ICAM2_HUMAN
ID ICAM2_HUMAN Reviewed; 275 AA.
AC P13598; Q14600;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Intercellular adhesion molecule 2;
DE Short=ICAM-2;
DE AltName: CD_antigen=CD102;
DE Flags: Precursor;
GN Name=ICAM2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Endothelial cell;
RX PubMed=2497351; DOI=10.1038/339061a0;
RA Staunton D.E., Dustin M.L., Springer T.A.;
RT "Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous
RT to ICAM-1.";
RL Nature 339:61-64(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Garcia-Aguilar J., Staunton D., Springer T.A.;
RT "Structure of the gene for the human intercellular adhesion molecule 2
RT (ICAM-2).";
RL Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 25-33.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective labeling of
RT protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105 AND ASN-176.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82; ASN-105; ASN-153 AND
RP ASN-176.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 25-216, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-47; ASN-82; ASN-105; ASN-153; ASN-176 AND ASN-187.
RX PubMed=9153399; DOI=10.1038/387312a0;
RA Casasnovas J.M., Springer T.A., Liu J.-H., Harrison S.C., Wang J.-H.;
RT "Crystal structure of ICAM-2 reveals a distinctive integrin recognition
RT surface.";
RL Nature 387:312-315(1997).
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 -!- 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}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=ICAM-2;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Itlect_262";
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DR EMBL; X15606; CAA33630.1; -; mRNA.
DR EMBL; M32334; AAA36035.1; -; Genomic_DNA.
DR EMBL; M32331; AAA36035.1; JOINED; Genomic_DNA.
DR EMBL; M32332; AAA36035.1; JOINED; Genomic_DNA.
DR EMBL; M32333; AAA36035.1; JOINED; Genomic_DNA.
DR EMBL; BC003097; AAH03097.1; -; mRNA.
DR CCDS; CCDS11657.1; -.
DR PIR; S03967; S03967.
DR RefSeq; NP_000864.2; NM_000873.3.
DR RefSeq; NP_001093256.1; NM_001099786.1.
DR RefSeq; NP_001093257.1; NM_001099787.1.
DR RefSeq; NP_001093258.1; NM_001099788.1.
DR RefSeq; NP_001093259.1; NM_001099789.1.
DR PDB; 1ZXQ; X-ray; 2.20 A; A=25-216.
DR PDBsum; 1ZXQ; -.
DR AlphaFoldDB; P13598; -.
DR SMR; P13598; -.
DR BioGRID; 109611; 70.
DR IntAct; P13598; 14.
DR MINT; P13598; -.
DR STRING; 9606.ENSP00000415283; -.
DR GlyConnect; 682; 18 N-Linked glycans (6 sites).
DR GlyGen; P13598; 8 sites, 21 N-linked glycans (6 sites).
DR iPTMnet; P13598; -.
DR PhosphoSitePlus; P13598; -.
DR SwissPalm; P13598; -.
DR BioMuta; ICAM2; -.
DR DMDM; 115502404; -.
DR CPTAC; CPTAC-677; -.
DR EPD; P13598; -.
DR jPOST; P13598; -.
DR MassIVE; P13598; -.
DR PaxDb; P13598; -.
DR PeptideAtlas; P13598; -.
DR PRIDE; P13598; -.
DR ProteomicsDB; 52937; -.
DR Antibodypedia; 796; 923 antibodies from 43 providers.
DR DNASU; 3384; -.
DR Ensembl; ENST00000412356.5; ENSP00000415283.1; ENSG00000108622.11.
DR Ensembl; ENST00000418105.5; ENSP00000388666.1; ENSG00000108622.11.
DR Ensembl; ENST00000449662.6; ENSP00000392634.2; ENSG00000108622.11.
DR Ensembl; ENST00000579687.5; ENSP00000462579.1; ENSG00000108622.11.
DR Ensembl; ENST00000579788.6; ENSP00000464665.1; ENSG00000108622.11.
DR GeneID; 3384; -.
DR KEGG; hsa:3384; -.
DR MANE-Select; ENST00000579788.6; ENSP00000464665.1; NM_001099789.2; NP_001093259.1.
DR CTD; 3384; -.
DR DisGeNET; 3384; -.
DR GeneCards; ICAM2; -.
DR HGNC; HGNC:5345; ICAM2.
DR HPA; ENSG00000108622; Tissue enhanced (lymphoid).
DR MIM; 146630; gene.
DR neXtProt; NX_P13598; -.
DR OpenTargets; ENSG00000108622; -.
DR PharmGKB; PA29593; -.
DR VEuPathDB; HostDB:ENSG00000108622; -.
DR eggNOG; ENOG502RZRA; Eukaryota.
DR GeneTree; ENSGT00940000161654; -.
DR HOGENOM; CLU_088446_0_0_1; -.
DR InParanoid; P13598; -.
DR OMA; QVYEPVQ; -.
DR OrthoDB; 731140at2759; -.
DR PhylomeDB; P13598; -.
DR TreeFam; TF333745; -.
DR PathwayCommons; P13598; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
DR SignaLink; P13598; -.
DR SIGNOR; P13598; -.
DR BioGRID-ORCS; 3384; 7 hits in 1076 CRISPR screens.
DR ChiTaRS; ICAM2; human.
DR EvolutionaryTrace; P13598; -.
DR GeneWiki; ICAM2; -.
DR GenomeRNAi; 3384; -.
DR Pharos; P13598; Tbio.
DR PRO; PR:P13598; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P13598; protein.
DR Bgee; ENSG00000108622; Expressed in spleen and 194 other tissues.
DR ExpressionAtlas; P13598; baseline and differential.
DR Genevisible; P13598; HS.
DR GO; GO:0032154; C:cleavage furrow; IDA:HGNC.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001931; C:uropod; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IPI:BHF-UCL.
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 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell projection; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:19892738"
FT CHAIN 25..275
FT /note="Intercellular adhesion molecule 2"
FT /id="PRO_0000014790"
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:0000269|PubMed:9153399,
FT ECO:0007744|PDB:1ZXQ"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:9153399, ECO:0007744|PDB:1ZXQ"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:9153399,
FT ECO:0007744|PDB:1ZXQ"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:9153399, ECO:0007744|PDB:1ZXQ"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9153399,
FT ECO:0007744|PDB:1ZXQ"
FT DISULFID 48..91
FT /evidence="ECO:0000269|PubMed:9153399,
FT ECO:0007744|PDB:1ZXQ"
FT DISULFID 52..95
FT /evidence="ECO:0000269|PubMed:9153399,
FT ECO:0007744|PDB:1ZXQ"
FT DISULFID 134..190
FT /evidence="ECO:0000269|PubMed:9153399,
FT ECO:0007744|PDB:1ZXQ"
FT VARIANT 37
FT /note="A -> T (in dbSNP:rs5503)"
FT /id="VAR_014655"
FT VARIANT 199
FT /note="R -> H (in dbSNP:rs5504)"
FT /id="VAR_014656"
FT VARIANT 256
FT /note="R -> Q (in dbSNP:rs3764867)"
FT /id="VAR_021920"
FT CONFLICT 65
FT /note="D -> N (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 98..108
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:1ZXQ"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1ZXQ"
SQ SEQUENCE 275 AA; 30654 MW; C54FB34D92A6FC38 CRC64;
MSSFGYRTLT VALFTLICCP GSDEKVFEVH VRPKKLAVEP KGSLEVNCST TCNQPEVGGL
ETSLDKILLD EQAQWKHYLV SNISHDTVLQ CHFTCSGKQE SMNSNVSVYQ PPRQVILTLQ
PTLVAVGKSF TIECRVPTVE PLDSLTLFLF RGNETLHYET FGKAAPAPQE ATATFNSTAD
REDGHRNFSC LAVLDLMSRG GNIFHKHSAP KMLEIYEPVS DSQMVIIVTV VSVLLSLFVT
SVLLCFIFGQ HLRQQRMGTY GVRAAWRRLP QAFRP
