ICAM2_GORGO
ID ICAM2_GORGO Reviewed; 275 AA.
AC Q5NKV1;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Intercellular adhesion molecule 2;
DE Short=ICAM-2;
DE AltName: CD_antigen=CD102;
DE Flags: Precursor;
GN Name=ICAM2;
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; 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). ICAM2 may play a role in lymphocyte
CC recirculation by blocking LFA-1-dependent cell adhesion. It mediates
CC adhesive interactions important for antigen-specific immune response,
CC NK-cell mediated clearance, lymphocyte recirculation, and other
CC cellular interactions important for immune response and surveillance
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RDX, EZR and MSN.
CC {ECO:0000250|UniProtKB:P35330}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}. Cell projection, microvillus
CC {ECO:0000250|UniProtKB:P35330}. Note=Co-localizes with RDX, EZR and MSN
CC in microvilli. {ECO:0000250|UniProtKB:P35330}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC {ECO:0000305}.
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DR EMBL; AF340051; AAQ14908.1; -; mRNA.
DR RefSeq; NP_001266588.1; NM_001279659.1.
DR RefSeq; XP_018881663.1; XM_019026118.1.
DR AlphaFoldDB; Q5NKV1; -.
DR SMR; Q5NKV1; -.
DR STRING; 9593.ENSGGOP00000013761; -.
DR Ensembl; ENSGGOT00000014155; ENSGGOP00000013761; ENSGGOG00000014108.
DR GeneID; 101130366; -.
DR KEGG; ggo:101130366; -.
DR CTD; 3384; -.
DR eggNOG; ENOG502RZRA; Eukaryota.
DR GeneTree; ENSGT00940000161654; -.
DR InParanoid; Q5NKV1; -.
DR OrthoDB; 731140at2759; -.
DR Proteomes; UP000001519; Chromosome 5.
DR Bgee; ENSGGOG00000014108; Expressed in heart and 6 other tissues.
DR GO; GO:0032154; C:cleavage furrow; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0001931; C:uropod; 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:0098609; P:cell-cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003988; ICAM.
DR InterPro; IPR015653; ICAM2.
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 PANTHER; PTHR13771:SF3; PTHR13771:SF3; 1.
DR Pfam; PF03921; ICAM_N; 1.
DR PRINTS; PR01473; ICAM.
DR PRINTS; PR01472; ICAMVCAM1.
DR SUPFAM; SSF48726; SSF48726; 2.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell projection; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..275
FT /note="Intercellular adhesion molecule 2"
FT /id="PRO_0000014789"
FT TOPO_DOM 25..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..98
FT /note="Ig-like C2-type 1"
FT DOMAIN 127..197
FT /note="Ig-like C2-type 2"
FT REGION 251..275
FT /note="Required for interaction with EZR, MSN and RDX and
FT co-localization to microvilli"
FT /evidence="ECO:0000250|UniProtKB:P35330"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..91
FT /evidence="ECO:0000250|UniProtKB:P13598"
FT DISULFID 52..95
FT /evidence="ECO:0000250|UniProtKB:P13598"
FT DISULFID 134..190
FT /evidence="ECO:0000250|UniProtKB:P13598"
SQ SEQUENCE 275 AA; 30578 MW; 15E3315847849E95 CRC64;
MSSFGYRTLT VALFALICCP GSDEKVFEVH VRPKKLAVEP KASLEVNCST TCNQPEVGGL
ETSLDKILLD EQAQWKHYLV SNISHDTVLQ CHFTCSGKQE SMNSNVSVYQ PPRQVILTLQ
PTLVAVGKSF TIECRVPTVE PLDSLTLFLF RGNETLHNQT FGKAAPALQE ATATFNSTAD
REDGHRNFSC LAVLDLISRG GNIFQEHSAP KMLEIYEPVS DSQMVIIVTV VSVLLSLFVT
SVLLCFIFGQ HLRQQRMGTY GVRAAWRRLP QAFRP
