ID U3JIE0_FICAL Unreviewed; 540 AA.
AC U3JIE0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Vascular cell adhesion molecule 1 {ECO:0000313|Ensembl:ENSFALP00000002544.1};
GN Name=VCAM1 {ECO:0000313|Ensembl:ENSFALP00000002544.1};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000002544.1, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000002544.1, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000002544.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_005050495.1; XM_005050438.1.
DR AlphaFoldDB; U3JIE0; -.
DR STRING; 59894.ENSFALP00000002544; -.
DR Ensembl; ENSFALT00000002556.2; ENSFALP00000002544.1; ENSFALG00000002444.2.
DR GeneID; 101820418; -.
DR KEGG; fab:101820418; -.
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; UP000016665; Chromosome 8.
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; 5.
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:SF9; INTERCELLULAR ADHESION MOLECULE 5; 1.
DR Pfam; PF05790; C2-set; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 2.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR PRINTS; PR01472; ICAMVCAM1.
DR PRINTS; PR01474; VCAM1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR PROSITE; PS50835; IG_LIKE; 4.
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:UP000016665};
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..540
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004645432"
FT TRANSMEM 497..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..110
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 223..307
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 314..397
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 402..484
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 540 AA; 59347 MW; D313B75EE5087804 CRC64;
MLKEMGRTSL AVLVILCVLR TVKAFEMEIL PAERTVAQIG GTLILTCNTT GCASPSFSWR
TQMDSPLGGK VSNYRTHSTL TMNPVSIVNS HSYLCTVVCD DREKKEKSIE VELYSFPSDP
VIEISPSLVA GEQATVICKI PDVYPSHHLE VLLKKDEHVL HEKNFFEDDS TNTETKIVTH
TFHPTAKDIG KEITCVARLL IADMDFEPKE RTSSQKLNAN FGPQNTVIAA SPGNSPMEGD
TLNLTCVTQS NPPAKIVWSK YLAEESIQHL IKNNVLSIPH VHFNDSGRYI CEAINPITNK
TEKAAMDIII QGAPVITKLS IEPSTTVQEG ENVSIQCSAE SNPPPKIILR RKSDNADMRA
YSARNILLPS VMFQNGGDYE CLAENKFGKS KSEITLNVKY GPKNTMITVI PTAALKEGET
VTMKCTSSGN PAPVISWKKK KANGESEKIS KNATLTIWNL QSQDLGLYEC EAYNQFGKEE
KAVKLYVQGL EEPDQTIPLI IAFSSVAAVV VPAVAILIYV SRQAKINGSY SLVKALRLKV
//
