IRPL1_MOUSE
ID IRPL1_MOUSE Reviewed; 695 AA.
AC P59823;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 1.
DT 25-MAY-2022, entry version 128.
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=X-linked interleukin-1 receptor accessory protein-like 1;
DE Flags: Precursor;
GN Name=Il1rapl1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, INTERACTION WITH PTPRD, AND SUBCELLULAR LOCATION.
RX PubMed=21940441; DOI=10.1523/jneurosci.2136-11.2011;
RA Yoshida T., Yasumura M., Uemura T., Lee S.J., Ra M., Taguchi R.,
RA Iwakura Y., Mishina M.;
RT "IL-1 receptor accessory protein-like 1 associated with mental retardation
RT and autism mediates synapse formation by trans-synaptic interaction with
RT protein tyrosine phosphatase delta.";
RL J. Neurosci. 31:13485-13499(2011).
RN [4]
RP TISSUE SPECIFICITY.
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 [5] {ECO:0007744|PDB:4YH6, ECO:0007744|PDB:4YH7, ECO:0007744|PDB:5Y32}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 19-352 IN COMPLEX WITH PTPRD,
RP GLYCOSYLATION AT ASN-63; ASN-122; ASN-138; ASN-213 AND ASN-264, DISULFIDE
RP BONDS, SUBUNIT, INTERACTION WITH PTPRD, MUTAGENESIS OF TRP-34; ASP-37;
RP 75-MET--TYR-77; 88-PRO--PHE-91 AND ASP-292, SITE, AND FUNCTION.
RX PubMed=25908590; DOI=10.1038/ncomms7926;
RA Yamagata A., Yoshida T., Sato Y., Goto-Ito S., Uemura T., Maeda A.,
RA Shiroshima T., Iwasawa-Okamoto S., Mori H., Mishina M., Fukai S.;
RT "Mechanisms of splicing-dependent trans-synaptic adhesion by PTPdelta-
RT IL1RAPL1/IL-1RAcP for synaptic differentiation.";
RL Nat. Commun. 6:6926-6926(2015).
CC -!- FUNCTION: May regulate secretion and presynaptic differentiation
CC through inhibition of the activity of N-type voltage-gated calcium
CC channel. May activate the MAP kinase JNK (By similarity). Plays a role
CC in neurite outgrowth (By similarity). During dendritic spine formation
CC can bidirectionally induce pre- and post-synaptic differentiation of
CC neurons by trans-synaptically binding to PTPRD (PubMed:25908590,
CC PubMed:21940441). {ECO:0000250|UniProtKB:P59824,
CC ECO:0000250|UniProtKB:Q9NZN1, ECO:0000269|PubMed:21940441,
CC ECO:0000269|PubMed:25908590}.
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:25908590). Interacts (calcium-independent)
CC with NCS1/FREQ (By similarity). 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 (PubMed:25908590, PubMed:21940441).
CC {ECO:0000250|UniProtKB:Q9NZN1, ECO:0000269|PubMed:21940441,
CC ECO:0000269|PubMed:25908590}.
CC -!- INTERACTION:
CC P59823; Q64487: Ptprd; NbExp=6; IntAct=EBI-5452114, EBI-771834;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell
CC projection, axon {ECO:0000269|PubMed:21940441}. Cell projection,
CC dendrite {ECO:0000269|PubMed:21940441}. Note=May localize to the cell
CC body and growth cones of dendrite-like processes.
CC -!- TISSUE SPECIFICITY: Detected in total brain extracts, olfactory bulb,
CC hippocampus and striatum (at protein level).
CC {ECO:0000269|PubMed:12783849}.
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 -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC {ECO:0000305}.
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DR EMBL; AL844900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK081272; -; NOT_ANNOTATED_CDS; mRNA.
DR PDB; 4YH6; X-ray; 3.00 A; A/B=19-352.
DR PDB; 4YH7; X-ray; 4.40 A; B=19-352.
DR PDB; 5Y32; X-ray; 2.70 A; B=19-352.
DR PDBsum; 4YH6; -.
DR PDBsum; 4YH7; -.
DR PDBsum; 5Y32; -.
DR AlphaFoldDB; P59823; -.
DR SMR; P59823; -.
DR IntAct; P59823; 1.
DR STRING; 10090.ENSMUSP00000109599; -.
DR GlyConnect; 2411; 4 N-Linked glycans (2 sites).
DR GlyGen; P59823; 6 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; P59823; -.
DR PhosphoSitePlus; P59823; -.
DR PaxDb; P59823; -.
DR PRIDE; P59823; -.
DR ProteomicsDB; 269097; -.
DR MGI; MGI:2687319; Il1rapl1.
DR eggNOG; KOG3971; Eukaryota.
DR InParanoid; P59823; -.
DR Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-MMU-9007892; Interleukin-38 signaling.
DR ChiTaRS; Il1rapl1; mouse.
DR PRO; PR:P59823; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P59823; protein.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS: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; IPI:BHF-UCL.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL.
DR GO; GO:0045920; P:negative regulation of exocytosis; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IDA:BHF-UCL.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:BHF-UCL.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:UniProtKB.
DR GO; GO:0097105; P:presynaptic membrane assembly; IMP:BHF-UCL.
DR GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0099545; P:trans-synaptic signaling by trans-synaptic complex; 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; 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; Cell membrane; Cell projection; Cytoplasm; Disulfide bond;
KW Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane; NAD; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..695
FT /note="Interleukin-1 receptor accessory protein-like 1"
FT /id="PRO_0000015455"
FT TOPO_DOM 25..357
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..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..558
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 548..643
FT /note="Interaction with NCS1"
FT /evidence="ECO:0000250"
FT REGION 657..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT SITE 34
FT /note="Essential for interaction with PTPRD"
FT /evidence="ECO:0000269|PubMed:25908590"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:5Y32"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:4YH6, ECO:0007744|PDB:4YH7,
FT ECO:0007744|PDB:5Y32"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:4YH6, ECO:0007744|PDB:4YH7,
FT ECO:0007744|PDB:5Y32"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:4YH6, ECO:0007744|PDB:4YH7,
FT ECO:0007744|PDB:5Y32"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:4YH6, ECO:0007744|PDB:4YH7,
FT ECO:0007744|PDB:5Y32"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..126
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:4YH6, ECO:0007744|PDB:4YH7,
FT ECO:0007744|PDB:5Y32"
FT DISULFID 53..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25908590, ECO:0007744|PDB:4YH6,
FT ECO:0007744|PDB:4YH7, ECO:0007744|PDB:5Y32"
FT DISULFID 143..185
FT /evidence="ECO:0000269|PubMed:25908590,
FT ECO:0007744|PDB:4YH6, ECO:0007744|PDB:4YH7,
FT ECO:0007744|PDB:5Y32"
FT DISULFID 164..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25908590, ECO:0007744|PDB:4YH6,
FT ECO:0007744|PDB:4YH7, ECO:0007744|PDB:5Y32"
FT DISULFID 267..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:25908590, ECO:0007744|PDB:4YH6,
FT ECO:0007744|PDB:4YH7, ECO:0007744|PDB:5Y32"
FT MUTAGEN 34
FT /note="W->A: Abolishes Interaction with PTPRD. Abolishes
FT synaptogenesis."
FT /evidence="ECO:0000269|PubMed:25908590"
FT MUTAGEN 37
FT /note="D->A: Decreases affinity for PTPRD. Significantly
FT decreases synaptogenesis."
FT /evidence="ECO:0000269|PubMed:25908590"
FT MUTAGEN 75..77
FT /note="MWY->AWA: Decreases affinity for PTPRD; when
FT associated with 88-A--A-91. Significantly decreases
FT synaptogenesis; when associated with 88-A--A-91."
FT /evidence="ECO:0000269|PubMed:25908590"
FT MUTAGEN 88..91
FT /note="PIAF->AIAA: Decreases affinity for PTPRD; when
FT associated with 75-A--A-77. Significantly decreases
FT synaptogenesis; when associated with 88-A--A-91."
FT /evidence="ECO:0000269|PubMed:25908590"
FT MUTAGEN 292
FT /note="D->A: Decreases affinity for PTPRD. Significantly
FT decreases synaptogenesis."
FT /evidence="ECO:0000269|PubMed:25908590"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:5Y32"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5Y32"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:5Y32"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 126..136
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4YH6"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5Y32"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:5Y32"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 223..234
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 313..323
FT /evidence="ECO:0007829|PDB:5Y32"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 330..338
FT /evidence="ECO:0007829|PDB:5Y32"
FT STRAND 341..351
FT /evidence="ECO:0007829|PDB:5Y32"
SQ SEQUENCE 695 AA; 79630 MW; 5FE34F204E5908B7 CRC64;
MKAPIPHLIL LYATFTQSLK VVTKRGSADG CTDWSVDIKK YQVLVGEPVR IKCALFYGYI
RTNYSLAQSA GLSLMWYKSS GPGDFEEPIA FDGSRMSKEE DSIWFRPTLL QDSGLYACVI
RNSTYCMKVS ISLTVGENDT GLCYNSKMKY FEKAELSKSK EISCRDIEDF LLPTREPEIL
WYKECRTKAW RPSIVFKRDT LLIKEVKEDD IGNYTCELKY GGFVVRRTTE LTVTAPLTDK
PPKLLYPMES KLTVQETQLG GSANLTCRAF FGYSGDVSPL IYWMKGEKFI EDLDENRVWE
SDIRILKEHL GEQEVSISLI VDSVEEGDLG NYSCYVENGN GRRHASVLLH KRELMYTVEL
AGGLGAILLL LICSVTIYKC YKIEIMLFYR NHFGAEELDG DNKDYDAYLS YTKVDPDQWN
QETGEEERFA LEILPDMLEK HYGYKLFIPD RDLIPTGNIE DVARCVDQSK RLIIVMTPNY
VVRRGWSIFE LETRLRNMLV TGEIKVILIE CSELRGIMNY QEVEALKHTI KLLTVIKWHG
PKCNKLNSKF WKRLQYEMPF KRIEPITHEQ ALDVSEQGPF GELQTVSAIS MAAATSTALA
TAHPDLRSTF HNTYHSQMRQ KHYYRSYEYD VPPTGTLPLT SIGNQHTYCN IPMTLINGQR
PQTKSNREPN PDEAHTNSAI LPLLPRETSI SSVIW
