ID A0A1S2ZXF1_ERIEU Unreviewed; 531 AA.
AC A0A1S2ZXF1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Intercellular adhesion molecule 1 {ECO:0000256|ARBA:ARBA00040566};
GN Name=ICAM1 {ECO:0000313|RefSeq:XP_007526085.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007526085.1};
RN [1] {ECO:0000313|RefSeq:XP_007526085.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00037418}.
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:0000256|ARBA:ARBA00038746}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ICAM family.
CC {ECO:0000256|ARBA:ARBA00005925}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_007526085.1; XM_007526023.2.
DR AlphaFoldDB; A0A1S2ZXF1; -.
DR GeneID; 103116160; -.
DR CTD; 3383; -.
DR eggNOG; ENOG502S45R; Eukaryota.
DR InParanoid; A0A1S2ZXF1; -.
DR OrthoDB; 4014106at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005178; F:integrin binding; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR InterPro; IPR003988; ICAM.
DR InterPro; IPR048679; ICAM1_3_5_D2.
DR InterPro; IPR013768; ICAM_N.
DR InterPro; IPR047012; ICAM_VCAM.
DR InterPro; IPR003987; ICAM_VCAM_N.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR PANTHER; PTHR13771; INTERCELLULAR ADHESION MOLECULE; 1.
DR PANTHER; PTHR13771:SF18; INTERCELLULAR ADHESION MOLECULE 1; 1.
DR Pfam; PF21146; ICAM1_3_5_D2; 1.
DR Pfam; PF03921; ICAM_N; 1.
DR PRINTS; PR01473; ICAM.
DR PRINTS; PR01472; ICAMVCAM1.
DR SMART; SM00409; IG; 4.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..531
FT /note="Intercellular adhesion molecule 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010349647"
FT TRANSMEM 477..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 113..186
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 531 AA; 57801 MW; 47A8FC0A64881186 CRC64;
MGLRVARNLL PALLALLGTL LPAPEAAQVS VYPPDATIPV GGSLLVNCSS DCNSLGLETI
LSKESRGFGG AEDTFWKAFL LNDIQEDDTP KCFSNCGGVQ SMASMTVTVY AFPDRVDLAP
LPPWVPAGDN FTLSCHVAGG APRKSLSVVF LRDKEELGRL SAEGEDPIKM TVTARREDHG
ANFSCRSELD LRPQGLELFQ NSSASQHLQI FVMPTTQPSL VSPKAVEVGT TWNLDCSLDG
LFPASEAKVH LEVGGQQLNP KITPRTDAVW AQVATKWEQE GELELKCEVT LAGQRREAVE
NVTFYSFPAP SLTLSASEVP EGTEVKVECE AFAGALATLR GAPARPPAPK SHFTFSASAQ
DHRRLFLCSA TLEVAGQKFH KNQSRELHVL YGPRLSDKDC PGNWTWEAGS HQTLRCQPWG
NPTPKLDCRR KGDDAPLPIG DLKPVKAEIR GTYVCHASSL LKTVTREVVV EVISPDYTLI
IIIGVVLVVV LTVAGFLGYH YNRQRKIRKY ELQKAQEEAA LKLNPLTAPP E
//
