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   24-JAN-2024, entry version 219.
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   GlyCosmos; P13598; 6 sites, 21 glycans.
DR   GlyGen; P13598; 9 sites, 21 N-linked glycans (6 sites), 1 O-linked glycan (1 site).
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; 9606-ENSP00000415283; -.
DR   PeptideAtlas; P13598; -.
DR   ProteomicsDB; 52937; -.
DR   Pumba; P13598; -.
DR   Antibodypedia; 796; 998 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   AGR; HGNC:5345; -.
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; 4014106at2759; -.
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 1156 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 195 other cell types or tissues.
DR   ExpressionAtlas; P13598; baseline and differential.
DR   GO; GO:0032154; C:cleavage furrow; IDA:HGNC.
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   CDD; cd05755; IgC2_2_ICAM-1_like; 1.
DR   CDD; cd20995; IgI_N_ICAM-2; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR003988; ICAM.
DR   InterPro; IPR013768; ICAM_N.
DR   InterPro; IPR047012; ICAM_VCAM.
DR   InterPro; IPR003987; ICAM_VCAM_N.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR13771; INTERCELLULAR ADHESION MOLECULE; 1.
DR   PANTHER; PTHR13771:SF3; INTERCELLULAR ADHESION MOLECULE 2; 1.
DR   Pfam; PF03921; ICAM_N; 1.
DR   PRINTS; PR01473; ICAM.
DR   PRINTS; PR01472; ICAMVCAM1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   Genevisible; P13598; HS.
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
//