IRPL1_HUMAN
ID IRPL1_HUMAN Reviewed; 696 AA.
AC Q9NZN1; A0AVG4; Q9UJ53;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Interleukin-1 receptor accessory protein-like 1;
DE Short=IL-1-RAPL-1;
DE Short=IL-1RAPL-1;
DE Short=IL1RAPL-1;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Oligophrenin-4;
DE AltName: Full=Three immunoglobulin domain-containing IL-1 receptor-related 2;
DE Short=TIGIRR-2;
DE AltName: Full=X-linked interleukin-1 receptor accessory protein-like 1;
DE Flags: Precursor;
GN Name=IL1RAPL1; Synonyms=OPHN4;
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], INVOLVEMENT IN NONSPECIFIC XLMR, TISSUE
RP SPECIFICITY, AND ALTERNATIVE SPLICING.
RC TISSUE=Fetal brain;
RX PubMed=10471494; DOI=10.1038/12623;
RA Carrie A., Jun L., Bienvenu T., Vinet M.-C., McDonell N., Couvert P.,
RA Zemni R., Cardona A., Van Buggenhout G., Frints S., Hamel B.C.J.,
RA Moraine C., Ropers H.-H., Strom T., Howell G.R., Whittaker A., Ross M.T.,
RA Kahn A., Fryns J.-P., Beldjord C., Marynen P., Chelly J.;
RT "A new member of the IL-1 receptor family highly expressed in hippocampus
RT and involved in X-linked mental retardation.";
RL Nat. Genet. 23:25-31(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN XLID21.
RX PubMed=10757639; DOI=10.1038/sj.ejhg.5200415;
RA Jin H., Gardner R.J., Viswesvaraiah R., Muntoni F., Roberts R.G.;
RT "Two novel members of the interleukin-1 receptor gene family, one deleted
RT in Xp22.3-Xp21.3 mental retardation.";
RL Eur. J. Hum. Genet. 8:87-94(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Testis;
RX PubMed=10882729; DOI=10.1074/jbc.m004077200;
RA Born T.L., Smith D.E., Garka K.E., Renshaw B.R., Bertles J.S., Sims J.E.;
RT "Identification and characterization of two members of a novel class of the
RT interleukin-1 receptor (IL-1R) family. Delineation of a new class of IL-1R-
RT related proteins based on signaling.";
RL J. Biol. Chem. 275:29946-29954(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12777533; DOI=10.1093/molbev/msg134;
RA Kitano T., Schwarz C., Nickel B., Paeaebo S.;
RT "Gene diversity patterns at 10 X-chromosomal loci in humans and
RT chimpanzees.";
RL Mol. Biol. Evol. 20:1281-1289(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NCS1.
RX PubMed=12783849; DOI=10.1093/hmg/ddg147;
RA Bahi N., Friocourt G., Carrie A., Graham M.E., Weiss J.L., Chafey P.,
RA Fauchereau F., Burgoyne R.D., Chelly J.;
RT "IL1 receptor accessory protein like, a protein involved in X-linked mental
RT retardation, interacts with Neuronal Calcium Sensor-1 and regulates
RT exocytosis.";
RL Hum. Mol. Genet. 12:1415-1425(2003).
RN [9]
RP INVOLVEMENT IN XLID21.
RX PubMed=16470793; DOI=10.1002/ajmg.a.31107;
RA Tabolacci E., Pomponi M.G., Pietrobono R., Terracciano A., Chiurazzi P.,
RA Neri G.;
RT "A truncating mutation in the IL1RAPL1 gene is responsible for X-linked
RT mental retardation in the MRX21 family.";
RL Am. J. Med. Genet. A 140:482-487(2006).
RN [10]
RP VARIANTS ARG-379; HIS-618; SER-637 AND VAL-643.
RX PubMed=18801879; DOI=10.1093/hmg/ddn300;
RA Piton A., Michaud J.L., Peng H., Aradhya S., Gauthier J., Mottron L.,
RA Champagne N., Lafreniere R.G., Hamdan F.F., Joober R., Fombonne E.,
RA Marineau C., Cossette P., Dube M.P., Haghighi P., Drapeau P., Barker P.A.,
RA Carbonetto S., Rouleau G.A.;
RT "Mutations in the calcium-related gene IL1RAPL1 are associated with
RT autism.";
RL Hum. Mol. Genet. 17:3965-3974(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 403-561, FUNCTION, AND
RP DIMERIZATION.
RX PubMed=15123616; DOI=10.1074/jbc.m403434200;
RA Khan J.A., Brint E.K., O'Neill L.A.J., Tong L.;
RT "Crystal structure of the Toll/interleukin-1 receptor domain of human IL-
RT 1RAPL.";
RL J. Biol. Chem. 279:31664-31670(2004).
CC -!- FUNCTION: May regulate secretion and presynaptic differentiation
CC through inhibition of the activity of N-type voltage-gated calcium
CC channel (PubMed:12783849). May activate the MAP kinase JNK
CC (PubMed:15123616). Plays a role in neurite outgrowth (By similarity).
CC During dendritic spine formation can bidirectionally induce pre- and
CC post-synaptic differentiation of neurons by trans-synaptically binding
CC to PTPRD (By similarity). {ECO:0000250|UniProtKB:P59823,
CC ECO:0000250|UniProtKB:P59824, ECO:0000269|PubMed:12783849,
CC ECO:0000269|PubMed:15123616}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC -!- SUBUNIT: Homodimer (PubMed:15123616). Interacts (calcium-independent)
CC with NCS1 (PubMed:12783849). Interacts (via the first immunoglobilin
CC domain) with PTPRD (via the second immunoglobilin domain); this
CC interaction is PTPRD-splicing-dependent and induces pre- and post-
CC synaptic differentiation of neurons and is required for IL1RAPL1-
CC mediated synapse formation (By similarity).
CC {ECO:0000250|UniProtKB:P59823, ECO:0000269|PubMed:12783849,
CC ECO:0000269|PubMed:15123616}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12783849};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:12783849}.
CC Cytoplasm {ECO:0000269|PubMed:12783849}. Cell projection, axon
CC {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=May
CC localize to the cell body and growth cones of dendrite-like processes.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q9NZN1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Detected at low levels in heart, skeletal muscle,
CC ovary, skin, amygdala, caudate nucleus, corpus callosum, hippocampus,
CC substantia nigra and thalamus. Detected at very low levels in tonsil,
CC prostate, testis, small intestine, placenta, colon and fetal liver.
CC {ECO:0000269|PubMed:10471494, ECO:0000269|PubMed:10882729}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked 21 (XLID21)
CC [MIM:300143]: A disorder characterized by significantly below average
CC general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC Intellectual deficiency is the only primary symptom of non-syndromic X-
CC linked forms, while syndromic intellectual disability presents with
CC associated physical, neurological and/or psychiatric manifestations.
CC {ECO:0000269|PubMed:10757639, ECO:0000269|PubMed:16470793}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; AJ243874; CAB56046.1; -; mRNA.
DR EMBL; AF181284; AAF59411.1; -; mRNA.
DR EMBL; AF284435; AAG21369.1; -; mRNA.
DR EMBL; AB102650; BAC81119.1; -; mRNA.
DR EMBL; AC005748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW99046.1; -; Genomic_DNA.
DR EMBL; BC126345; AAI26346.1; -; mRNA.
DR EMBL; BC126347; AAI26348.1; -; mRNA.
DR CCDS; CCDS14218.1; -. [Q9NZN1-1]
DR RefSeq; NP_055086.1; NM_014271.3. [Q9NZN1-1]
DR RefSeq; XP_016884729.1; XM_017029240.1. [Q9NZN1-1]
DR PDB; 1T3G; X-ray; 2.30 A; A/B=403-561.
DR PDB; 4M92; X-ray; 1.60 A; B=207-222.
DR PDB; 5WY8; X-ray; 3.07 A; B=27-349.
DR PDBsum; 1T3G; -.
DR PDBsum; 4M92; -.
DR PDBsum; 5WY8; -.
DR AlphaFoldDB; Q9NZN1; -.
DR SMR; Q9NZN1; -.
DR BioGRID; 116313; 6.
DR IntAct; Q9NZN1; 1.
DR STRING; 9606.ENSP00000368278; -.
DR GlyGen; Q9NZN1; 6 sites.
DR iPTMnet; Q9NZN1; -.
DR PhosphoSitePlus; Q9NZN1; -.
DR BioMuta; IL1RAPL1; -.
DR DMDM; 34222654; -.
DR EPD; Q9NZN1; -.
DR MassIVE; Q9NZN1; -.
DR PaxDb; Q9NZN1; -.
DR PeptideAtlas; Q9NZN1; -.
DR PRIDE; Q9NZN1; -.
DR ProteomicsDB; 83457; -. [Q9NZN1-1]
DR Antibodypedia; 433; 239 antibodies from 27 providers.
DR DNASU; 11141; -.
DR Ensembl; ENST00000378993.6; ENSP00000368278.1; ENSG00000169306.10. [Q9NZN1-1]
DR GeneID; 11141; -.
DR KEGG; hsa:11141; -.
DR MANE-Select; ENST00000378993.6; ENSP00000368278.1; NM_014271.4; NP_055086.1.
DR CTD; 11141; -.
DR DisGeNET; 11141; -.
DR GeneCards; IL1RAPL1; -.
DR GeneReviews; IL1RAPL1; -.
DR HGNC; HGNC:5996; IL1RAPL1.
DR HPA; ENSG00000169306; Tissue enriched (brain).
DR MalaCards; IL1RAPL1; -.
DR MIM; 300143; phenotype.
DR MIM; 300206; gene.
DR neXtProt; NX_Q9NZN1; -.
DR OpenTargets; ENSG00000169306; -.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA29812; -.
DR VEuPathDB; HostDB:ENSG00000169306; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT01050000244913; -.
DR HOGENOM; CLU_025552_0_1_1; -.
DR InParanoid; Q9NZN1; -.
DR OMA; WRSSIVF; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; Q9NZN1; -.
DR TreeFam; TF333913; -.
DR PathwayCommons; Q9NZN1; -.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-HSA-9007892; Interleukin-38 signaling.
DR SignaLink; Q9NZN1; -.
DR SIGNOR; Q9NZN1; -.
DR BioGRID-ORCS; 11141; 10 hits in 697 CRISPR screens.
DR ChiTaRS; IL1RAPL1; human.
DR EvolutionaryTrace; Q9NZN1; -.
DR GeneWiki; IL1RAPL1; -.
DR GenomeRNAi; 11141; -.
DR Pharos; Q9NZN1; Tbio.
DR PRO; PR:Q9NZN1; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NZN1; protein.
DR Bgee; ENSG00000169306; Expressed in buccal mucosa cell and 87 other tissues.
DR ExpressionAtlas; Q9NZN1; baseline and differential.
DR Genevisible; Q9NZN1; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; NAS:BHF-UCL.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0005102; F:signaling receptor binding; ISS:BHF-UCL.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:BHF-UCL.
DR GO; GO:0045920; P:negative regulation of exocytosis; IDA:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:BHF-UCL.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:BHF-UCL.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0099545; P:trans-synaptic signaling by trans-synaptic complex; IDA:SynGO.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.40.50.10140; -; 1.
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; IPR015621; IL-1_rcpt_fam.
DR InterPro; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain;
KW Intellectual disability; Membrane; NAD; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..696
FT /note="Interleukin-1 receptor accessory protein-like 1"
FT /id="PRO_0000015454"
FT TOPO_DOM 19..357
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..134
FT /note="Ig-like C2-type 1"
FT DOMAIN 143..232
FT /note="Ig-like C2-type 2"
FT DOMAIN 242..350
FT /note="Ig-like C2-type 3"
FT DOMAIN 403..559
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 549..644
FT /note="Interaction with NCS1"
FT /evidence="ECO:0000269|PubMed:12783849"
FT REGION 659..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT SITE 34
FT /note="Essential for interaction with PTPRD"
FT /evidence="ECO:0000250|UniProtKB:P59823"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..126
FT /evidence="ECO:0000250|UniProtKB:P59823"
FT DISULFID 53..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 143..185
FT /evidence="ECO:0000250|UniProtKB:P59823"
FT DISULFID 164..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 267..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 379
FT /note="K -> R (in dbSNP:rs138267399)"
FT /evidence="ECO:0000269|PubMed:18801879"
FT /id="VAR_062263"
FT VARIANT 618
FT /note="Q -> H (in dbSNP:rs890627874)"
FT /evidence="ECO:0000269|PubMed:18801879"
FT /id="VAR_062264"
FT VARIANT 637
FT /note="T -> S (in dbSNP:rs756672167)"
FT /evidence="ECO:0000269|PubMed:18801879"
FT /id="VAR_062265"
FT VARIANT 643
FT /note="I -> V (in dbSNP:rs746481663)"
FT /evidence="ECO:0000269|PubMed:18801879"
FT /id="VAR_062266"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:5WY8"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:5WY8"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 73..84
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:5WY8"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 126..136
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5WY8"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:5WY8"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 223..234
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:5WY8"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 312..323
FT /evidence="ECO:0007829|PDB:5WY8"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 330..338
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:5WY8"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:1T3G"
FT HELIX 426..431
FT /evidence="ECO:0007829|PDB:1T3G"
FT HELIX 433..440
FT /evidence="ECO:0007829|PDB:1T3G"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:1T3G"
FT HELIX 459..468
FT /evidence="ECO:0007829|PDB:1T3G"
FT STRAND 470..477
FT /evidence="ECO:0007829|PDB:1T3G"
FT HELIX 479..483
FT /evidence="ECO:0007829|PDB:1T3G"
FT TURN 484..487
FT /evidence="ECO:0007829|PDB:1T3G"
FT HELIX 488..492
FT /evidence="ECO:0007829|PDB:1T3G"
FT HELIX 494..501
FT /evidence="ECO:0007829|PDB:1T3G"
FT STRAND 504..511
FT /evidence="ECO:0007829|PDB:1T3G"
FT HELIX 518..529
FT /evidence="ECO:0007829|PDB:1T3G"
FT STRAND 532..538
FT /evidence="ECO:0007829|PDB:1T3G"
FT HELIX 542..545
FT /evidence="ECO:0007829|PDB:1T3G"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:1T3G"
FT HELIX 550..558
FT /evidence="ECO:0007829|PDB:1T3G"
SQ SEQUENCE 696 AA; 79969 MW; 9B7A0B503D73CCA9 CRC64;
MKAPIPHLIL LYATFTQSLK VVTKRGSADG CTDWSIDIKK YQVLVGEPVR IKCALFYGYI
RTNYSLAQSA GLSLMWYKSS GPGDFEEPIA FDGSRMSKEE DSIWFRPTLL QDSGLYACVI
RNSTYCMKVS ISLTVGENDT GLCYNSKMKY FEKAELSKSK EISCRDIEDF LLPTREPEIL
WYKECRTKTW RPSIVFKRDT LLIREVREDD IGNYTCELKY GGFVVRRTTE LTVTAPLTDK
PPKLLYPMES KLTIQETQLG DSANLTCRAF FGYSGDVSPL IYWMKGEKFI EDLDENRVWE
SDIRILKEHL GEQEVSISLI VDSVEEGDLG NYSCYVENGN GRRHASVLLH KRELMYTVEL
AGGLGAILLL LVCLVTIYKC YKIEIMLFYR NHFGAEELDG DNKDYDAYLS YTKVDPDQWN
QETGEEERFA LEILPDMLEK HYGYKLFIPD RDLIPTGTYI EDVARCVDQS KRLIIVMTPN
YVVRRGWSIF ELETRLRNML VTGEIKVILI ECSELRGIMN YQEVEALKHT IKLLTVIKWH
GPKCNKLNSK FWKRLQYEMP FKRIEPITHE QALDVSEQGP FGELQTVSAI SMAAATSTAL
ATAHPDLRST FHNTYHSQMR QKHYYRSYEY DVPPTGTLPL TSIGNQHTYC NIPMTLINGQ
RPQTKSSREQ NPDEAHTNSA ILPLLPRETS ISSVIW
