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NSF_CAEEL
ID   NSF_CAEEL               Reviewed;         824 AA.
AC   Q94392;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=Vesicle-fusing ATPase;
DE            EC=3.6.4.6;
DE   AltName: Full=N-ethylmaleimide-sensitive fusion protein;
DE            Short=NEM-sensitive fusion protein;
DE   AltName: Full=Vesicular-fusion protein NSF;
GN   Name=nsf-1; ORFNames=H15N14.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion
CC       of transport vesicles within the Golgi cisternae. Is also required for
CC       transport from the endoplasmic reticulum to the Golgi stack. Seems to
CC       function as a fusion protein required for the delivery of cargo
CC       proteins to all compartments of the Golgi stack independent of vesicle
CC       origin (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P18708};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P18708};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q94392; Q22227: mig-5; NbExp=3; IntAct=EBI-316816, EBI-316403;
CC       Q94392; Q27488: pas-2; NbExp=3; IntAct=EBI-316816, EBI-318271;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; Z96100; CAB09531.1; -; Genomic_DNA.
DR   EMBL; Z79698; CAB09531.1; JOINED; Genomic_DNA.
DR   PIR; T23096; T23096.
DR   RefSeq; NP_001076603.1; NM_001083134.3.
DR   AlphaFoldDB; Q94392; -.
DR   SMR; Q94392; -.
DR   BioGRID; 57330; 6.
DR   DIP; DIP-24326N; -.
DR   IntAct; Q94392; 4.
DR   STRING; 6239.H15N14.2a; -.
DR   EPD; Q94392; -.
DR   PaxDb; Q94392; -.
DR   PeptideAtlas; Q94392; -.
DR   PRIDE; Q94392; -.
DR   EnsemblMetazoa; H15N14.2a.1; H15N14.2a.1; WBGene00003818.
DR   GeneID; 266842; -.
DR   KEGG; cel:CELE_H15N14.2; -.
DR   UCSC; H15N14.2a; c. elegans.
DR   CTD; 266842; -.
DR   WormBase; H15N14.2a; CE19925; WBGene00003818; nsf-1.
DR   eggNOG; KOG0741; Eukaryota.
DR   GeneTree; ENSGT00530000064085; -.
DR   InParanoid; Q94392; -.
DR   OMA; IQHVKGM; -.
DR   OrthoDB; 197562at2759; -.
DR   PhylomeDB; Q94392; -.
DR   Reactome; R-CEL-204005; COPII-mediated vesicle transport.
DR   Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-CEL-6811438; Intra-Golgi traffic.
DR   Reactome; R-CEL-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   SignaLink; Q94392; -.
DR   PRO; PR:Q94392; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00003818; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   ExpressionAtlas; Q94392; baseline and differential.
DR   GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR004201; Cdc48_dom2.
DR   InterPro; IPR029067; CDC48_domain_2-like_sf.
DR   InterPro; IPR003338; CDC4_N-term_subdom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039812; Vesicle-fus_ATPase.
DR   PANTHER; PTHR23078; PTHR23078; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF02933; CDC48_2; 1.
DR   Pfam; PF02359; CDC48_N; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01073; CDC48_N; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54585; SSF54585; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Protein transport; Reference proteome; Repeat;
KW   Transport.
FT   CHAIN           1..824
FT                   /note="Vesicle-fusing ATPase"
FT                   /id="PRO_0000084565"
FT   BINDING         582..587
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P18708"
FT   BINDING         622..629
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P18708"
FT   BINDING         627
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P18708"
SQ   SEQUENCE   824 AA;  91335 MW;  67232C5115B0B03A CRC64;
     MSPVPCLSTC CCFRKIVEYS TMSWFRKSAN DSLLETNHDR IPVAPPREVR APSPRLPPSY
     QTSNEKMFRV RKAPSEEHTL ANYAYVNRSD FDDKQIKHVR VNPGPAHHYI FSIRNDGSIK
     PGEIAFGVPH RKWAALSLDQ EVRVTPFTFQ QSEYVGSMIL TADFNAKKNV TSEPLNADLM
     AREFSIQFGG QAFSKGMQMA FRFEDKEKNK THTLSLVVKS IEGFDIGKAA AAASGASNTD
     SSATKPKQIE AGELLPNSVI VFDKEEGSML NLIGKSKGKS AYRSIINPDW DFQQMGIGGL
     DTEFSHIFRR AFASRVFPPE FIEQLGMKHV RGILLFGPPG TGKTLMARQI GKMLNAREPK
     IVNGPQILDK YVGESESNVR KLFADAEEEW RRCGANSGLH IIIFDEIDAI CKQRGSMAGS
     SSVHDTVVNQ LLSKMDGVEQ LNNILVIGMT NRRDMIDEAL LRPGRLEVQM EVSLPDETGR
     LQILKIHTAR MREYNKMDPN VDLEDISKRT KNFSGAELEG LVRAAQSSAM NRLVKAGGKA
     QADPDAIEKL AINSGDFDYA LENDIKPAFG RSDESLNRFL SRGMIVWGPE VTKILDEGSL
     LAATVKNPEN SGFRTVVLAG AAKTGKTSLA AQMAKSSDFP FVKVISPEDT VGFSESAKCM
     ALKKAFEDAK RSKLSVLLID NLERLIDYHP VGPRYSNLVI QALLVLLNAP PPAGHRLFVI
     ATSSDRMFLR DMGLMDVFGD VIDIPKLTTA GQMMNVIQES NIYSDDQLPM IEQKLASICR
     GEGFHGVGIK HLLELIESAR QCEADYRVPT LLNMMEGLAL NLYR
 
 
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