ID G1T1S9_RABIT Unreviewed; 828 AA.
AC G1T1S9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Ig-like domain-containing protein {ECO:0000259|PROSITE:PS50835};
GN Name=VCAM1 {ECO:0000313|Ensembl:ENSOCUP00000010056.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000010056.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000010056.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000010056.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000010056.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000010056.3};
RG Ensembl;
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}.
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; AAGW02001248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008262180.1; XM_008263958.2.
DR AlphaFoldDB; G1T1S9; -.
DR SMR; G1T1S9; -.
DR STRING; 9986.ENSOCUP00000010056; -.
DR PaxDb; 9986-ENSOCUP00000010056; -.
DR Ensembl; ENSOCUT00000011697.4; ENSOCUP00000010056.3; ENSOCUG00000011697.4.
DR GeneID; 100008901; -.
DR CTD; 7412; -.
DR eggNOG; ENOG502QSKQ; Eukaryota.
DR GeneTree; ENSGT00940000156511; -.
DR HOGENOM; CLU_022321_0_0_1; -.
DR InParanoid; G1T1S9; -.
DR OMA; TYVCEGV; -.
DR OrthoDB; 5359770at2759; -.
DR TreeFam; TF333571; -.
DR Proteomes; UP000001811; Chromosome 13.
DR Bgee; ENSOCUG00000011697; Expressed in lung and 16 other cell types or tissues.
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 CDD; cd07689; IgC2_VCAM-1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 8.
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; 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; 3.
DR PRINTS; PR01472; ICAMVCAM1.
DR PRINTS; PR01474; VCAM1.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; Immunoglobulin; 8.
DR PROSITE; PS50835; IG_LIKE; 6.
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:UP000001811};
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..828
FT /note="Ig-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003422695"
FT TRANSMEM 789..809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..105
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 312..399
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 504..595
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 600..682
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 689..773
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 828 AA; 91712 MW; 55883610BF039B3F CRC64;
MPGKMVLFFG VSTLLWMMIA ASQAFKIETF PESRSLAQIG DSVSLTCTTT GCASPTFSWR
TQIDSPLNGK VRSEGTTSTL TMDPVSFENE HSYLCTATCE SKKLEKGIQV EIYSFPKDPE
IHLSGPLEVG EPITVKCLVP DVYPFDRLEV DLLKGDYLMK KQDFLEDMDR KSLETKSLEV
TFIPVIEDIG KLLVCRAKLH IDEIDSEPKE RETTKELQVY ISPKNTVISV NPSTRLQEGG
SVTMTCSSEG LPVPEIFWSK KQDNGNLQRL SGNATLTLIA MRMEDSGIYV CEGVNQIGKS
RKEVELIVQE KPFTVEISPG PRIAAQIGDP VVLTCSVRGC ETPSFSWRTQ IDSPLSGKVT
SEGTKSLLTL SPVSFENEHS YLCTVTCGHK KLEKGIQVEL YSFPRDPEIE LSGPPVNGRP
VTVSCKVPNV YPFDRLEIEL LKGETMMKNK EFLEEEDKKS LETKSLEMTF IPTMEDTGKV
LVCQAKLHID EMEFEPKQRQ STQPLFVNVA PRDIAVWVSP SSIVEEGRSV NMTCSSYGLP
APKILWSRQL KNGDLQPLSE NTTLALISTK LEDSGIYVCE GINLAGKSRK EVELVIQVAP
KDIQLTAFPS KSVKEGDTVI ISCTCGNVPE TWIILKKKAE TGDTVLKSID GAYTIRKAQL
EDAGVYECES KNEVGSQLRS ITLDVKVPPR NTTISIYPSS NVKEGENITI TCKTFSHPPA
VIILKRIDLA NEITMCSKNG TFTLYHVTQS DTGVYVIRAS NEVGDDSGRI EISVMRRENS
KDYFSPELLV LYCASSLIIP AIGMIIYFAR KANMKGSYSL VEAQKSKV
//
