LIRB5_PANTR
ID LIRB5_PANTR Reviewed; 643 AA.
AC Q8MJZ7;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 5;
DE AltName: Full=Leukocyte immunoglobulin-like receptor 8;
DE Short=LIR-8;
DE Flags: Precursor;
GN Name=LILRB5; Synonyms=LIR8;
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].
RX PubMed=11698452; DOI=10.4049/jimmunol.167.10.5786;
RA Canavez F.C., Young N.T., Guethlein L.A., Rajalingam R., Khakoo S.I.,
RA Shum B.P., Parham P.;
RT "Comparison of chimpanzee and human leukocyte Ig-like receptor genes
RT reveals framework and rapidly evolving genes.";
RL J. Immunol. 167:5786-5794(2001).
CC -!- FUNCTION: May act as receptor for class I MHC antigens. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
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DR EMBL; AF383164; AAL31873.1; -; mRNA.
DR RefSeq; NP_001009027.1; NM_001009027.1.
DR AlphaFoldDB; Q8MJZ7; -.
DR SMR; Q8MJZ7; -.
DR STRING; 9598.ENSPTRP00000054290; -.
DR PaxDb; Q8MJZ7; -.
DR PRIDE; Q8MJZ7; -.
DR GeneID; 449640; -.
DR KEGG; ptr:449640; -.
DR CTD; 10990; -.
DR eggNOG; ENOG502RYEX; Eukaryota.
DR HOGENOM; CLU_021100_2_3_1; -.
DR InParanoid; Q8MJZ7; -.
DR OrthoDB; 1000446at2759; -.
DR TreeFam; TF336644; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032396; F:inhibitory MHC class I receptor activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 4.
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 InterPro; IPR003598; Ig_sub2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 4.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Disulfide bond; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..643
FT /note="Leukocyte immunoglobulin-like receptor subfamily B
FT member 5"
FT /id="PRO_0000014826"
FT TOPO_DOM 24..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..116
FT /note="Ig-like C2-type 1"
FT DOMAIN 111..228
FT /note="Ig-like C2-type 2"
FT DOMAIN 224..313
FT /note="Ig-like C2-type 3"
FT DOMAIN 337..418
FT /note="Ig-like C2-type 4"
FT REGION 417..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 605..610
FT /note="ITIM motif 1"
FT MOTIF 635..640
FT /note="ITIM motif 2"
FT COMPBIAS 533..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75023"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..98
FT /evidence="ECO:0000250|UniProtKB:Q8NHL6"
FT DISULFID 144..195
FT /evidence="ECO:0000250|UniProtKB:Q8NHL6"
FT DISULFID 244..295
FT /evidence="ECO:0000250|UniProtKB:Q8NHL6"
FT DISULFID 344..395
FT /evidence="ECO:0000250|UniProtKB:Q8NHL6"
SQ SEQUENCE 643 AA; 70505 MW; BEBC8F940B5F65AC CRC64;
MTLTLSVLIC LGLNVGPRTC VQAGTLPKPT LWAEPASVIA RGKPVTLWCQ GPLETEEYRL
DKEGLPWAWE RQNPLEPGAK AKFHILSTVY DSAGRYRCYY ETPAGWSEPS DPLELVATGF
YAEPTLLALP SPVVASGGNV TLQCDTRDGL LTFVLVEEEQ KLPRTLYSQK LPKGPSRALF
PVGPVTPSFR WRFRCYYYYR KNPQVWSHPS DLLEILVPGV SRKPSLLIPQ GSVVARGGSL
TLQCRSDVGY DRFVLYKEGG HDLVQGSGQQ PQAGLSQANF TLSPVSRSYG GQYRCYGAHN
LSPRWSAPSD PLDILIAGLI PDRPSLSVQP GPTVASGENV TLLCQSWRQI DTFFLTKEGA
AHPPLCLKSK YQFYKYQAEF SMSPVTSARG GTYRCYSAIR SYPHLLSSPS YPLELVVSGP
SGDPSLSPTG STPTPGPEDQ PLTPTGLDPQ SGLGRHLGVV TGVSVAFVLL LFLLLFLLLR
HRHQSKHRTS AHFYRPAGAA GPEPKDQVLQ KRASPVADTQ EEILNAAVKD TQPKDGAEMD
ARQSPRDEDP QAVTYAEVKH SRPRREMASP PSPLSGEFLD TKDTQAEEDR QMDTQAAASE
APQDVTYAQL HSLTLRREAT EPPPSQEREP PAEPSIYAPL AIH
