IRL1A_DANRE
ID IRL1A_DANRE Reviewed; 701 AA.
AC B6ZK76; Q08BS0;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Interleukin-1 receptor accessory protein-like 1-A;
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE Flags: Precursor;
GN Name=il1rapl1a; ORFNames=zgc:152866;
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], AND DEVELOPMENTAL STAGE.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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.
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:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B6ZK76-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B6ZK76-2; Sequence=VSP_038547;
CC -!- DEVELOPMENTAL STAGE: Maternally provided it is detected at all tested
CC stages of development. {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; AB449367; BAG85346.1; -; mRNA.
DR EMBL; BC124594; AAI24595.1; -; mRNA.
DR RefSeq; NP_001071044.1; NM_001077576.1.
DR RefSeq; XP_005174755.1; XM_005174698.3. [B6ZK76-2]
DR RefSeq; XP_009303034.1; XM_009304759.2. [B6ZK76-2]
DR RefSeq; XP_009303035.1; XM_009304760.2. [B6ZK76-2]
DR RefSeq; XP_017213199.1; XM_017357710.1. [B6ZK76-2]
DR AlphaFoldDB; B6ZK76; -.
DR SMR; B6ZK76; -.
DR STRING; 7955.ENSDARP00000117551; -.
DR PaxDb; B6ZK76; -.
DR Ensembl; ENSDART00000089206; ENSDARP00000083639; ENSDARG00000115285. [B6ZK76-1]
DR GeneID; 568868; -.
DR KEGG; dre:568868; -.
DR CTD; 568868; -.
DR ZFIN; ZDB-GENE-061013-249; il1rapl1a.
DR eggNOG; KOG3971; Eukaryota.
DR InParanoid; B6ZK76; -.
DR OrthoDB; 651291at2759; -.
DR PhylomeDB; B6ZK76; -.
DR PRO; PR:B6ZK76; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR Bgee; ENSDARG00000115285; Expressed in multicellular organism and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004908; F:interleukin-1 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:0045920; P:negative regulation of exocytosis; IBA:GO_Central.
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; IPR004074; IL-1_rcpt_I/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; PF18452; Ig_6; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR01536; INTRLKN1R12F.
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; Cell membrane; Cytoplasm; Disulfide bond;
KW Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane; NAD; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..701
FT /note="Interleukin-1 receptor accessory protein-like 1-A"
FT /id="PRO_0000390562"
FT TOPO_DOM 20..361
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..701
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..133
FT /note="Ig-like C2-type 1"
FT DOMAIN 146..235
FT /note="Ig-like C2-type 2"
FT DOMAIN 245..353
FT /note="Ig-like C2-type 3"
FT DOMAIN 407..563
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 568..701
FT /note="Required for synaptic vesicle accumulation during
FT synaptogenesis"
FT /evidence="ECO:0000250"
FT ACT_SITE 495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 167..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 270..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 462
FT /note="T -> SMSSQHYQDDTHLLRA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_038547"
FT CONFLICT 42
FT /note="Y -> C (in Ref. 2; AAI24595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 79647 MW; 08B38920D4542584 CRC64;
MTALNPVLFL LCGVSVSLSL KVVSKRGSVD GCTDWSVDYL KYRVLHGEPV RIKCALFYGY
IRANYTQAQS IGLSLMWYRS SGLGHGDFEE PISFDGTRMS KEEDAIWFRP AELQDAGLYS
CVLRNSTFCM KVSMTLLVAD NDTAGCYNSK LRYTEKGELG KSKDISCPDI QDYVQPGEKP
QITWYKECNV QQWRSSVLQT ADLLAIQDVR EDDIGNYTCE LLFGGFLVRR TTYLSVTAPL
TEEPPRILFP SENKLLAMDV QLGSMLNLTC RAFFGYSGDI SPLVYWMKGE KFIEDMDQSR
IRESEIKTVR EHLGEQEVSI TLTIDSLEEV DLGNYSCYAE NGNGRRQANV QIGKRVELMY
TVELAGGLGA ILLLLALLLS VYKCYRIELL LCYRHHFGGE DTDGDNKEYD AYLSYSKVEL
DQWGQELQEE ERFALEILPD VLEKHYGYKL FIPDRDLIPT STYIEDVSRC VDMSKRLIIV
LTPSYVLRRG WSIFELESRL RNSLVSGDIK VILIECADLR GVINYQEVEE LKQSIKCLSV
VHWNGPQSNK PGSRFWKQLR YTMPYRRPQQ TITNHALDTS EPGPFADLQT VSAISMATAT
SAALAPAHPE LRPSLRSSYR SHSLARQKHS HYRSYDYELP FTAGGTLPPQ HTYCNLPLTL
LNGQRPVNNK TLRQHSLDEH HGNNAMLPLL PRETSISSVI W
