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ICAM1_GORGO
ID   ICAM1_GORGO             Reviewed;         532 AA.
AC   Q5NKV9;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Intercellular adhesion molecule 1;
DE            Short=ICAM-1;
DE   AltName: CD_antigen=CD54;
DE   Flags: Precursor;
GN   Name=ICAM1;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Isolate Kudzu, and Isolate Rok; TISSUE=Blood;
RA   Messier W., Walter N.A.R., Hink R.L.;
RT   "The chimpanzee ICAM proteins have been positively selected.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein
CC       LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial
CC       migration, ICAM1 engagement promotes the assembly of endothelial apical
CC       cups through ARHGEF26/SGEF and RHOG activation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with MUC1 and promotes cell aggregation
CC       in epithelial cells. Interacts with ARHGEF26/SGEF. Interacts (on T cell
CC       side) with CD81, CD247 and CD9 at immunological synapses between
CC       antigen-presenting cells and T cells. {ECO:0000250|UniProtKB:P05362}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to
CC       endocytosis. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC       {ECO:0000305}.
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DR   EMBL; AF340036; AAQ14899.1; -; mRNA.
DR   EMBL; AF340037; AAQ14900.1; -; mRNA.
DR   RefSeq; NP_001266532.1; NM_001279603.1.
DR   AlphaFoldDB; Q5NKV9; -.
DR   SMR; Q5NKV9; -.
DR   STRING; 9593.ENSGGOP00000005852; -.
DR   Ensembl; ENSGGOT00000064956; ENSGGOP00000038077; ENSGGOG00000005980.
DR   GeneID; 101127502; -.
DR   KEGG; ggo:101127502; -.
DR   CTD; 3383; -.
DR   eggNOG; ENOG502RZRA; Eukaryota.
DR   GeneTree; ENSGT00940000162311; -.
DR   HOGENOM; CLU_036160_1_1_1; -.
DR   InParanoid; Q5NKV9; -.
DR   OMA; NLTVYWF; -.
DR   OrthoDB; 731140at2759; -.
DR   Proteomes; UP000001519; Chromosome 19.
DR   Bgee; ENSGGOG00000005980; Expressed in liver and 6 other tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0061028; P:establishment of endothelial barrier; IEA:Ensembl.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0022614; P:membrane to membrane docking; IEA:Ensembl.
DR   GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR   GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0002693; P:positive regulation of cellular extravasation; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IEA:Ensembl.
DR   GO; GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl.
DR   GO; GO:0002291; P:T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IEA:Ensembl.
DR   GO; GO:0002457; P:T cell antigen processing and presentation; IEA:Ensembl.
DR   GO; GO:0072683; P:T cell extravasation; IEA:Ensembl.
DR   Gene3D; 2.60.40.10; -; 5.
DR   InterPro; IPR003988; ICAM.
DR   InterPro; IPR013768; ICAM_N.
DR   InterPro; IPR003987; ICAM_VCAM_N.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   Pfam; PF03921; ICAM_N; 1.
DR   PRINTS; PR01473; ICAM.
DR   PRINTS; PR01472; ICAMVCAM1.
DR   SMART; SM00409; IG; 3.
DR   SUPFAM; SSF48726; SSF48726; 5.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..532
FT                   /note="Intercellular adhesion molecule 1"
FT                   /id="PRO_0000014782"
FT   TOPO_DOM        28..480
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        481..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        504..532
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          41..103
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          128..193
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          230..297
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          325..378
FT                   /note="Ig-like C2-type 4"
FT   DOMAIN          412..464
FT                   /note="Ig-like C2-type 5"
FT   MOTIF           152..154
FT                   /note="Cell attachment site; atypical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         521
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P05362"
FT   MOD_RES         530
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P05362"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..92
FT                   /evidence="ECO:0000250|UniProtKB:P05362"
FT   DISULFID        52..96
FT                   /evidence="ECO:0000250|UniProtKB:P05362"
FT   DISULFID        135..186
FT                   /evidence="ECO:0000250|UniProtKB:P05362"
FT   DISULFID        237..290
FT                   /evidence="ECO:0000250|UniProtKB:P05362"
FT   DISULFID        332..371
FT                   /evidence="ECO:0000250|UniProtKB:P05362"
FT   DISULFID        403..419
FT                   /evidence="ECO:0000250|UniProtKB:P05362"
FT   DISULFID        419..457
FT                   /evidence="ECO:0000250"
FT   DISULFID        431..457
FT                   /evidence="ECO:0000250|UniProtKB:P05362"
SQ   SEQUENCE   532 AA;  57848 MW;  53D400591CCE0B52 CRC64;
     MAPSSPRPAL PALLVLLGAL FPGPGNAQTS VSPPKVILPR GGSVLVTCST SCDQPTLLGI
     ETPLPKKELL LLGNNQKVYE LSNVQEDSQP MCYSNCPDGQ STAKTFLTVY WTPERVELAP
     LPSWQPVGKD LTLRCQVEGG APRANLIVVL LRGEEELKRE PAVGEPAEVT TTVPVEKDHH
     GANFLCRTEL DLRPQGLKLF ENTSAPYQLQ TFVLPATPPQ LVSPRVLEVD TQGTVVCSLD
     GLFPVSEAQV HLALGDQRLN PTVTYGNDSF SAKASVSVTA EDEGTQWLTC AVILGTQSQE
     TLQTVTIYSF PAPNVILTKP EVSEGTEVTV KCEAHPRAKV TLNGVPAQPP GPRTQFLLKA
     TPEDNGRSFS CSATLEVAGQ LIHKNQTREL RVLYGPRLDE RDCPGNWTWP ENSQQTPMCQ
     AWGNPLPELK CLKDGTFPLP VGESVTVTRD LEGTYLCRAR STQGEVTREV TVNVLSPRYE
     FVIIAVVAAA VIMGTAGLST YLYNRQRKIR KYRLQQAQKG TPMKPNTQAT PP
 
 
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