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NEL1_YEAST
ID   NEL1_YEAST              Reviewed;         630 AA.
AC   P38769; D3DKY2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=GTPase-activating protein NEL1 {ECO:0000303|PubMed:24947508};
DE   AltName: Full=Non-ERES-localized SEC23 homolog 1 {ECO:0000303|PubMed:24947508};
GN   Name=NEL1 {ECO:0000303|PubMed:24947508}; OrderedLocusNames=YHR035W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   FUNCTION, MUTAGENESIS OF ARG-592, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=24947508; DOI=10.1074/jbc.m114.553917;
RA   Kodera C., Yorimitsu T., Sato K.;
RT   "Sec23 homolog Nel1 is a novel GTPase-activating protein for Sar1 but does
RT   not function as a subunit of the coat protein complex II (COPII) coat.";
RL   J. Biol. Chem. 289:21423-21432(2014).
CC   -!- FUNCTION: Acts as a GTPase-activating protein (GAP) for SAR1
CC       (PubMed:24947508). Contrary to its SEC23 homolog, NEL1 does not
CC       associate with SEC24 and its homologs, nor does it associate with the
CC       COPII components, suggesting that it is unlikely that NEL1 functions as
CC       a structural component of the vesicle coat machinery (PubMed:24947508).
CC       May function as a signaling molecule (PubMed:24947508).
CC       {ECO:0000269|PubMed:24947508}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24947508}. Nucleus
CC       {ECO:0000269|PubMed:24947508}. Note=Is diffusely localized throughout
CC       the cytosol, and does not accumulate at ER exit sites (ERES).
CC       {ECO:0000269|PubMed:24947508}.
CC   -!- DISRUPTION PHENOTYPE: Leads to a significant growth defect in the
CC       temperature-sensitive SAR1-D32G mutant background.
CC       {ECO:0000269|PubMed:24947508}.
CC   -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U00062; AAB68909.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06726.1; -; Genomic_DNA.
DR   PIR; S46740; S46740.
DR   RefSeq; NP_011900.1; NM_001179165.1.
DR   AlphaFoldDB; P38769; -.
DR   SMR; P38769; -.
DR   BioGRID; 36466; 70.
DR   DIP; DIP-806N; -.
DR   IntAct; P38769; 3.
DR   MINT; P38769; -.
DR   STRING; 4932.YHR035W; -.
DR   iPTMnet; P38769; -.
DR   PaxDb; P38769; -.
DR   PRIDE; P38769; -.
DR   EnsemblFungi; YHR035W_mRNA; YHR035W; YHR035W.
DR   GeneID; 856430; -.
DR   KEGG; sce:YHR035W; -.
DR   SGD; S000001077; NEL1.
DR   VEuPathDB; FungiDB:YHR035W; -.
DR   eggNOG; KOG1986; Eukaryota.
DR   GeneTree; ENSGT00390000006916; -.
DR   HOGENOM; CLU_463922_0_0_1; -.
DR   InParanoid; P38769; -.
DR   OMA; VIDTICE; -.
DR   BioCyc; YEAST:G3O-31095-MON; -.
DR   PRO; PR:P38769; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38769; protein.
DR   GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR036180; Gelsolin-like_dom_sf.
DR   InterPro; IPR037364; Sec23.
DR   InterPro; IPR006896; Sec23/24_trunk_dom.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   PANTHER; PTHR11141; PTHR11141; 1.
DR   Pfam; PF04811; Sec23_trunk; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF82754; SSF82754; 1.
DR   SUPFAM; SSF82919; SSF82919; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; GTPase activation; Nucleus; Reference proteome.
FT   CHAIN           1..630
FT                   /note="GTPase-activating protein NEL1"
FT                   /id="PRO_0000202891"
FT   MUTAGEN         592
FT                   /note="R->A: Abolishes the GAP activity."
FT                   /evidence="ECO:0000269|PubMed:24947508"
SQ   SEQUENCE   630 AA;  72307 MW;  C42D24351D4FA75D CRC64;
     MCSPTNFLYE PFSSDAVTQN YDQNLKCTKC GAYYSMACSL REQNVWTCLF CNQSNSNAEL
     PLVPSNTYTL TSAKKEILSR RTIMIIDAIC DPHELNYLVS ILCNNYITRQ QEPLSIITIQ
     QSGHVILHNA VNHRRDAVFS INEFMTKYNL DKLNASYFEK KISEINQESY WFDKSTQGSL
     RKLLREICKI ANKVNISSKR DKRCTGLALF VSSVLASQCS LSAYCHIVSF LNGPCTKGGG
     KVMSRERGES MRQNHHFESK SSQLQLSKSP TKFYKKMLEK FANQSLIYEF FIASLDQIGI
     LEMSPLITSS MAVSQFDSFN DERFAMSFQK YLNLRDHNAI YNCHSKIMTA KNAIVVKDFP
     KYSLNPKNLS LPLEISLGHN SAEAPIQFQT TFENQTEKYI RIETLLLPKA NRSFGAQNEI
     VFSMKKIASR IIDSFAYSSK HTKELMKQLF LLPNQIRGKD VDMVNLIQWC YHIYRSPILS
     VRNTSPDERY LFLHRIINAS KDTCLSLCKP FIWSYSDLKH DWIVLDVPLT RAQILQDDKT
     TICVDGGSYL VLRRGKLLEK EGRELCCKLL NDLQRFPQPL YVETKTGGSQ DRFLKSKIIP
     LDITDKETLG TEDMTFNEYF NLFTDLSGSK
 
 
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