IRPL1_RAT
ID IRPL1_RAT Reviewed; 696 AA.
AC P59824;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Hippocampus;
RA Boda B., Parisi L., Muller D.;
RT "Full length cloning of rat IL1RAPL in the hippocampus.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=17502602; DOI=10.1073/pnas.0701133104;
RA Gambino F., Pavlowsky A., Begle A., Dupont J.-L., Bahi N., Courjaret R.,
RA Gardette R., Hadjkacem H., Skala H., Poulain B., Chelly J., Vitale N.,
RA Humeau Y.;
RT "IL1-receptor accessory protein-like 1 (IL1RAPL1), a protein involved in
RT cognitive functions, regulates N-type Ca2+-channel and neurite
RT elongation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9063-9068(2007).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: May regulate secretion and presynaptic differentiation
CC through inhibition of the activity of N-type voltage-gated calcium
CC channel (PubMed:17502602). May activate the MAP kinase JNK (By
CC similarity). Plays a role in neurite outgrowth (PubMed:18801879).
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:Q9NZN1, ECO:0000269|PubMed:17502602,
CC ECO:0000269|PubMed:18801879}.
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 (By similarity). 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 (By similarity).
CC {ECO:0000250|UniProtKB:P59823, ECO:0000250|UniProtKB:Q9NZN1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18801879};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:18801879}.
CC Cytoplasm {ECO:0000269|PubMed:18801879}. 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 -!- 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; AY216593; AAO62634.1; -; mRNA.
DR RefSeq; NP_808796.1; NM_177935.2.
DR AlphaFoldDB; P59824; -.
DR SMR; P59824; -.
DR STRING; 10116.ENSRNOP00000068289; -.
DR CarbonylDB; P59824; -.
DR GlyGen; P59824; 6 sites.
DR iPTMnet; P59824; -.
DR PhosphoSitePlus; P59824; -.
DR SwissPalm; P59824; -.
DR PaxDb; P59824; -.
DR PRIDE; P59824; -.
DR GeneID; 317553; -.
DR KEGG; rno:317553; -.
DR CTD; 11141; -.
DR RGD; 727891; Il1rapl1.
DR eggNOG; KOG3971; Eukaryota.
DR InParanoid; P59824; -.
DR PhylomeDB; P59824; -.
DR Reactome; R-RNO-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-RNO-9007892; Interleukin-38 signaling.
DR PRO; PR:P59824; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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; ISO:RGD.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR GO; GO:0045920; P:negative regulation of exocytosis; IDA:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0097105; P:presynaptic membrane assembly; ISO:RGD.
DR GO; GO:0010975; P:regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0099175; P:regulation of postsynapse organization; ISO:RGD.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0099545; P:trans-synaptic signaling by trans-synaptic complex; ISO:RGD.
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 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasm; Disulfide bond; Glycoprotein;
KW 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..696
FT /note="Interleukin-1 receptor accessory protein-like 1"
FT /id="PRO_0000015458"
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..696
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..559
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 549..644
FT /note="Interaction with NCS1"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 696 AA; 79771 MW; 3684FCCD0A0B3FD9 CRC64;
MKAPIPHLIL LYATFTQSLK VVTKRGSADG CTDWSVDIKK YQVLVGEPVR IKCALFYGYI
RTNYTLAQSA GLSLMWYKSS GPGDFEEPIA FDGSRMSKEE DSIWFRPTLL QDSGLYACVI
RNSTYCMKVS ISLTVGENDT GLCYNSKMKY FEKAELSKSK EISCRDIEDF LLPTREPEIL
WYKECRTKTW RPSIVFKRDT LLIKEVKEDD IGNYTCELKY GGFVVRRTTE LTVTAPLTDK
PPKLLYPMES KLTIQETQLG GSANLTCRAF FGYSGDVSPL IYWMKGEKFI EDLDENRVWE
SDIRILKEHL GEQEVSISLI VDSVEEGDLG NYSCYVENGN GRRHASVLLH KRELMYTVEL
AGGLGAILLL LVCSVTIYKC 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
RPQTKSSREP NPDEAHTNSA ILPLLARETS ISSVIW
