VCAM1_HUMAN
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 03-AUG-2022, entry version 249.
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 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 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 [14]
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 [15]
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 [16]
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 [17]
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: Important in cell-cell recognition. Appears to function in
CC leukocyte-endothelial cell adhesion. Interacts with integrin alpha-
CC 4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both adhesion and
CC signal transduction. The VCAM1/ITGA4/ITGB1 interaction may play a
CC pathophysiologic role both in immune responses and in leukocyte
CC emigration to sites of inflammation.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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 cytokines (e.g. IL-1, TNF-alpha).
CC -!- DOMAIN: Either the first or the fourth Ig-like C2-type domain is
CC required for VLA4-dependent cell adhesion.
CC -!- PTM: Sialoglycoprotein.
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";
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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; 465.
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 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 jPOST; P19320; -.
DR MassIVE; P19320; -.
DR MaxQB; P19320; -.
DR PaxDb; P19320; -.
DR PeptideAtlas; P19320; -.
DR PRIDE; P19320; -.
DR ProteomicsDB; 19636; -.
DR ProteomicsDB; 53645; -. [P19320-1]
DR ProteomicsDB; 53646; -. [P19320-2]
DR ABCD; P19320; 2 sequenced antibodies.
DR Antibodypedia; 3955; 2127 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 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; 544376at2759; -.
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; 11 hits in 1076 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 179 other tissues.
DR ExpressionAtlas; P19320; baseline and differential.
DR Genevisible; P19320; HS.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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:0002526; P:acute inflammatory response; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
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: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 Gene3D; 2.60.40.10; -; 7.
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:SF14; PTHR13771:SF14; 6.
DR Pfam; PF05790; C2-set; 2.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00047; ig; 1.
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; SSF48726; 7.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
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 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 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
