LIRB5_HUMAN
ID LIRB5_HUMAN Reviewed; 590 AA.
AC O75023; Q8N760;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Leukocyte immunoglobulin-like receptor subfamily B member 5;
DE AltName: Full=CD85 antigen-like family member C;
DE AltName: Full=Leukocyte immunoglobulin-like receptor 8;
DE Short=LIR-8;
DE AltName: CD_antigen=CD85c;
DE Flags: Precursor;
GN Name=LILRB5; Synonyms=LIR8;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP ARG-542.
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=9548455;
RA Borges L., Hsu M.-L., Fanger N., Kubin M., Cosman D.;
RT "A family of human lymphoid and myeloid Ig-like receptors, some of which
RT bind to MHC class I molecules.";
RL J. Immunol. 159:5192-5196(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ARG-542.
RC TISSUE=Small intestine, and Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-542.
RC TISSUE=Pancreas, and Spleen;
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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-279.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May act as receptor for class I MHC antigens.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75023-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75023-2; Sequence=VSP_008461, VSP_008462;
CC Name=3;
CC IsoId=O75023-3; Sequence=VSP_008462;
CC -!- TISSUE SPECIFICITY: Detected in a natural killer (NK) cells.
CC {ECO:0000269|PubMed:9548455}.
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; AF025534; AAB87668.1; -; mRNA.
DR EMBL; AK057072; BAB71361.1; -; mRNA.
DR EMBL; AK223296; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC010492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025704; AAH25704.1; -; mRNA.
DR CCDS; CCDS12885.1; -. [O75023-1]
DR CCDS; CCDS42611.1; -. [O75023-2]
DR CCDS; CCDS46176.1; -. [O75023-3]
DR RefSeq; NP_001074911.1; NM_001081442.2.
DR RefSeq; NP_001074912.1; NM_001081443.2.
DR RefSeq; NP_001291386.1; NM_001304457.1.
DR RefSeq; NP_006831.1; NM_006840.4.
DR AlphaFoldDB; O75023; -.
DR BioGRID; 116186; 1.
DR IntAct; O75023; 1.
DR MINT; O75023; -.
DR STRING; 9606.ENSP00000406478; -.
DR GlyGen; O75023; 6 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; O75023; -.
DR PhosphoSitePlus; O75023; -.
DR BioMuta; LILRB5; -.
DR jPOST; O75023; -.
DR MassIVE; O75023; -.
DR PaxDb; O75023; -.
DR PeptideAtlas; O75023; -.
DR PRIDE; O75023; -.
DR ProteomicsDB; 49699; -. [O75023-1]
DR ProteomicsDB; 49700; -. [O75023-2]
DR ProteomicsDB; 49701; -. [O75023-3]
DR Antibodypedia; 2302; 143 antibodies from 27 providers.
DR DNASU; 10990; -.
DR Ensembl; ENST00000316219.9; ENSP00000320390.5; ENSG00000105609.17. [O75023-1]
DR Ensembl; ENST00000345866.10; ENSP00000263430.8; ENSG00000105609.17. [O75023-2]
DR Ensembl; ENST00000449561.3; ENSP00000406478.1; ENSG00000105609.17. [O75023-3]
DR Ensembl; ENST00000610764.4; ENSP00000479022.1; ENSG00000277414.4.
DR Ensembl; ENST00000614318.1; ENSP00000483649.1; ENSG00000278437.4.
DR Ensembl; ENST00000615429.1; ENSP00000482404.1; ENSG00000274311.4.
DR Ensembl; ENST00000615837.4; ENSP00000478835.1; ENSG00000277414.4.
DR Ensembl; ENST00000616618.4; ENSP00000478912.1; ENSG00000274311.4.
DR Ensembl; ENST00000616805.4; ENSP00000483502.1; ENSG00000273991.4.
DR Ensembl; ENST00000617355.4; ENSP00000483481.1; ENSG00000274311.4.
DR Ensembl; ENST00000619608.4; ENSP00000479413.1; ENSG00000277414.4.
DR Ensembl; ENST00000620714.4; ENSP00000480909.1; ENSG00000273991.4.
DR Ensembl; ENST00000621193.4; ENSP00000482062.1; ENSG00000278437.4.
DR Ensembl; ENST00000621867.4; ENSP00000481263.1; ENSG00000273991.4.
DR Ensembl; ENST00000622596.4; ENSP00000482535.1; ENSG00000278437.4.
DR GeneID; 10990; -.
DR KEGG; hsa:10990; -.
DR MANE-Select; ENST00000449561.3; ENSP00000406478.1; NM_001081442.3; NP_001074911.2. [O75023-3]
DR UCSC; uc002qex.4; human. [O75023-1]
DR CTD; 10990; -.
DR DisGeNET; 10990; -.
DR GeneCards; LILRB5; -.
DR HGNC; HGNC:6609; LILRB5.
DR HPA; ENSG00000105609; Tissue enhanced (adipose tissue, lymphoid tissue).
DR MIM; 604814; gene.
DR neXtProt; NX_O75023; -.
DR OpenTargets; ENSG00000105609; -.
DR PharmGKB; PA30383; -.
DR VEuPathDB; HostDB:ENSG00000105609; -.
DR eggNOG; ENOG502RYEX; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR HOGENOM; CLU_021100_2_3_1; -.
DR InParanoid; O75023; -.
DR OrthoDB; 1000446at2759; -.
DR PhylomeDB; O75023; -.
DR TreeFam; TF336644; -.
DR PathwayCommons; O75023; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR SignaLink; O75023; -.
DR BioGRID-ORCS; 10990; 15 hits in 1063 CRISPR screens.
DR GeneWiki; LILRB5; -.
DR GenomeRNAi; 10990; -.
DR Pharos; O75023; Tbio.
DR PRO; PR:O75023; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75023; protein.
DR Bgee; ENSG00000105609; Expressed in spleen and 99 other tissues.
DR Genevisible; O75023; HS.
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:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
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 InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF00047; ig; 2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Disulfide bond; Glycoprotein;
KW Immunity; Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..590
FT /note="Leukocyte immunoglobulin-like receptor subfamily B
FT member 5"
FT /id="PRO_0000014825"
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..590
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 416..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 552..557
FT /note="ITIM motif 1"
FT MOTIF 582..587
FT /note="ITIM motif 2"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
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:0000269|PubMed:16335952"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 244..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 344..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 119..218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008461"
FT VAR_SEQ 435
FT /note="P -> PA (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008462"
FT VARIANT 247
FT /note="D -> G (in dbSNP:rs12975366)"
FT /id="VAR_061316"
FT VARIANT 542
FT /note="P -> R"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9548455"
FT /id="VAR_085724"
FT CONFLICT 12
FT /note="G -> W (in Ref. 2; AK223296)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="L -> R (in Ref. 2; AK223296)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="L -> S (in Ref. 2; BAB71361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 590 AA; 64067 MW; 8DF70491112E44CD CRC64;
MTLTLSVLIC LGLSVGPRTC VQAGTLPKPT LWAEPASVIA RGKPVTLWCQ GPLETEEYRL
DKEGLPWARK RQNPLEPGAK AKFHIPSTVY DSAGRYRCYY ETPAGWSEPS DPLELVATGF
YAEPTLLALP SPVVASGGNV TLQCDTLDGL LTFVLVEEEQ KLPRTLYSQK LPKGPSQALF
PVGPVTPSCR WRFRCYYYYR KNPQVWSNPS DLLEILVPGV SRKPSLLIPQ GSVVARGGSL
TLQCRSDVGY DIFVLYKEGE HDLVQGSGQQ PQAGLSQANF TLGPVSRSHG GQYRCYGAHN
LSPRWSAPSD PLDILIAGLI PDIPALSVQP GPKVASGENV TLLCQSWHQI DTFFLTKEGA
AHPPLCLKSK YQSYRHQAEF SMSPVTSAQG GTYRCYSAIR SYPYLLSSPS YPQELVVSGP
SGDPSLSPTG STPTPGPEDQ PLTPTGLDPQ SGLGRHLGVV TGVSVAFVLL LFLLLFLLLR
HRHQSKHRTS AHFYRPAGAA GPEPKDQGLQ KRASPVADIQ EEILNAAVKD TQPKDGVEMD
APAAASEAPQ DVTYAQLHSL TLRREATEPP PSQEREPPAE PSIYAPLAIH
