ID   ILDR1_XENLA             Reviewed;         545 AA.
AC   Q32NM7;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Immunoglobulin-like domain-containing receptor 1;
DE   Flags: Precursor;
GN   Name=ildr1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Maintains epithelial barrier function by recruiting
CC       MARVELD2/tricellulin to tricellular tight junctions (tTJs).
CC       {ECO:0000250|UniProtKB:Q86SU0}.
CC   -!- SUBUNIT: Homooligomer (By similarity). Interacts with MARVELD2 and
CC       OCLN; the interaction is required to recruit MARVELD2 to tricellular
CC       contacts (By similarity). {ECO:0000250|UniProtKB:Q86SU0,
CC       ECO:0000250|UniProtKB:Q8CBR1}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86SU0};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q86SU0}.
CC       Cell junction, tight junction {ECO:0000250|UniProtKB:Q86SU0}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. LISCH7 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC108559; AAI08560.1; -; mRNA.
DR   RefSeq; NP_001089861.1; NM_001096392.1.
DR   AlphaFoldDB; Q32NM7; -.
DR   PRIDE; Q32NM7; -.
DR   DNASU; 734927; -.
DR   GeneID; 734927; -.
DR   KEGG; xla:734927; -.
DR   CTD; 734927; -.
DR   Xenbase; XB-GENE-994994; ildr1.L.
DR   OrthoDB; 860055at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 734927; Expressed in internal ear and 13 other tissues.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070160; C:tight junction; ISS:UniProtKB.
DR   GO; GO:0061689; C:tricellular tight junction; ISS:UniProtKB.
DR   GO; GO:0010669; P:epithelial structure maintenance; 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:1904274; P:tricellular tight junction assembly; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008664; LISCH7.
DR   Pfam; PF05624; LSR; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Disulfide bond; Immunoglobulin domain;
KW   Membrane; Receptor; Reference proteome; Signal; Tight junction;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..545
FT                   /note="Immunoglobulin-like domain-containing receptor 1"
FT                   /id="PRO_0000245307"
FT   TOPO_DOM        21..164
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..545
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          21..159
FT                   /note="Ig-like V-type"
FT   REGION          338..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..353
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..415
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        42..142
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   545 AA;  62755 MW;  671AFD0C550314EB CRC64;
     MIPPRALLLI SVWMVSGGRT LLVTVQDTQR YTMLFSSIIL KCDYSTSAQI QDVAVTWRFK
     SFCKDPIFDY YSAAYQASLS LNQDPANDCN DNQREVRIVI QKRGQNEPVL GVDYRQRKIT
     IQNKADLVIS EVMWWDHGVY FCSVEAQGDT SGDPDKEVKL VVLHWLTVLF IILGALFLFL
     LIGICWCQCC PHCCCCYVRC PCCPTRCCCP EEALARHNYM KQMESMTPWM LDRPYYAGAD
     RNSQHSSYQL NPLLQRDLSL QSSLPMPAPM SFSPPNNKVL DFLETEIKNL NTAQPLMSAP
     HYGGASHHPS MLSSLSEVGV REVDRRVIQL PPLVEHIVSS HRSSNSSHQR RNMGSWDPLD
     GERDRRRNRQ LDDSLSNETN WRAQERQHSD RSSGHRRDPP NNRRPRRDVS PPRRYGDSYS
     DESANNDPRG RSNPHSDRAR PTERRRSPER GDQGRRGSPD RYSRSQRHRR SYSPPHRRDS
     WSSEDETRNN QRGRGRRERS YEWPEEKPPS YKSLEICAGK APTQRPGAVR QSDRASSRSG
     RSMVI