ID H2UVQ9_TAKRU Unreviewed; 716 AA.
AC H2UVQ9;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=NAD(+) hydrolase SARM1 {ECO:0000256|ARBA:ARBA00024128};
DE EC=3.2.2.6 {ECO:0000256|ARBA:ARBA00011982};
DE AltName: Full=NADP(+) hydrolase SARM1 {ECO:0000256|ARBA:ARBA00032222};
DE AltName: Full=Sterile alpha and TIR motif-containing protein 1 {ECO:0000256|ARBA:ARBA00031160};
GN Name=sarm1 {ECO:0000313|Ensembl:ENSTRUP00000041037.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000041037.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000041037.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000041037.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) +
CC nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58673; Evidence={ECO:0000256|ARBA:ARBA00023911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850;
CC Evidence={ECO:0000256|ARBA:ARBA00023911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) = cyclic ADP-beta-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:38611, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:73672;
CC Evidence={ECO:0000256|ARBA:ARBA00034259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38612;
CC Evidence={ECO:0000256|ARBA:ARBA00034259};
CC -!- SIMILARITY: Belongs to the SARM1 family.
CC {ECO:0000256|ARBA:ARBA00008291}.
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DR AlphaFoldDB; H2UVQ9; -.
DR STRING; 31033.ENSTRUP00000085736; -.
DR Ensembl; ENSTRUT00000041180.3; ENSTRUP00000041037.3; ENSTRUG00000016046.3.
DR GeneTree; ENSGT00390000004155; -.
DR HOGENOM; CLU_003286_2_0_1; -.
DR Proteomes; UP000005226; Chromosome 11.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Immunity {ECO:0000256|ARBA:ARBA00022588};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..716
FT /note="NAD(+) hydrolase SARM1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025402019"
FT DOMAIN 414..478
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 558..701
FT /note="TIR"
FT /evidence="ECO:0000259|PROSITE:PS50104"
SQ SEQUENCE 716 AA; 80747 MW; BFD01EA050ED9F64 CRC64;
MLFSLTLFLW RLYRHFATMF SSERLTVPDY VSRLQRGRSG SGSGSGSDPR AVSPGIAADI
QEVLDTSLPA LRGAIRKLRT GNEHSHSEET RTAIAEIFQL VEEAWVLPTV GRQVAEEICN
RIRLEGGLEL LLQLQQTPDV EIIYESAKLL EQILVSENRD YLAKMGLGVI LNLTRQQEDA
QLARSVSGIL EHMFKHTEET SIHLISNGAL DALLFWCRGT DPTVLRHCAV ALANCAMYGG
HRCQRWMIEK QAAEWLFPLA FSKEDEIIRF HACLAVTVLA TNREIEKEVV KSGTLELVEP
FIASLDPDDF LRSLLDSADC MQGKTAADLQ HFLPLLDGRR VEGKCIAAFY LCVEASIKSR
QRNTKIFQEI GAVQSLKRIV MYSSNGTASS LAKRALRMMG EEVPKRILPS VPNWKTCEVQ
TWLQQVGFSA FCNRFQELQV DGDLLLNITD QDLSADLGMT AGLTRKRFLR DLRVLKTYAN
YSTCDPHNMA DWLSEVDPHF RQYTYGLVQS GVNHNNVQSL TEQQLQHDCQ IINGVHRAKI
LSCSCKPLKP SHTDAQPAGP DVFVSYRRTT GSQLASLLKV HLQVRGYSVF IDVEKLEAGK
FEDKLIQSVQ RARNFILVLS SSALDKCKGD TAMKDWVHKE IVTALNSKKN IVPVTDNFIW
PDPLSLPEDM RAILNFNGVK WSHEYQEATI EKILRFLKGQ HDQMDSPYTP QEKNKL
//
