IRL1B_DANRE
ID IRL1B_DANRE Reviewed; 700 AA.
AC B6ZK77;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Interleukin-1 receptor accessory protein-like 1-B;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE Flags: Precursor;
GN Name=il1rapl1b;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF PRO-455.
RX PubMed=18657618; DOI=10.1016/j.mcn.2008.06.013;
RA Yoshida T., Mishina M.;
RT "Zebrafish orthologue of mental retardation protein IL1RAPL1 regulates
RT presynaptic differentiation.";
RL Mol. Cell. Neurosci. 39:218-228(2008).
CC -!- FUNCTION: May regulate secretion and presynaptic differentiation
CC through inhibition of the activity of N-type voltage-gated calcium
CC channel. During presynaptic differentiation may regulate both synaptic
CC vesicle accumulation in axon terminals and subsequent axon terminal
CC remodeling. {ECO:0000269|PubMed:18657618}.
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: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=May
CC localize to the cell body and growth cones of dendrite-like processes.
CC {ECO:0000269|PubMed:18657618}.
CC -!- DEVELOPMENTAL STAGE: Detectable at 24 hpf and gradually increases
CC through development. Detected in the nervous system in olfactory
CC placode, olfactory bulb, telencephalon and tectum.
CC {ECO:0000269|PubMed:18657618}.
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; AB449368; BAG85347.1; -; mRNA.
DR RefSeq; NP_001136054.1; NM_001142582.1.
DR AlphaFoldDB; B6ZK77; -.
DR SMR; B6ZK77; -.
DR STRING; 7955.ENSDARP00000099490; -.
DR PaxDb; B6ZK77; -.
DR GeneID; 557801; -.
DR KEGG; dre:557801; -.
DR CTD; 557801; -.
DR ZFIN; ZDB-GENE-090109-2; il1rapl1b.
DR eggNOG; KOG3971; Eukaryota.
DR InParanoid; B6ZK77; -.
DR OrthoDB; 651291at2759; -.
DR PhylomeDB; B6ZK77; -.
DR Reactome; R-DRE-388844; Receptor-type tyrosine-protein phosphatases.
DR Reactome; R-DRE-9007892; Interleukin-38 signaling.
DR PRO; PR:B6ZK77; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0043679; C:axon terminus; IDA:ZFIN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:ZFIN.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0016322; P:neuron remodeling; IMP:ZFIN.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0050808; P:synapse organization; IMP:ZFIN.
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; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11890; PTHR11890; 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 Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase;
KW Immunoglobulin domain; Membrane; NAD; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..700
FT /note="Interleukin-1 receptor accessory protein-like 1-B"
FT /id="PRO_0000390563"
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..700
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..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 564..700
FT /note="Required for synaptic vesicle accumulation during
FT synaptogenesis"
FT ACT_SITE 491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
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 53..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 164..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 267..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 455
FT /note="P->H: Unable to induce axon terminal remodeling."
FT /evidence="ECO:0000269|PubMed:18657618"
SQ SEQUENCE 700 AA; 80314 MW; 4871CC6BE227C51A CRC64;
MRSRVPLQIL LYAAVIRSLK VVSKRGSVDG CTDWSVDYLR YRVLLGEPVR IKCALFYGYI
RANYTHAQSA GLSLMWYRSA THTDHEEPIT LDGTRTLKEE DALWFRPAQL QDSGHYSCVL
RNSSYCMKVS MALTVAENSS GLCYNSKMRR LEKAELSKSK DILCPDIQDY TPAGSEPHVT
WYKECRPKQW RSSIIRTADL LSIRDVREDD IGNYTCEIQF GRFLVRRTTE LTVTAPLTDK
PPKILQPPEH KLSVMELQLG GPVNLTCRAF FGYSGDVSPL IYWMKGEKFI EDLDETRIRE
SEIKMVREHL GEQEVSVSLT IDSLQEEDLG NYSCYVENGH GRRHAIIQLS RRELMYTVEL
AGGLGAILLM LIFLVSLYKC YRIELMLFYR NHFGSEDVDG ENKDYDAYVS YTKVDPDQWS
QETREEEHFA LEILPDMLEK HYGYKLFIPD RDLIPTGTYI EDVARCVDQS KRLIIVMTPN
YVVRRGWSIF ELETRLRNML VSGEIKVILI ECSDLRGIMN YQEVEALKHT IKLLTVIRWP
GPGSSKPNSR FWKQLQYEMP FRRPEPKLSH EQVLDASEQG PFGELQTVSA LSMVSATSTA
MATAHPDLRS GFHNTYNTQL RQKHYYRGYE YDIPSSGTLP PLATMGSQHT YCNIPMSLLN
GQRPPGQPAH GQQQSLEEQQ VNNALLPLLP RETSISSVIW
