ILDR1_PONAB
ID ILDR1_PONAB Reviewed; 546 AA.
AC Q5R8C7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Immunoglobulin-like domain-containing receptor 1;
DE Flags: Precursor;
GN Name=ILDR1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Maintains epithelial barrier function by recruiting
CC MARVELD2/tricellulin to tricellular tight junctions (tTJs). Crucial for
CC normal hearing by maintaining the structural and functional integrity
CC of tTJs, which are critical for the survival of auditory neurosensory
CC HCs. Mediates fatty acids and lipoproteins-stimulated
CC CCK/cholecystokinin secretion in the small intestine. In the inner ear,
CC may regulate alternative pre-mRNA splicing via binding to TRA2A, TRA2B
CC and SRSF1. {ECO:0000250|UniProtKB:Q8CBR1}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with MARVELD2 and
CC OCLN; the interaction is required to recruit MARVELD2 to tricellular
CC contacts. Interacts (via C-terminus) with TRA2A, TRA2B and SRSF1 (By
CC similarity). {ECO:0000250|UniProtKB:Q86SU0,
CC ECO:0000250|UniProtKB:Q8CBR1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8CBR1};
CC Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight
CC junction {ECO:0000250|UniProtKB:Q8CBR1}. Nucleus
CC {ECO:0000250|UniProtKB:Q8CBR1}. Note=Localizes to tricellular tight
CC junctions (tTJs) between epithelial cells.
CC {ECO:0000250|UniProtKB:Q8CBR1}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. LISCH7 family.
CC {ECO:0000305}.
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DR EMBL; CR859826; CAH91983.1; -; mRNA.
DR RefSeq; NP_001126151.1; NM_001132679.1.
DR AlphaFoldDB; Q5R8C7; -.
DR STRING; 9601.ENSPPYP00000015089; -.
DR PRIDE; Q5R8C7; -.
DR GeneID; 100173110; -.
DR KEGG; pon:100173110; -.
DR CTD; 286676; -.
DR eggNOG; ENOG502QS11; Eukaryota.
DR InParanoid; Q5R8C7; -.
DR OrthoDB; 860055at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0070160; C:tight junction; ISS:UniProtKB.
DR GO; GO:0061689; C:tricellular tight junction; ISS:UniProtKB.
DR GO; GO:0070506; F:high-density lipoprotein particle receptor activity; ISS:UniProtKB.
DR GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISS:UniProtKB.
DR GO; GO:0061833; P:protein localization to tricellular tight junction; ISS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0070542; P:response to fatty acid; ISS:UniProtKB.
DR GO; GO:1904274; P:tricellular tight junction assembly; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Disulfide bond; Immunoglobulin domain;
KW Membrane; Nucleus; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..546
FT /note="Immunoglobulin-like domain-containing receptor 1"
FT /id="PRO_0000245306"
FT TOPO_DOM 24..167
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..162
FT /note="Ig-like V-type"
FT REGION 399..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CBR1"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CBR1"
FT DISULFID 45..145
FT /evidence="ECO:0000250"
SQ SEQUENCE 546 AA; 63066 MW; 966CCA828C835D35 CRC64;
MAWPKLPAPW LLLCTWLPAG CLSLLVTVQH TERYVTLFAS IILKCDYTTS AQLQDVVVTW
RFKSFCKDPI FDYYSASYQA ALSLGQDPSN DCNDNQREVR IVAQRRGQNE PVLGVDYRQR
KITIQNRADL VINEVMWWDH GVYYCTIEAP GDTSGDPDKE VKLIVLHWLT VIFIILGALL
LLLLIGVCWC QCCPQYCCCY IRCPCCPARC CCPEEALARH RYMKQAQALG PQMMEKPLYW
GADRSSQVSS YPMHPLLQRD LSLRSSLPQM PMTQTTNHPP IANGVLEYLE KELRNLNLAQ
PLPPDLKARF GHPCSMLSSL GSEVVERRFI HLPPLIRDLS SSRRTSDSLH QQWLTPIPSR
PWDLREGRRQ HHYPDFHQEL QDRGPKSWAL ERRELDPSWS GRHRSSRLNG SPIHWSDRDS
LSDVPSSIEA RWQPSHPPFR SRCQERPRRP SPRESTQRHG RRRRHRSYSP PLPSGLSSWS
SEEDKERQPQ SWGAHRRRSH SPHWPEEKPP SYRSLDVTPG KNSRKKGSVE RRSEKDSSHS
GRSVVI
