ID M3YKY1_MUSPF Unreviewed; 739 AA.
AC M3YKY1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Vascular cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSMPUP00000011988.1};
DE SubName: Full=Vascular cell adhesion protein 1 {ECO:0000313|RefSeq:XP_004775232.1};
GN Name=VCAM1 {ECO:0000313|Ensembl:ENSMPUP00000011988.1,
GN ECO:0000313|RefSeq:XP_004775232.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000011988.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000011988.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004775232.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004775232.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
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DR EMBL; AEYP01085876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01085877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004775232.1; XM_004775175.3.
DR STRING; 9669.ENSMPUP00000011988; -.
DR Ensembl; ENSMPUT00000012183.1; ENSMPUP00000011988.1; ENSMPUG00000012080.1.
DR GeneID; 101683254; -.
DR KEGG; mpuf:101683254; -.
DR CTD; 7412; -.
DR eggNOG; ENOG502QSKQ; Eukaryota.
DR GeneTree; ENSGT00940000156511; -.
DR HOGENOM; CLU_022321_0_0_1; -.
DR OMA; TYVCEGV; -.
DR OrthoDB; 5359770at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0071065; C:alpha9-beta1 integrin-vascular cell adhesion molecule-1 complex; IEA:Ensembl.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0002102; C:podosome; IEA:Ensembl.
DR GO; GO:0098631; F:cell adhesion mediator activity; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:Ensembl.
DR GO; GO:0009308; P:amine metabolic process; IEA:Ensembl.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IEA:Ensembl.
DR GO; GO:0140039; P:cell-cell adhesion in response to extracellular stimulus; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IEA:Ensembl.
DR GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR CDD; cd00096; Ig; 1.
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; 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; PF13927; Ig_3; 3.
DR PRINTS; PR01472; ICAMVCAM1.
DR PRINTS; PR01474; VCAM1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; Immunoglobulin; 7.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..739
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041118199"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..105
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 223..309
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 312..397
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 511..595
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 600..684
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 739 AA; 81519 MW; 3A0F7205C46D43EB CRC64;
MPGKMVVIFG ASNVLWMVFT VSQAFKMEIF PEHRVIAQIG DVISLTCRTT GCEPPSFSWR
TQIDSPLNGK VRNEGNNSTL TMDPVSFNNE HAYVCTATCG SKKLEKGIQV EIYSFPKDPE
IHLSGPLELG KPVTVTCMVP DVYPFDRLEV NLMKDNKLLK NQEFLEPMER KSLETKSLVV
TFIPTNEDIG KALVCQAKLN IDEFDFEPKE RETTKKLQVY ISPKNTVISV SPSTKLQEGG
SVTMTCSSEG FPAPQIFWSK KLDNGNVQLL SGNATLTLIA MRIEDSGIYV CEGVNQVGKD
GKEVELIVQE KPFIVEISPG PQVIAQIGDS VVLTCGVTGC ESPSFSWRTQ IDSPLSGQVK
TEGSKSTLTL SPVSFENEHS YLCTVTCGRK KLEKRISVDL YSFPRDPEIE MSGLLVSGNP
VTVSCEVPNV YPSDRLEIEL FKGESVIESK TFLEDMDRKS LETKSLDMTF IPTTEDTGKV
LVCLAQLRVG EMEFEPKQRQ STRMLHVNVA PRDTTILVSP SSILEEGSSV NMTCSSNGLP
APKILWSRQL SNGDLQPLSE NSTLTLTSTK MDDSGIYVCE GINQAGISRK EVELIIQVAP
KDIQLTAFPS ESVKEGDTVI ISCTCGNVPK TWIILKKKAE TGDTVLKSRD GAYTIHKVQL
EDAGVYECES KNEVGLQLRS LTLDVKGREN NKDYFSPELL VLYCASSLII PAIGMIIYFA
RRANMKGSYS LVEAQKSKV
//