LIRA5_HUMAN
ID LIRA5_HUMAN Reviewed; 299 AA.
AC A6NI73; A6NHI3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Leukocyte immunoglobulin-like receptor subfamily A member 5;
DE AltName: Full=CD85 antigen-like family member F;
DE AltName: Full=Immunoglobulin-like transcript 11;
DE Short=ILT-11;
DE AltName: Full=Leukocyte immunoglobulin-like receptor 9;
DE Short=LIR-9;
DE AltName: CD_antigen=CD85f;
DE Flags: Precursor;
GN Name=LILRA5; Synonyms=ILT11, LILRB7, LIR9;
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).
RX PubMed=10941842; DOI=10.1007/s002510000187;
RA Wende H., Volz A., Ziegler A.;
RT "Extensive gene duplications and a large inversion characterize the human
RT leukocyte receptor cluster.";
RL Immunogenetics 51:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=12393390; DOI=10.1182/blood-2002-05-1432;
RA Borges L., Kubin M., Kuhlman T.;
RT "LIR9, an immunoglobulin-superfamily-activating receptor, is expressed as a
RT transmembrane and as a secreted molecule.";
RL Blood 101:1484-1486(2003).
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 42-237, FUNCTION, AND DISULFIDE
RP BOND.
RX PubMed=16675463; DOI=10.1074/jbc.m603076200;
RA Shiroishi M., Kajikawa M., Kuroki K., Ose T., Kohda D., Maenaka K.;
RT "Crystal structure of the human monocyte-activating receptor, 'Group 2'
RT leukocyte Ig-like receptor A5 (LILRA5/LIR9/ILT11).";
RL J. Biol. Chem. 281:19536-19544(2006).
CC -!- FUNCTION: May play a role in triggering innate immune responses. Does
CC not seem to play a role for any class I MHC antigen recognition.
CC {ECO:0000269|PubMed:16675463}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12393390};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted
CC {ECO:0000269|PubMed:12393390}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=LIR9m1;
CC IsoId=A6NI73-1; Sequence=Displayed;
CC Name=2; Synonyms=LIR9m2;
CC IsoId=A6NI73-2; Sequence=VSP_031276;
CC Name=3; Synonyms=LIR9s1;
CC IsoId=A6NI73-3; Sequence=VSP_031277;
CC Name=4; Synonyms=LIR9s2;
CC IsoId=A6NI73-4; Sequence=VSP_031276, VSP_031277;
CC -!- TISSUE SPECIFICITY: Expressed mostly in tissues of the hematopoietic
CC system, including bone marrow, spleen, lymph node and peripheral
CC leukocytes. Among leukocytes, monocytes and neutrophils express the
CC highest level. Expressed in CD14+ monocytes, but not in T-cells, B-
CC cells or natural killer (NK) cells (at protein level).
CC {ECO:0000269|PubMed:12393390}.
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DR EMBL; AF212842; AAF73849.1; -; mRNA.
DR EMBL; AF324830; AAK52451.1; -; mRNA.
DR EMBL; AF499916; AAN27925.1; -; mRNA.
DR EMBL; AF499917; AAN27926.1; -; mRNA.
DR EMBL; AF499918; AAN27927.1; -; mRNA.
DR EMBL; AF499919; AAN27928.1; -; mRNA.
DR EMBL; AC008984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72226.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72227.1; -; Genomic_DNA.
DR CCDS; CCDS12888.1; -. [A6NI73-1]
DR CCDS; CCDS12889.1; -. [A6NI73-2]
DR RefSeq; NP_067073.1; NM_021250.3. [A6NI73-1]
DR RefSeq; NP_870994.1; NM_181879.2. [A6NI73-3]
DR RefSeq; NP_871714.1; NM_181985.3. [A6NI73-2]
DR RefSeq; NP_871715.1; NM_181986.2. [A6NI73-4]
DR PDB; 2D3V; X-ray; 1.85 A; A=42-237.
DR PDBsum; 2D3V; -.
DR AlphaFoldDB; A6NI73; -.
DR SMR; A6NI73; -.
DR BioGRID; 131702; 46.
DR STRING; 9606.ENSP00000404236; -.
DR GlyGen; A6NI73; 3 sites.
DR iPTMnet; A6NI73; -.
DR PhosphoSitePlus; A6NI73; -.
DR BioMuta; LILRA5; -.
DR jPOST; A6NI73; -.
DR MassIVE; A6NI73; -.
DR PaxDb; A6NI73; -.
DR PeptideAtlas; A6NI73; -.
DR PRIDE; A6NI73; -.
DR ProteomicsDB; 1250; -. [A6NI73-1]
DR ProteomicsDB; 1251; -. [A6NI73-2]
DR ProteomicsDB; 1252; -. [A6NI73-3]
DR ProteomicsDB; 1253; -. [A6NI73-4]
DR Antibodypedia; 46350; 177 antibodies from 27 providers.
DR DNASU; 353514; -.
DR Ensembl; ENST00000432233.8; ENSP00000404236.4; ENSG00000187116.14. [A6NI73-1]
DR Ensembl; ENST00000486742.2; ENSP00000484372.1; ENSG00000187116.14. [A6NI73-2]
DR Ensembl; ENST00000611164.4; ENSP00000482658.1; ENSG00000278355.4. [A6NI73-2]
DR Ensembl; ENST00000612266.4; ENSP00000480436.1; ENSG00000274914.4. [A6NI73-4]
DR Ensembl; ENST00000612621.4; ENSP00000484785.1; ENSG00000278355.4. [A6NI73-1]
DR Ensembl; ENST00000613559.1; ENSP00000484775.1; ENSG00000274914.4. [A6NI73-3]
DR Ensembl; ENST00000614299.4; ENSP00000483992.1; ENSG00000274914.4. [A6NI73-2]
DR Ensembl; ENST00000615820.1; ENSP00000480204.1; ENSG00000274113.4. [A6NI73-2]
DR Ensembl; ENST00000616133.1; ENSP00000484062.1; ENSG00000275404.4. [A6NI73-4]
DR Ensembl; ENST00000618711.4; ENSP00000478354.1; ENSG00000274914.4. [A6NI73-1]
DR Ensembl; ENST00000619516.3; ENSP00000480382.1; ENSG00000278355.4. [A6NI73-4]
DR Ensembl; ENST00000620091.4; ENSP00000480458.1; ENSG00000274113.4. [A6NI73-1]
DR Ensembl; ENST00000620692.4; ENSP00000483958.1; ENSG00000275404.4. [A6NI73-3]
DR Ensembl; ENST00000620898.4; ENSP00000484869.1; ENSG00000275404.4. [A6NI73-2]
DR Ensembl; ENST00000621042.4; ENSP00000482882.1; ENSG00000275404.4. [A6NI73-1]
DR Ensembl; ENST00000621482.2; ENSP00000477785.1; ENSG00000278355.4. [A6NI73-3]
DR GeneID; 353514; -.
DR KEGG; hsa:353514; -.
DR MANE-Select; ENST00000432233.8; ENSP00000404236.4; NM_021250.4; NP_067073.1.
DR UCSC; uc032idp.1; human. [A6NI73-1]
DR CTD; 353514; -.
DR DisGeNET; 353514; -.
DR GeneCards; LILRA5; -.
DR HGNC; HGNC:16309; LILRA5.
DR HPA; ENSG00000187116; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 606047; gene.
DR neXtProt; NX_A6NI73; -.
DR OpenTargets; ENSG00000187116; -.
DR PharmGKB; PA142671547; -.
DR VEuPathDB; HostDB:ENSG00000187116; -.
DR eggNOG; ENOG502RU0A; Eukaryota.
DR GeneTree; ENSGT01000000214458; -.
DR HOGENOM; CLU_021100_1_4_1; -.
DR InParanoid; A6NI73; -.
DR OMA; SSHRGTF; -.
DR OrthoDB; 1327293at2759; -.
DR PhylomeDB; A6NI73; -.
DR TreeFam; TF336644; -.
DR PathwayCommons; A6NI73; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 353514; 10 hits in 1055 CRISPR screens.
DR EvolutionaryTrace; A6NI73; -.
DR GenomeRNAi; 353514; -.
DR Pharos; A6NI73; Tbio.
DR PRO; PR:A6NI73; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; A6NI73; protein.
DR Bgee; ENSG00000187116; Expressed in blood and 92 other tissues.
DR Genevisible; A6NI73; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IMP:UniProtKB.
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:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; IDA:UniProtKB.
DR GO; GO:0032696; P:negative regulation of interleukin-13 production; IDA:UniProtKB.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:UniProtKB.
DR GO; GO:0050867; P:positive regulation of cell activation; IDA:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
DR DisProt; DP02812; -.
DR Gene3D; 2.60.40.10; -; 2.
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; 2.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Immunoglobulin domain; Innate immunity; Membrane;
KW Receptor; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..299
FT /note="Leukocyte immunoglobulin-like receptor subfamily A
FT member 5"
FT /id="PRO_0000318708"
FT TOPO_DOM 42..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 51..136
FT /note="Ig-like C2-type 1"
FT DOMAIN 142..230
FT /note="Ig-like C2-type 2"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..116
FT /evidence="ECO:0000269|PubMed:16675463,
FT ECO:0007744|PDB:2D3V"
FT DISULFID 162..214
FT /evidence="ECO:0000269|PubMed:16675463,
FT ECO:0007744|PDB:2D3V"
FT VAR_SEQ 31..42
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12393390"
FT /id="VSP_031276"
FT VAR_SEQ 239..299
FT /note="AADNLSPSQNKSDSGTASHLQDYAVENLIRMGMAGLILVVLGILIFQDWHSQ
FT RSPQAAAGR -> EEATVFSSTIQGSQTGCGELYRQGSPC (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:12393390"
FT /id="VSP_031277"
FT CONFLICT 100
FT /note="R -> G (in Ref. 1; AAF73849)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="H -> R (in Ref. 1; AAF73849)"
FT /evidence="ECO:0000305"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:2D3V"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:2D3V"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:2D3V"
SQ SEQUENCE 299 AA; 32755 MW; F5EE25361D4E0F02 CRC64;
MAPWSHPSAQ LQPVGGDAVS PALMVLLCLG LSLGPRTHVQ AGNLSKATLW AEPGSVISRG
NSVTIRCQGT LEAQEYRLVK EGSPEPWDTQ NPLEPKNKAR FSIPSMTEHH AGRYRCYYYS
PAGWSEPSDP LELVVTGFYN KPTLSALPSP VVTSGENVTL QCGSRLRFDR FILTEEGDHK
LSWTLDSQLT PSGQFQALFP VGPVTPSHRW MLRCYGSRRH ILQVWSEPSD LLEIPVSGAA
DNLSPSQNKS DSGTASHLQD YAVENLIRMG MAGLILVVLG ILIFQDWHSQ RSPQAAAGR
