VCAM1_CANLF
ID VCAM1_CANLF Reviewed; 739 AA.
AC Q28260;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Vascular cell adhesion protein 1;
DE Short=V-CAM 1;
DE Short=VCAM-1;
DE AltName: CD_antigen=CD106;
DE Flags: Precursor;
GN Name=VCAM1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Ballantyne C.M., Clubb F.J., Perrard J.L., Radovencovic B., Youker K.A.,
RA Smith C.W., Entman M.L., Hawkins H.K., Frazier O.H., Willerson J.T.;
RT "Increased expression of VCAM-1 and ICAM-1 in early cardiac allograft
RT arteriopathy in the dog.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: Either the first or the fourth Ig-like C2-type domain is
CC required for VLA4-dependent cell adhesion. {ECO:0000250}.
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DR EMBL; U32086; AAA84866.1; -; mRNA.
DR RefSeq; NP_001003298.1; NM_001003298.1.
DR AlphaFoldDB; Q28260; -.
DR SMR; Q28260; -.
DR STRING; 9612.ENSCAFP00000029643; -.
DR PaxDb; Q28260; -.
DR GeneID; 403982; -.
DR KEGG; cfa:403982; -.
DR CTD; 7412; -.
DR eggNOG; ENOG502QSKQ; Eukaryota.
DR InParanoid; Q28260; -.
DR OrthoDB; 544376at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
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; 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; 2.
DR Pfam; PF00047; ig; 1.
DR PRINTS; PR01472; ICAMVCAM1.
DR PRINTS; PR01474; VCAM1.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 7.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..739
FT /note="Vascular cell adhesion protein 1"
FT /id="PRO_0000014996"
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 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 52..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 137..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
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"
SQ SEQUENCE 739 AA; 81412 MW; BB5DA3853739C615 CRC64;
MPRKMVVIFG ASNILWMVFA VSQASKMEIF LEPRVAAQIG DVISLTCSTT GCETPSFSWR
TQIDSPLNGK VKNEGNNSTL TMDPVSFNNE HAYLCTATCG SKKLEKGIQV EIYSFPKDPE
IQLSGPLEVG KPVTVTCLVR DVYPFDRLEM NLLNGNDLLQ SKDFLEPMEK KSLETKSLEV
TFTPTNEDIG KGLVCRAQLH MDEIDFEPKE RETTKELQVY ISPRNTFISV TPSMRLQEGG
SVTMTCASEG LPPPQIFWSK KLDNGNLQLL SGNATLTLIA MRLEDSGTYV CEGVNEVGKD
GKEVELIVQE KPFTVEISPG PQIIAQIGDS VVLTCGVTDC ESPSFSWRTQ IDSPLSGTVK
VEGAKSTLTL SPVNLENEHS YLCTVTCGHK KLEKGIKVDL YSFPRDPEVE MSGLLVDGNP
VTVSCEVPNV YPSDRLEIEL FKGETIIESK SFLEDMDKKS LETKSLEMTF IPTTEDTGKV
LVCLAKLHID EMEFEPKQRQ STQTLYVNVA PRDTTVVVSP SSIVEEGSPV NMTCSSDGLP
APNILWSRRL SNGRLQSLSE DPILTLTSAK MEDSGIYVCE GINQAGISRK EVELIIQVAP
KDIQLIAFPS ESVKEGDTVI ISCTCGNVPK TWIILKKKAE TGDTVLKSRD GAYTIHKVQL
EDAGVYECES KNEAGLQLRS LTLDVKGREN NKDYFSPELL VLYCASSLII PAIGMIIYFA
RRANMKGSYS LVEAQKSKV
