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ICAM2_PANTR
ID   ICAM2_PANTR             Reviewed;         275 AA.
AC   Q5NKV2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Intercellular adhesion molecule 2;
DE            Short=ICAM-2;
DE   AltName: CD_antigen=CD102;
DE   Flags: Precursor;
GN   Name=ICAM2;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Isolate Angela, and Isolate Jenny; 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; AF340049; AAQ14906.1; -; mRNA.
DR   EMBL; AF340050; AAQ14907.1; -; mRNA.
DR   RefSeq; NP_001009166.1; NM_001009166.1.
DR   RefSeq; XP_009431260.1; XM_009432985.2.
DR   RefSeq; XP_009431261.1; XM_009432986.1.
DR   AlphaFoldDB; Q5NKV2; -.
DR   SMR; Q5NKV2; -.
DR   STRING; 9598.ENSPTRP00000016198; -.
DR   PaxDb; Q5NKV2; -.
DR   Ensembl; ENSPTRT00000017489; ENSPTRP00000016198; ENSPTRG00000009534.
DR   GeneID; 494137; -.
DR   KEGG; ptr:494137; -.
DR   CTD; 3384; -.
DR   VGNC; VGNC:9329; ICAM2.
DR   eggNOG; ENOG502RZRA; Eukaryota.
DR   GeneTree; ENSGT00940000161654; -.
DR   HOGENOM; CLU_088446_0_0_1; -.
DR   InParanoid; Q5NKV2; -.
DR   OMA; QVYEPVQ; -.
DR   OrthoDB; 731140at2759; -.
DR   TreeFam; TF333745; -.
DR   Proteomes; UP000002277; Chromosome 17.
DR   Bgee; ENSPTRG00000009534; Expressed in heart and 20 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_0000014792"
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        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;  30667 MW;  CA3A5048712A59B3 CRC64;
     MSSFSYRTLT VALFALICCP GSDEKVFEVH VRPKKLAVEP KGSLKVNCST TCNQPEVGGL
     ETSLDKILLD EQAQWKHYLV SNISHDTVLQ CHFTCSGKQE SMNSNVSVYQ PPRQVILTLQ
     PTLVAVGKSF TIECRVPTVE PLDSLTLFLF RGNETLHYET FGKAAPAPQE ATVTFNSTAD
     RDDGHRNFSC LAVLDLMSRG GNIFHKHSAP KMLEIYEPVS DSQMVIIVTV VSVLLSLFVT
     SVLLCFIFGQ HLRQQRMGTY GVRAAWRRLP QAFRP
 
 
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