ID Q5I9W0_CAEEL Unreviewed; 984 AA.
AC Q5I9W0;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase {ECO:0000256|ARBA:ARBA00011982};
DE EC=3.2.2.6 {ECO:0000256|ARBA:ARBA00011982};
GN Name=tir-1 {ECO:0000313|EMBL:CTQ86566.1,
GN ECO:0000313|WormBase:F13B10.1f};
GN ORFNames=CELE_F13B10.1 {ECO:0000313|EMBL:CTQ86566.1}, F13B10.1
GN {ECO:0000313|WormBase:F13B10.1f};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:AAV91313.1};
RN [1] {ECO:0000313|EMBL:CTQ86566.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CTQ86566.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000313|EMBL:CTQ86566.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CTQ86566.1};
RA Sulson J.E., Waterston R.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAV91313.1}
RP NUCLEOTIDE SEQUENCE.
RA Chuang C.-F., Bargmann C.I.;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AAV91313.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15625192; DOI=10.1101/gad.1276505;
RA Chuang C.-F., Bargmann C.I.;
RT "A Toll-interleukin 1 repeat protein at the synapse specifies asymmetric
RT odorant receptor expression via ASK1 MAPKKK signaling.";
RL Genes Dev. 19:270-281(2005).
RN [5] {ECO:0000313|EMBL:CTQ86566.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CTQ86566.1};
RG WormBase Consortium;
RA WormBase;
RL Submitted (AUG-2023) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000256|ARBA:ARBA00000404};
CC -!- SIMILARITY: Belongs to the SARM1 family.
CC {ECO:0000256|ARBA:ARBA00008291}.
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DR EMBL; AY834227; AAV91313.1; -; mRNA.
DR EMBL; BX284603; CTQ86566.1; -; Genomic_DNA.
DR RefSeq; NP_001299866.1; NM_001312937.1.
DR SMR; Q5I9W0; -.
DR EnsemblMetazoa; F13B10.1f.1; F13B10.1f.1; WBGene00006575.
DR GeneID; 175502; -.
DR AGR; WB:WBGene00006575; -.
DR WormBase; F13B10.1f; CE50709; WBGene00006575; tir-1.
DR OMA; ANIIEGC; -.
DR OrthoDB; 5475697at2759; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006575; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
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:0035591; F:signaling adaptor activity; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0019677; P:NAD catabolic process; IEA:UniProt.
DR GO; GO:0034128; P:negative regulation of MyD88-independent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048678; P:response to axon injury; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09501; SAM_SARM1-like_repeat1; 1.
DR CDD; cd09502; SAM_SARM1-like_repeat2; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR039184; SARM1.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR22998:SF1; NAD(+) HYDROLASE SARM1; 1.
DR PANTHER; PTHR22998; SARM1; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF13676; TIR_2; 1.
DR SMART; SM00454; SAM; 2.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 2.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CTQ86566.1};
KW Immunity {ECO:0000256|ARBA:ARBA00022588};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Proteomics identification {ECO:0007829|EPD:Q5I9W0,
KW ECO:0007829|PeptideAtlas:Q5I9W0}; Receptor {ECO:0000313|EMBL:AAV91313.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 614..678
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 760..905
FT /note="TIR"
FT /evidence="ECO:0000259|PROSITE:PS50104"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 110890 MW; EA33ECEC79EC26FA CRC64;
MLPNRKPPRP SPSFQSLNNN NQRFPLRRSL KIAQAHSLPT VPSEDAKDDD LITPELSTDF
DFREIQHRYL MALQNEQDGE TTSTDDAFFE LDDDDDLSSP SVPGSPVDPP SISVPLPPKS
APPCPTQPAP LTNGDLYPTI LSNGTPIPNG RITPALSTVS VSLIHEARLQ QSLSTPCNGS
EEEMHNGQVR KESEYRRFKS EGSTAGASLP AAEKTHMDEL SPVDQRSTSG TARFLIQQDS
VVNPSTKMSN TEQVAMMHTL KTKLSKYQAM MDKAFEEIAK VEDANIIEGC TIVRKLMRKV
WNTPKVSADL ANALCDYLRD RDYFDKLIKM FISPNTAACD QVRMECGKVL EECTSSANLE
YIVNKSYTKK IMIVAMKLNK TPDQQRLSLS LIGNLFKHSN AVSLSLIETD VIDHIILTFK
RAPECPDILR HAALALANIL LYTCFEGKKK IIQKKIPEWL FFLASQADDV TRYYACIAVC
TIVSVKEFEP LVRKSDTMKL VEPFLQVHDP ATFARDYHKY AQGNTKEWLE RLLPMLQPSR
RREARSVAAF HFTLEATIKK EQNKLDVFQE IGAIQALKEV ASSPDEVAAK FASEALTVIG
EEVPYKLAQQ VPGWTCADVQ YWVKKIGFEE YVEKFAKQMV DGDLLLQLTE NDLKHDVGMI
SGLHRKRFLR ELQTLKVAAD YSSVDESNLD NFLMGLSPEL SVYTYQMLTN GVNRSLLSSL
TDEMMQNACG ITNPIHRLKL TQAFETAKHP DDVEVAMLSK QIDVFISYRR STGNQLASLI
KVLLQLRGYR VFIDVDKLYA GKFDSSLLKN IQAAKHFILV LTPNSLDRLL NDDNCEDWVH
KELKCAFEHQ KNIIPIFDTA FEFPTKEDQI PNDIRMITKY NGVKWVHDYQ DACMAKVVRF
ITGELNRTTP TTKEMPSISR KTTQQRWQTT NTVSRTGPSR SIGGPRMEPP TPTFFSVTPT
GSQERATSTR RKIQPSASTT SDRN
//
