ID VCAM1_HUMAN Reviewed; 739 AA. AC P19320; A8K6R7; B4DKS4; E9PDD1; Q6NUP8; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 24-JAN-2024, entry version 257. DE RecName: Full=Vascular cell adhesion protein 1; DE Short=V-CAM 1; DE Short=VCAM-1; DE AltName: Full=INCAM-100; DE AltName: CD_antigen=CD106; DE Contains: DE RecName: Full=Soluble Vascular Cell Adhesion Molecule-1; DE Flags: Precursor; GN Name=VCAM1; 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 2). RX PubMed=2688898; DOI=10.1016/0092-8674(89)90775-7; RA Osborn L., Hession C., Tizard R., Vassallo C., Luhowskyj S., Chi-Rosso G., RA Lobb R.; RT "Direct expression cloning of vascular cell adhesion molecule 1, a RT cytokine-induced endothelial protein that binds to lymphocytes."; RL Cell 59:1203-1211(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Umbilical vein; RX PubMed=1699207; DOI=10.1093/nar/18.19.5901; RA Polte T., Newman W., Gopal T.V.; RT "Full length vascular cell adhesion molecule 1 (VCAM-1)."; RL Nucleic Acids Res. 18:5901-5901(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1707873; DOI=10.1016/s0021-9258(20)89551-9; RA Hession C., Tizard R., Vassallo C., Schiffer S.B., Goff D., Moy P., RA Chi-Rosso G., Luhowskyj S., Lobb R., Osborn L.; RT "Cloning of an alternate form of vascular cell adhesion molecule-1 RT (VCAM1)."; RL J. Biol. Chem. 266:6682-6685(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND ALTERNATIVE SPLICING. RX PubMed=1715583; DOI=10.1073/pnas.88.17.7859; RA Cybulsky M.I., Fries J.W.U., Williams A.J., Sultan P., Eddy R., Byers M., RA Shows T., Gimbrone M.A. Jr., Collins T.; RT "Gene structure, chromosomal location, and basis for alternative mRNA RT splicing of the human VCAM1 gene."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7859-7863(1991). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PHE-318; ALA-384; ALA-413 RP AND LEU-716. RG SeattleSNPs variation discovery resource; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Placenta, and Tongue; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Retinal pigment epithelium; 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 [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. RX PubMed=1379595; DOI=10.1016/s0021-9258(18)42004-2; RA Iademarco M.F., McQuillan J.J., Rosen G.D., Dean D.C.; RT "Characterization of the promoter for vascular cell adhesion molecule-1 RT (VCAM-1)."; RL J. Biol. Chem. 267:16323-16329(1992). RN [11] RP NUCLEOTIDE SEQUENCE OF 25-686 (ISOFORMS 1 AND 2). RC TISSUE=Umbilical vein endothelial cell; RX PubMed=1707234; RA Cybulsky M.I., Fries J.W., Williams A.J., Sultan P., Davis V.M., RA Gimbrone M.A. Jr., Collins T.; RT "Alternative splicing of human VCAM-1 in activated vascular endothelium."; RL Am. J. Pathol. 138:815-820(1991). RN [12] RP NUCLEOTIDE SEQUENCE OF 25-402 (ISOFORMS 1 AND 2), AND CELL ADHESION DOMAIN. RC TISSUE=Endothelial cell; RX PubMed=1377228; DOI=10.1084/jem.176.1.99; RA Osborn L., Vassallo C., Benjamin C.D.; RT "Activated endothelium binds lymphocytes through a novel binding site in RT the alternately spliced domain of vascular cell adhesion molecule-1."; RL J. Exp. Med. 176:99-107(1992). RN [13] RP FUNCTION. RX PubMed=10209034; DOI=10.1083/jcb.145.2.413; RA Taooka Y., Chen J., Yednock T., Sheppard D.; RT "The integrin alpha9beta1 mediates adhesion to activated endothelial cells RT and transendothelial neutrophil migration through interaction with vascular RT cell adhesion molecule-1."; RL J. Cell Biol. 145:413-420(1999). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE. RX PubMed=12878595; DOI=10.1074/jbc.m305877200; RA Garton K.J., Gough P.J., Philalay J., Wille P.T., Blobel C.P., RA Whitehead R.H., Dempsey P.J., Raines E.W.; RT "Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is RT mediated by tumor necrosis factor-alpha-converting enzyme (ADAM 17)."; RL J. Biol. Chem. 278:37459-37464(2003). RN [15] RP PROTEIN SEQUENCE OF 25-39. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-561. 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 [17] RP FUNCTION, AND MUTAGENESIS OF SER-730 AND SER-737. RX PubMed=22970700; DOI=10.1021/bi300925r; RA Marchese M.E., Berdnikovs S., Cook-Mills J.M.; RT "Distinct sites within the vascular cell adhesion molecule-1 (VCAM-1) RT cytoplasmic domain regulate VCAM-1 activation of calcium fluxes versus Rac1 RT during leukocyte transendothelial migration."; RL Biochemistry 51:8235-8246(2012). RN [18] RP FUNCTION, AND UBIQUITINATION BY TRIM65. RX PubMed=31310649; DOI=10.1093/jmcb/mjz077; RA Li Y., Huang X., Guo F., Lei T., Li S., Monaghan-Nichols P., Jiang Z., RA Xin H.B., Fu M.; RT "TRIM65 E3 ligase targets VCAM-1 degradation to limit LPS-induced lung RT inflammation."; RL J. Mol. Cell Biol. 12:190-201(2020). RN [19] RP SUBCELLULAR LOCATION. RX PubMed=36127634; DOI=10.1186/s12885-022-10096-3; RA Heo S.K., Noh E.K., Lee Y.J., Shin Y., Kim Y., Im H.S., Kim H., Koh S.J., RA Min Y.J., Jo J.C., Choi Y.; RT "The soluble VCAM-1 level is a potential biomarker predicting severe acute RT graft versus host disease after allogeneic hematopoietic cell RT transplantation."; RL BMC Cancer 22:997-997(2022). RN [20] RP FUNCTION. RX PubMed=35210567; DOI=10.1038/s41556-022-00849-4; RA Pinho S., Wei Q., Maryanovich M., Zhang D., Balandran J.C., Pierce H., RA Nakahara F., Di Staulo A., Bartholdy B.A., Xu J., Borger D.K., Verma A., RA Frenette P.S.; RT "VCAM1 confers innate immune tolerance on haematopoietic and leukaemic stem RT cells."; RL Nat. Cell Biol. 24:290-298(2022). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 25-226. RX PubMed=7531291; DOI=10.1038/373539a0; RA Jones E.Y., Harlos K., Bottomley M.J., Robinson R.C., Driscoll P.C., RA Edwards R.M., Clements J.M., Dudgeon T.J., Stuart D.I.; RT "Crystal structure of an integrin-binding fragment of vascular cell RT adhesion molecule-1 at 1.8-A resolution."; RL Nature 373:539-544(1995). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 25-219, AND DISULFIDE BONDS. RX PubMed=7539925; DOI=10.1073/pnas.92.12.5714; RA Wang J.-H., Pepinsky R.B., Stehle T., Liu J.-H., Karpusas M., Browning B., RA Osborn L.; RT "The crystal structure of an N-terminal two-domain fragment of vascular RT cell adhesion molecule 1 (VCAM-1): a cyclic peptide based on the domain 1 RT C-D loop can inhibit VCAM-1-alpha 4 integrin interaction."; RL Proc. Natl. Acad. Sci. U.S.A. 92:5714-5718(1995). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-220. RX PubMed=15299708; DOI=10.1107/s0907444995012352; RA Wang J.-H., Stehle T., Pepinsky R.B., Liu J.-H., Karpusas M., Osborn L.; RT "Structure of a functional fragment of VCAM-1 refined at 1.9-A RT resolution."; RL Acta Crystallogr. D 52:369-379(1996). CC -!- FUNCTION: Cell adhesion glycoprotein predominantly expressed on the CC surface of endothelial cells that plays an important role in immune CC surveillance and inflammation (PubMed:31310649). Acts as a major CC regulator of leukocyte adhesion to the endothelium through interaction CC with different types of integrins (PubMed:10209034). During CC inflammatory responses, binds ligands on the surface of activated CC endothelial cells to initiate the activation of calcium channels and CC the plasma membrane-associated small GTPase RAC1 leading to leukocyte CC transendothelial migration (PubMed:22970700). Serves also as a quality- CC control checkpoint for entry into bone marrow by providing a 'don't- CC eat-me' stamping in the context of major histocompatibility complex CC (MHC) class-I presentation (PubMed:35210567). CC {ECO:0000269|PubMed:10209034, ECO:0000269|PubMed:22970700, CC ECO:0000269|PubMed:31310649, ECO:0000269|PubMed:35210567}. CC -!- SUBCELLULAR LOCATION: [Vascular cell adhesion protein 1]: Cell membrane CC {ECO:0000305|PubMed:12878595}; Single-pass type I membrane protein. CC -!- SUBCELLULAR LOCATION: [Soluble Vascular Cell Adhesion Molecule-1]: CC Secreted {ECO:0000269|PubMed:12878595, ECO:0000269|PubMed:36127634}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=Long, VCAM-7D; CC IsoId=P19320-1; Sequence=Displayed; CC Name=2; Synonyms=Short, VCAM-6D; CC IsoId=P19320-2; Sequence=VSP_002580; CC Name=3; CC IsoId=P19320-3; Sequence=VSP_044636; CC -!- TISSUE SPECIFICITY: Expressed on inflamed vascular endothelium, as well CC as on macrophage-like and dendritic cell types in both normal and CC inflamed tissue. CC -!- INDUCTION: By pro-inflammatory cytokines, including TNFalpha, and also CC by ROS, oxidized low density lipoprotein, high glucose concentration, CC toll-like receptor agonists, and shear stress. CC -!- DOMAIN: Either the first or the fourth Ig-like C2-type domain is CC required for VLA4-dependent cell adhesion. CC -!- PTM: Cleaved by the metalloproteinase ADAM17 to generate the soluble CC form. {ECO:0000269|PubMed:12878595}. CC -!- PTM: Sialoglycoprotein. CC -!- PTM: Ubiquitinated by TRIM65 via 'Lys-48'-linked ubiquitination; CC leading to proteasomal degradation. {ECO:0000269|PubMed:31310649}. CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform. CC -!- WEB RESOURCE: Name=Wikipedia; Note=VCAM1 entry; CC URL="https://en.wikipedia.org/wiki/VCAM1"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/vcam1/"; CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=VCAM-1; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_266"; 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; M30257; AAA51917.1; -; mRNA. DR EMBL; X53051; CAA37218.1; -; mRNA. DR EMBL; M60335; AAA61269.1; -; mRNA. DR EMBL; M73255; AAA61270.1; -; Genomic_DNA. DR EMBL; AF536818; AAM96190.1; -; Genomic_DNA. DR EMBL; AK291732; BAF84421.1; -; mRNA. DR EMBL; AK296692; BAG59286.1; -; mRNA. DR EMBL; AC093428; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471097; EAW72950.1; -; Genomic_DNA. DR EMBL; BC017276; AAH17276.3; -; mRNA. DR EMBL; BC068490; AAH68490.2; -; mRNA. DR EMBL; BC085003; AAH85003.1; -; mRNA. DR EMBL; M92431; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS55617.1; -. [P19320-3] DR CCDS; CCDS773.1; -. [P19320-1] DR CCDS; CCDS774.1; -. [P19320-2] DR PIR; A41288; A41288. DR PIR; B41288; B41288. DR RefSeq; NP_001069.1; NM_001078.3. [P19320-1] DR RefSeq; NP_001186763.1; NM_001199834.1. [P19320-3] DR RefSeq; NP_542413.1; NM_080682.2. [P19320-2] DR PDB; 1IJ9; X-ray; 3.00 A; A=25-220. DR PDB; 1VCA; X-ray; 1.80 A; A/B=25-226. DR PDB; 1VSC; X-ray; 1.90 A; A/B=25-219. DR PDBsum; 1IJ9; -. DR PDBsum; 1VCA; -. DR PDBsum; 1VSC; -. DR AlphaFoldDB; P19320; -. DR SMR; P19320; -. DR BioGRID; 113255; 466. DR CORUM; P19320; -. DR IntAct; P19320; 639. DR MINT; P19320; -. DR STRING; 9606.ENSP00000294728; -. DR BindingDB; P19320; -. DR ChEMBL; CHEMBL3735; -. DR DrugBank; DB01136; Carvedilol. DR DrugBank; DB11338; Clove oil. DR DrugBank; DB00898; Ethanol. DR DrugBank; DB05399; Succinobucol. DR GlyConnect; 1984; 6 N-Linked glycans (2 sites). DR GlyCosmos; P19320; 10 sites, 7 glycans. DR GlyGen; P19320; 10 sites, 6 N-linked glycans (2 sites), 1 O-linked glycan (3 sites). DR iPTMnet; P19320; -. DR PhosphoSitePlus; P19320; -. DR BioMuta; VCAM1; -. DR DMDM; 137560; -. DR CPTAC; CPTAC-5950; -. DR jPOST; P19320; -. DR MassIVE; P19320; -. DR MaxQB; P19320; -. DR PaxDb; 9606-ENSP00000294728; -. DR PeptideAtlas; P19320; -. DR ProteomicsDB; 19636; -. DR ProteomicsDB; 53645; -. [P19320-1] DR ProteomicsDB; 53646; -. [P19320-2] DR ABCD; P19320; 2 sequenced antibodies. DR Antibodypedia; 3955; 2396 antibodies from 52 providers. DR CPTC; P19320; 1 antibody. DR DNASU; 7412; -. DR Ensembl; ENST00000294728.7; ENSP00000294728.2; ENSG00000162692.12. [P19320-1] DR Ensembl; ENST00000347652.6; ENSP00000304611.2; ENSG00000162692.12. [P19320-2] DR Ensembl; ENST00000370119.8; ENSP00000359137.3; ENSG00000162692.12. [P19320-3] DR GeneID; 7412; -. DR KEGG; hsa:7412; -. DR MANE-Select; ENST00000294728.7; ENSP00000294728.2; NM_001078.4; NP_001069.1. DR UCSC; uc001dti.5; human. [P19320-1] DR AGR; HGNC:12663; -. DR CTD; 7412; -. DR DisGeNET; 7412; -. DR GeneCards; VCAM1; -. DR HGNC; HGNC:12663; VCAM1. DR HPA; ENSG00000162692; Tissue enriched (lymphoid). DR MIM; 192225; gene. DR neXtProt; NX_P19320; -. DR OpenTargets; ENSG00000162692; -. DR PharmGKB; PA37286; -. DR VEuPathDB; HostDB:ENSG00000162692; -. DR eggNOG; ENOG502QSKQ; Eukaryota. DR GeneTree; ENSGT00940000156511; -. DR InParanoid; P19320; -. DR OMA; TYVCEGV; -. DR OrthoDB; 5359770at2759; -. DR PhylomeDB; P19320; -. DR TreeFam; TF333571; -. DR PathwayCommons; P19320; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SignaLink; P19320; -. DR SIGNOR; P19320; -. DR BioGRID-ORCS; 7412; 13 hits in 1156 CRISPR screens. DR ChiTaRS; VCAM1; human. DR EvolutionaryTrace; P19320; -. DR GeneWiki; VCAM-1; -. DR GenomeRNAi; 7412; -. DR Pharos; P19320; Tchem. DR PRO; PR:P19320; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P19320; Protein. DR Bgee; ENSG00000162692; Expressed in cartilage tissue and 181 other cell types or tissues. DR ExpressionAtlas; P19320; baseline and differential. DR GO; GO:0071065; C:alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex; IDA:BHF-UCL. DR GO; GO:0045177; C:apical part of cell; IDA:BHF-UCL. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0030175; C:filopodium; IDA:BHF-UCL. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0005902; C:microvillus; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0002102; C:podosome; IDA:BHF-UCL. DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl. DR GO; GO:0098631; F:cell adhesion mediator activity; IDA:UniProt. DR GO; GO:0050839; F:cell adhesion molecule binding; IDA:BHF-UCL. DR GO; GO:0005178; F:integrin binding; IDA:BHF-UCL. DR GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB. DR GO; GO:0009308; P:amine metabolic process; IDA:UniProtKB. DR GO; GO:0030183; P:B cell differentiation; IC:BHF-UCL. DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IGI:UniProtKB. DR GO; GO:0060945; P:cardiac neuron differentiation; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IDA:BHF-UCL. DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl. DR GO; GO:0140039; P:cell-cell adhesion in response to extracellular stimulus; IGI:ARUK-UCL. DR GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB. DR GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IEA:Ensembl. DR GO; GO:0002544; P:chronic inflammatory response; IEA:Ensembl. DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL. DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IGI:ARUK-UCL. DR GO; GO:0006954; P:inflammatory response; IDA:UniProt. DR GO; GO:0060384; P:innervation; IEA:Ensembl. DR GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL. DR GO; GO:0050901; P:leukocyte tethering or rolling; IDA:UniProtKB. DR GO; GO:0022614; P:membrane to membrane docking; IEP:BHF-UCL. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl. DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl. DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl. DR CDD; cd04979; Ig_Semaphorin_C; 1. DR CDD; cd07689; IgC2_VCAM-1; 2. DR CDD; cd20943; IgI_VCAM-1; 2. DR Gene3D; 2.60.40.10; Immunoglobulins; 7. DR InterPro; IPR047012; ICAM_VCAM. DR InterPro; IPR003987; ICAM_VCAM_N. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR008424; Ig_C2-set. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR013151; Immunoglobulin. DR InterPro; IPR003989; VCAM-1. DR PANTHER; PTHR13771; INTERCELLULAR ADHESION MOLECULE; 1. DR PANTHER; PTHR13771:SF14; VASCULAR CELL ADHESION PROTEIN 1; 1. DR Pfam; PF05790; C2-set; 2. DR Pfam; PF07679; I-set; 2. DR Pfam; PF00047; ig; 1. DR Pfam; PF13927; Ig_3; 2. DR PRINTS; PR01472; ICAMVCAM1. DR PRINTS; PR01474; VCAM1. DR SMART; SM00409; IG; 5. DR SMART; SM00408; IGc2; 5. DR SMART; SM00406; IGv; 2. DR SUPFAM; SSF48726; Immunoglobulin; 7. DR PROSITE; PS50835; IG_LIKE; 5. DR Genevisible; P19320; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Secreted; KW Signal; Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1..24 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 25..739 FT /note="Vascular cell adhesion protein 1" FT /id="PRO_0000014997" FT CHAIN 25..? FT /note="Soluble Vascular Cell Adhesion Molecule-1" FT /id="PRO_0000457762" FT TOPO_DOM 25..698 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 699..720 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 721..739 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 25..105 FT /note="Ig-like C2-type 1" FT DOMAIN 109..212 FT /note="Ig-like C2-type 2" FT DOMAIN 223..309 FT /note="Ig-like C2-type 3" FT DOMAIN 312..399 FT /note="Ig-like C2-type 4" FT DOMAIN 408..506 FT /note="Ig-like C2-type 5" FT DOMAIN 511..595 FT /note="Ig-like C2-type 6" FT DOMAIN 600..684 FT /note="Ig-like C2-type 7" FT CARBOHYD 273 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 365 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 417 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 463 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 531 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 561 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952" FT DISULFID 47..95 FT /evidence="ECO:0000269|PubMed:7539925" FT DISULFID 52..99 FT /evidence="ECO:0000269|PubMed:7539925" FT DISULFID 137..195 FT /evidence="ECO:0000269|PubMed:7539925" FT DISULFID 246..291 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 335..383 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 534..579 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 52..113 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044636" FT VAR_SEQ 310..402 FT /note="EKPFTVEISPGPRIAAQIGDSVMLTCSVMGCESPSFSWRTQIDSPLSGKVRS FT EGTNSTLTLSPVSFENEHSYLCTVTCGHKKLEKGIQVELYS -> A (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:2688898" FT /id="VSP_002580" FT VARIANT 18 FT /note="M -> I (in dbSNP:rs34228330)" FT /id="VAR_049951" FT VARIANT 318 FT /note="S -> F (in dbSNP:rs3783611)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_014309" FT VARIANT 384 FT /note="T -> A (in dbSNP:rs3783612)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_014310" FT VARIANT 413 FT /note="G -> A (in dbSNP:rs3783613)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_014311" FT VARIANT 421 FT /note="V -> I (in dbSNP:rs34100871)" FT /id="VAR_049952" FT VARIANT 488 FT /note="H -> R (in dbSNP:rs34199378)" FT /id="VAR_049953" FT VARIANT 716 FT /note="I -> L (in dbSNP:rs3783615)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_014312" FT MUTAGEN 730 FT /note="S->A: Loss of RAC1 activation and subsequent FT leukocyte transmigration." FT /evidence="ECO:0000269|PubMed:22970700" FT MUTAGEN 737 FT /note="S->A: Loss of RAC1 activation and subsequent FT leukocyte transmigration." FT /evidence="ECO:0000269|PubMed:22970700" FT CONFLICT 182 FT /note="F -> G (in Ref. 12)" FT /evidence="ECO:0000305" FT CONFLICT 402 FT /note="S -> T (in Ref. 11)" FT /evidence="ECO:0000305" FT CONFLICT 728 FT /note="S -> P (in Ref. 6; BAG59286)" FT /evidence="ECO:0000305" FT STRAND 26..38 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 43..51 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 68..74 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 77..84 FT /evidence="ECO:0007829|PDB:1VCA" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 91..99 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 102..114 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 120..125 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 133..144 FT /evidence="ECO:0007829|PDB:1VCA" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 148..154 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 157..163 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:1IJ9" FT STRAND 174..182 FT /evidence="ECO:0007829|PDB:1VCA" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 192..199 FT /evidence="ECO:0007829|PDB:1VCA" FT STRAND 209..216 FT /evidence="ECO:0007829|PDB:1VCA" SQ SEQUENCE 739 AA; 81276 MW; 050E2EBD39AC2FF4 CRC64; MPGKMVVILG ASNILWIMFA ASQAFKIETT PESRYLAQIG DSVSLTCSTT GCESPFFSWR TQIDSPLNGK VTNEGTTSTL TMNPVSFGNE HSYLCTATCE SRKLEKGIQV EIYSFPKDPE IHLSGPLEAG KPITVKCSVA DVYPFDRLEI DLLKGDHLMK SQEFLEDADR KSLETKSLEV TFTPVIEDIG KVLVCRAKLH IDEMDSVPTV RQAVKELQVY ISPKNTVISV NPSTKLQEGG SVTMTCSSEG LPAPEIFWSK KLDNGNLQHL SGNATLTLIA MRMEDSGIYV CEGVNLIGKN RKEVELIVQE KPFTVEISPG PRIAAQIGDS VMLTCSVMGC ESPSFSWRTQ IDSPLSGKVR SEGTNSTLTL SPVSFENEHS YLCTVTCGHK KLEKGIQVEL YSFPRDPEIE MSGGLVNGSS VTVSCKVPSV YPLDRLEIEL LKGETILENI EFLEDTDMKS LENKSLEMTF IPTIEDTGKA LVCQAKLHID DMEFEPKQRQ STQTLYVNVA PRDTTVLVSP SSILEEGSSV NMTCLSQGFP APKILWSRQL PNGELQPLSE NATLTLISTK MEDSGVYLCE GINQAGRSRK EVELIIQVTP KDIKLTAFPS ESVKEGDTVI ISCTCGNVPE TWIILKKKAE TGDTVLKSID GAYTIRKAQL KDAGVYECES KNKVGSQLRS LTLDVQGREN NKDYFSPELL VLYFASSLII PAIGMIIYFA RKANMKGSYS LVEAQKSKV //