IRPL2_MOUSE
ID IRPL2_MOUSE Reviewed; 686 AA.
AC Q9ERS6; Q9ER66;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=X-linked interleukin-1 receptor accessory protein-like 2;
DE Short=IL-1 receptor accessory protein-like 2;
DE Short=IL-1-RAPL-2;
DE Short=IL-1RAPL-2;
DE Short=IL1RAPL-2;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=IL1RAPL-2-related protein;
DE AltName: Full=Three immunoglobulin domain-containing IL-1 receptor-related 1;
DE Short=TIGIRR-1;
DE Flags: Precursor;
GN Name=Il1rapl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11587848; DOI=10.1016/s0378-1119(01)00659-x;
RA Ferrante M.I., Ghiani M., Bulfone A., Franco B.;
RT "IL1RAPL2 maps to Xq22 and is specifically expressed in the central nervous
RT system.";
RL Gene 275:217-221(2001).
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 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ERS6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ERS6-2; Sequence=VSP_008056, VSP_008057;
CC -!- TISSUE SPECIFICITY: Detected in fetal brain after day 12.5, in
CC particular in parts of the diencephalon and in the basal plate of the
CC spinal cord. In postnatal brain detected in cerebral cortex, olfactory
CC bulb, in the CA1 region of the hippocampus and in Purkinje cells of the
CC Xth cerebellar lobule. {ECO:0000269|PubMed:11587848}.
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 -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the interleukin-1 receptor 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; AF284437; AAG21371.1; -; mRNA.
DR EMBL; AJ277831; CAC10559.1; -; mRNA.
DR CCDS; CCDS30429.1; -. [Q9ERS6-1]
DR RefSeq; NP_109613.1; NM_030688.2. [Q9ERS6-1]
DR AlphaFoldDB; Q9ERS6; -.
DR SMR; Q9ERS6; -.
DR STRING; 10090.ENSMUSP00000108686; -.
DR GlyGen; Q9ERS6; 5 sites.
DR iPTMnet; Q9ERS6; -.
DR PhosphoSitePlus; Q9ERS6; -.
DR PaxDb; Q9ERS6; -.
DR PRIDE; Q9ERS6; -.
DR ProteomicsDB; 268997; -. [Q9ERS6-1]
DR ProteomicsDB; 268998; -. [Q9ERS6-2]
DR Antibodypedia; 35255; 284 antibodies from 30 providers.
DR DNASU; 60367; -.
DR Ensembl; ENSMUST00000075471; ENSMUSP00000074917; ENSMUSG00000059203. [Q9ERS6-1]
DR Ensembl; ENSMUST00000113063; ENSMUSP00000108686; ENSMUSG00000059203. [Q9ERS6-1]
DR GeneID; 60367; -.
DR KEGG; mmu:60367; -.
DR UCSC; uc009ujt.1; mouse. [Q9ERS6-2]
DR UCSC; uc009ujv.1; mouse. [Q9ERS6-1]
DR CTD; 26280; -.
DR MGI; MGI:1913106; Il1rapl2.
DR VEuPathDB; HostDB:ENSMUSG00000059203; -.
DR eggNOG; KOG3971; Eukaryota.
DR GeneTree; ENSGT01050000244913; -.
DR HOGENOM; CLU_025552_0_1_1; -.
DR InParanoid; Q9ERS6; -.
DR OMA; DYHQADS; -.
DR PhylomeDB; Q9ERS6; -.
DR TreeFam; TF333913; -.
DR Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR BioGRID-ORCS; 60367; 2 hits in 58 CRISPR screens.
DR ChiTaRS; Il1rapl2; mouse.
DR PRO; PR:Q9ERS6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9ERS6; protein.
DR Bgee; ENSMUSG00000059203; Expressed in regional part of spinal cord and 46 other tissues.
DR ExpressionAtlas; Q9ERS6; baseline and differential.
DR Genevisible; Q9ERS6; MM.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004910; F:interleukin-1, type II, blocking receptor activity; IEA:InterPro.
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:1905606; P:regulation of presynapse assembly; ISO:MGI.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR015621; IL-1_rcpt_fam.
DR InterPro; IPR004077; IL-1_rcpt_II-typ.
DR InterPro; IPR041416; IL-1RAcP-like_ig.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11890; PTHR11890; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01539; INTRLEUKN1R2.
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 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase;
KW Immunoglobulin domain; Membrane; NAD; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..686
FT /note="X-linked interleukin-1 receptor accessory protein-
FT like 2"
FT /id="PRO_0000015460"
FT TOPO_DOM 17..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..132
FT /note="Ig-like C2-type 1"
FT DOMAIN 141..232
FT /note="Ig-like C2-type 2"
FT DOMAIN 239..347
FT /note="Ig-like C2-type 3"
FT DOMAIN 400..556
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT ACT_SITE 488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 162..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 265..331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 350..354
FT /note="DLIYK -> GILFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11587848"
FT /id="VSP_008056"
FT VAR_SEQ 355..686
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11587848"
FT /id="VSP_008057"
SQ SEQUENCE 686 AA; 78798 MW; 36160D1CDE9B8264 CRC64;
MKLPLLLALV VCSAVSTNLK MVSKRNSVDG CIDWSVDLKT YMALAGEPVR VKCALFYSYI
RTNYSMAQST GLRLMWYRNK GDLEEPIIFS EVRMSKEEDA IWFHSAEEQD SGFYTCVLRN
STYCMKVSMS LTVAENESGL CYNSRIRYLE KSEVTKRKEI SCPDMDDFKK SDQEPDVVWY
KECKPKMWRS IIIQKGNALL IQEVQEEDGG NYTCELKYEG KLVRRTTELK VTALLTDKPP
KPLFPMENQP SVIDVQLGKP LNIPCKAFFG FSGESGPMIY WMKGEKFIEE LAGHIREGEI
RLLKEHLGEK EVELTLIFDS VVEADLANYT CHVENRNGRK HASVLLRKKD LIYKIELAGG
LGAIFLLLIL LLVVYKCYNI ELMLFYRQRF GGDETTDDNK EYDAYLSYTK VDQDTLDCDN
TEEEQFALEI LPDVLEKHYG YKLFIPERDL IPSGTYIEDL TRCVEQSRRL IIVLTPDYIL
RRGWSIFELE SRLHNMLVSG EIKVILIECT ELKGKVNCQE VESLKHNIKL LSLIKWKGPK
SSKLNSKFWK HLVYEMPIKK KEMLSHCHVL DSAEQGLFGE LQPIPSIAMT STSATMVPSQ
ADLPEFHHSD SMQMRHCCRG YQHEMPANTL SVPSLGNHHT YCNLPLTLLN GQLPLNNSLK
ETEEFSRNNP LLPLTSKELS FTSDIW
