ID IRPL1_PONPY Reviewed; 696 AA.
AC Q7YQL9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 22-FEB-2023, entry version 100.
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; Synonyms=OPHN4;
OS Pongo pygmaeus (Bornean orangutan).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
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).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P59823, ECO:0000250|UniProtKB:P59824,
CC ECO:0000250|UniProtKB:Q9NZN1}.
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:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell
CC projection, axon {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}. Note=May localize to the cell body and growth cones of
CC dendrite-like processes. {ECO:0000250}.
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; AB102652; BAC81121.1; -; mRNA.
DR AlphaFoldDB; Q7YQL9; -.
DR SMR; Q7YQL9; -.
DR GlyCosmos; Q7YQL9; 6 sites, No reported glycans.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
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:0045920; P:negative regulation of exocytosis; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00096; Ig; 1.
DR CDD; cd05896; Ig1_IL1RAPL-1_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 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:SF22; INTERLEUKIN-1 RECEPTOR ACCESSORY PROTEIN-LIKE 1; 1.
DR PANTHER; PTHR11890; INTERLEUKIN-1 RECEPTOR FAMILY MEMBER; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01537; INTRLKN1R1F.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 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; Repeat; Signal;
KW 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_0000015457"
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 1"
FT DOMAIN 143..232
FT /note="Ig-like 2"
FT DOMAIN 242..350
FT /note="Ig-like 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; 79937 MW; 0332FE0C31C2D4E1 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
PPKLLYPVES 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
//
