baseline and differential. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0048846; P:axon extension involved in axon guidance; ISS:UniProtKB. DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB. DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:UniProtKB. DR GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl. DR GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB. DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd00096; Ig; 2. DR DisProt; DP02515; -. DR Gene3D; 2.60.40.10; Immunoglobulins; 5. DR InterPro; IPR013162; CD80_C2-set. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR PANTHER; PTHR11973:SF2; CD166 ANTIGEN; 1. DR PANTHER; PTHR11973; CELL SURFACE GLYCOPROTEIN MUC18-RELATED; 1. DR Pfam; PF08205; C2-set_2; 1. DR Pfam; PF13927; Ig_3; 1. DR SMART; SM00409; IG; 3. DR SMART; SM00408; IGc2; 3. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; Immunoglobulin; 5. DR PROSITE; PS50835; IG_LIKE; 4. DR Genevisible; Q13740; HS. PE 1: Evidence at protein level; KW 3D-structure; Adaptive immunity; Alternative splicing; Cell adhesion; KW Cell membrane; Cell projection; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Immunity; Immunoglobulin domain; Membrane; KW Reference proteome; Repeat; Secreted; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..27 FT /evidence="ECO:0000255" FT CHAIN 28..583 FT /note="CD166 antigen" FT /id="PRO_0000014659" FT TOPO_DOM 28..527 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 528..549 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 550..583 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 28..120 FT /note="Ig-like V-type 1" FT DOMAIN 125..234 FT /note="Ig-like V-type 2" FT DOMAIN 245..328 FT /note="Ig-like C2-type 1" FT DOMAIN 333..409 FT /note="Ig-like C2-type 2" FT DOMAIN 416..501 FT /note="Ig-like C2-type 3" FT REGION 562..583 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 91 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 95 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 167 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519" FT CARBOHYD 265 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT CARBOHYD 306 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 361 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 457 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19349973" FT CARBOHYD 480 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 499 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:12754519, FT ECO:0000269|PubMed:16335952" FT DISULFID 43..113 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0007744|PDB:5A2F" FT DISULFID 157..220 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0007744|PDB:5A2F" FT DISULFID 270..313 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 354..392 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 435..485 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1..191 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053529" FT VAR_SEQ 132..133 FT /note="KQ -> SK (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15496415" FT /id="VSP_053530" FT VAR_SEQ 134..583 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15496415" FT /id="VSP_053531" FT VAR_SEQ 244..330 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053532" FT VAR_SEQ 503..516 FT /note="ISIPEHDEADEISD -> N (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3" FT /id="VSP_021797" FT VARIANT 229 FT /note="G -> D (in dbSNP:rs10933819)" FT /id="VAR_029514" FT VARIANT 258 FT /note="N -> S (in dbSNP:rs1044240)" FT /id="VAR_003907" FT VARIANT 301 FT /note="T -> M (in dbSNP:rs1044243)" FT /evidence="ECO:0000269|PubMed:7760007" FT /id="VAR_003908" FT VARIANT 315 FT /note="L -> M (in dbSNP:rs12629872)" FT /id="VAR_029515" FT VARIANT 352 FT /note="V -> M (in dbSNP:rs2291375)" FT /id="VAR_029516" FT VARIANT 367 FT /note="M -> I (in dbSNP:rs34926152)" FT /id="VAR_049856" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 51..59 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 65..72 FT /evidence="ECO:0007829|PDB:5A2F" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:5A2F" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:5A2F" FT TURN 87..89 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 98..102 FT /evidence="ECO:0007829|PDB:5A2F" FT HELIX 105..107 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 109..117 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 120..132 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 138..141 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 144..148 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 152..164 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 167..172 FT /evidence="ECO:0007829|PDB:5A2F" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 184..192 FT /evidence="ECO:0007829|PDB:5A2F" FT TURN 194..196 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 199..207 FT /evidence="ECO:0007829|PDB:5A2F" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 218..226 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 229..234 FT /evidence="ECO:0007829|PDB:5A2F" FT STRAND 241..243 FT /evidence="ECO:0007829|PDB:5A2F" SQ SEQUENCE 583 AA; 65102 MW; 68FEFD67C14B0C57 CRC64; MESKGASSCR LLFCLLISAT VFRPGLGWYT VNSAYGDTII IPCRLDVPQN LMFGKWKYEK PDGSPVFIAF RSSTKKSVQY DDVPEYKDRL NLSENYTLSI SNARISDEKR FVCMLVTEDN VFEAPTIVKV FKQPSKPEIV SKALFLETEQ LKKLGDCISE DSYPDGNITW YRNGKVLHPL EGAVVIIFKK EMDPVTQLYT MTSTLEYKTT KADIQMPFTC SVTYYGPSGQ KTIHSEQAVF DIYYPTEQVT IQVLPPKNAI KEGDNITLKC LGNGNPPPEE FLFYLPGQPE GIRSSNTYTL TDVRRNATGD YKCSLIDKKS MIASTAITVH YLDLSLNPSG EVTRQIGDAL PVSCTISASR NATVVWMKDN IRLRSSPSFS SLHYQDAGNY VCETALQEVE GLKKRESLTL IVEGKPQIKM TKKTDPSGLS KTIICHVEGF PKPAIQWTIT GSGSVINQTE ESPYINGRYY SKIIISPEEN VTLTCTAENQ LERTVNSLNV SAISIPEHDE ADEISDENRE KVNDQAKLIV GIVVGLLLAA LVAGVVYWLY MKKSKTASKH VNKDLGNMEE NKKLEENNHK TEA //