ILDR2_HUMAN
ID ILDR2_HUMAN Reviewed; 639 AA.
AC Q71H61;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Immunoglobulin-like domain-containing receptor 2 {ECO:0000305};
DE AltName: Full=Angulin-3;
DE Flags: Precursor;
GN Name=ILDR2 {ECO:0000312|HGNC:HGNC:18131}; Synonyms=C1orf32;
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].
RA Schulz H.L., Stohr H., Weber B.H.F.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=29431694; DOI=10.4049/jimmunol.1700325;
RA Hecht I., Toporik A., Podojil J.R., Vaknin I., Cojocaru G., Oren A.,
RA Aizman E., Liang S.C., Leung L., Dicken Y., Novik A., Marbach-Bar N.,
RA Elmesmari A., Tange C., Gilmour A., McIntyre D., Kurowska-Stolarska M.,
RA McNamee K., Leitner J., Greenwald S., Dassa L., Levine Z., Steinberger P.,
RA Williams R.O., Miller S.D., McInnes I.B., Neria E., Rotman G.;
RT "ILDR2 Is a Novel B7-like Protein That Negatively Regulates T Cell
RT Responses.";
RL J. Immunol. 200:2025-2037(2018).
CC -!- FUNCTION: May be involved in ER stress pathways with effects on lipid
CC homeostasis and insulin secretion. With ILDR1 and LSR, involved in the
CC maintain of the epithelial barrier function through the recruitment of
CC MARVELD2/tricellulin to tricellular tight junctions (By similarity).
CC Also functions as a B7-like protein family member expressed on immune
CC cells and inflamed tissue and with T-cell inhibitory activity
CC (PubMed:29431694). In the inner ear, may regulate alternative pre-mRNA
CC splicing via binding to TRA2A, TRA2B and SRSF1 (By similarity).
CC {ECO:0000250|UniProtKB:B5TVM2, ECO:0000269|PubMed:29431694}.
CC -!- SUBUNIT: Interacts with MARVELD2 and OCLN. Interacts with P4HB AND
CC HSPA5; the interaction with HSPA5 stabilizes ILDR2 expression.
CC Interacts (via C-terminus) with TRA2A, TRA2B and SRSF1.
CC {ECO:0000250|UniProtKB:B5TVM2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:B5TVM2}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:B5TVM2}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:B5TVM2}. Nucleus {ECO:0000250|UniProtKB:B5TVM2}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, brain, pituitary, colon,
CC heart, nerves, prostate, esophagus, lung liver and small intestine
CC (PubMed:29431694). Highly expressed in macrophages, also expressed in
CC monocytes and at low levels in NK and NKT cells (at protein level)
CC (PubMed:29431694). {ECO:0000269|PubMed:29431694}.
CC -!- DEVELOPMENTAL STAGE: Expression is up-regulated following
CC differentiation of monocytes to macrophages.
CC {ECO:0000269|PubMed:29431694}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. LISCH7 family.
CC {ECO:0000305}.
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DR EMBL; AF503509; AAQ07593.1; -; mRNA.
DR EMBL; AL009182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS1256.1; -.
DR RefSeq; NP_955383.1; NM_199351.2.
DR AlphaFoldDB; Q71H61; -.
DR BioGRID; 132364; 44.
DR IntAct; Q71H61; 6.
DR MINT; Q71H61; -.
DR STRING; 9606.ENSP00000271417; -.
DR iPTMnet; Q71H61; -.
DR PhosphoSitePlus; Q71H61; -.
DR SwissPalm; Q71H61; -.
DR BioMuta; ILDR2; -.
DR DMDM; 74749770; -.
DR jPOST; Q71H61; -.
DR MassIVE; Q71H61; -.
DR MaxQB; Q71H61; -.
DR PaxDb; Q71H61; -.
DR PeptideAtlas; Q71H61; -.
DR PRIDE; Q71H61; -.
DR ProteomicsDB; 68602; -.
DR Antibodypedia; 2487; 30 antibodies from 9 providers.
DR DNASU; 387597; -.
DR Ensembl; ENST00000271417.8; ENSP00000271417.2; ENSG00000143195.13.
DR GeneID; 387597; -.
DR KEGG; hsa:387597; -.
DR MANE-Select; ENST00000271417.8; ENSP00000271417.2; NM_199351.3; NP_955383.1.
DR UCSC; uc001gdx.3; human.
DR CTD; 387597; -.
DR DisGeNET; 387597; -.
DR GeneCards; ILDR2; -.
DR HGNC; HGNC:18131; ILDR2.
DR HPA; ENSG00000143195; Group enriched (brain, kidney, retina, testis).
DR MIM; 618081; gene.
DR neXtProt; NX_Q71H61; -.
DR OpenTargets; ENSG00000143195; -.
DR PharmGKB; PA164720916; -.
DR VEuPathDB; HostDB:ENSG00000143195; -.
DR eggNOG; ENOG502QSI2; Eukaryota.
DR GeneTree; ENSGT00950000183058; -.
DR HOGENOM; CLU_028969_0_0_1; -.
DR InParanoid; Q71H61; -.
DR OMA; EMEVLEY; -.
DR OrthoDB; 457764at2759; -.
DR PhylomeDB; Q71H61; -.
DR TreeFam; TF330877; -.
DR PathwayCommons; Q71H61; -.
DR SignaLink; Q71H61; -.
DR BioGRID-ORCS; 387597; 11 hits in 1064 CRISPR screens.
DR ChiTaRS; ILDR2; human.
DR GenomeRNAi; 387597; -.
DR Pharos; Q71H61; Tdark.
DR PRO; PR:Q71H61; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q71H61; protein.
DR Bgee; ENSG00000143195; Expressed in oocyte and 134 other tissues.
DR ExpressionAtlas; Q71H61; baseline and differential.
DR Genevisible; Q71H61; HS.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0070160; C:tight junction; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0050868; P:negative regulation of T cell activation; IDA:UniProtKB.
DR GO; GO:0031016; P:pancreas development; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR008664; LISCH7.
DR Pfam; PF05624; LSR; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Cell junction; Disulfide bond; Endoplasmic reticulum;
KW Immunoglobulin domain; Membrane; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Signal; Tight junction; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..639
FT /note="Immunoglobulin-like domain-containing receptor 2"
FT /id="PRO_0000278607"
FT TOPO_DOM 21..186
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..162
FT /note="Ig-like V-type"
FT REGION 273..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B5TVM2"
FT MOD_RES 544
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:B5TVM2"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B5TVM2"
FT DISULFID 42..145
FT /evidence="ECO:0000250"
FT VARIANT 202
FT /note="V -> I (in dbSNP:rs33958744)"
FT /id="VAR_049948"
SQ SEQUENCE 639 AA; 71200 MW; CBC1067684102090 CRC64;
MDRVLLRWIS LFWLTAMVEG LQVTVPDKKK VAMLFQPTVL RCHFSTSSHQ PAVVQWKFKS
YCQDRMGESL GMSSTRAQSL SKRNLEWDPY LDCLDSRRTV RVVASKQGST VTLGDFYRGR
EITIVHDADL QIGKLMWGDS GLYYCIITTP DDLEGKNEDS VELLVLGRTG LLADLLPSFA
VEIMPEWVFV GLVLLGVFLF FVLVGICWCQ CCPHSCCCYV RCPCCPDSCC CPQALYEAGK
AAKAGYPPSV SGVPGPYSIP SVPLGGAPSS GMLMDKPHPP PLAPSDSTGG SHSVRKGYRI
QADKERDSMK VLYYVEKELA QFDPARRMRG RYNNTISELS SLHEEDSNFR QSFHQMRSKQ
FPVSGDLESN PDYWSGVMGG SSGASRGPSA MEYNKEDRES FRHSQPRSKS EMLSRKNFAT
GVPAVSMDEL AAFADSYGQR PRRADGNSHE ARGGSRFERS ESRAHSGFYQ DDSLEEYYGQ
RSRSREPLTD ADRGWAFSPA RRRPAEDAHL PRLVSRTPGT APKYDHSYLG SARERQARPE
GASRGGSLET PSKRSAQLGP RSASYYAWSP PGTYKAGSSQ DDQEDASDDA LPPYSELELT
RGPSYRGRDL PYHSNSEKKR KKEPAKKTND FPTRMSLVV
