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SPF1_YEAST
ID   SPF1_YEAST              Reviewed;        1215 AA.
AC   P39986; D3DLL8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 200.
DE   RecName: Full=Endoplasmic reticulum transmembrane helix translocase {ECO:0000305};
DE            EC=7.4.2.- {ECO:0000269|PubMed:32973005};
DE   AltName: Full=Complexed with DOR1 protein 1 {ECO:0000303|PubMed:12058017};
DE   AltName: Full=Endoplasmic reticulum P5A-ATPase {ECO:0000303|PubMed:32973005};
DE   AltName: Full=Sensitivity to the P.farinosa killer toxin protein 1 {ECO:0000303|PubMed:10361284};
GN   Name=SPF1 {ECO:0000303|PubMed:10361284, ECO:0000312|SGD:S000000757};
GN   Synonyms=COD1 {ECO:0000303|PubMed:12058017}; OrderedLocusNames=YEL031W;
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=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
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   DISRUPTION PHENOTYPE.
RX   PubMed=10361284; DOI=10.1046/j.1365-2958.1999.01400.x;
RA   Suzuki C., Shimma Y.;
RT   "P-type ATPase spf1 mutants show a novel resistance mechanism for the
RT   killer toxin SMKT.";
RL   Mol. Microbiol. 32:813-823(1999).
RN   [4]
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12058017; DOI=10.1083/jcb.200203052;
RA   Cronin S.R., Rao R., Hampton R.Y.;
RT   "Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+
RT   homeostasis.";
RL   J. Cell Biol. 157:1017-1028(2002).
RN   [5]
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   [6]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-936, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [8]
RP   ATPASE ACTIVITY, ACTIVE SITE, COFACTOR, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF ASP-487.
RX   PubMed=22745129; DOI=10.1074/jbc.m112.363465;
RA   Corradi G.R., de Tezanos Pinto F., Mazzitelli L.R., Adamo H.P.;
RT   "Shadows of an absent partner: ATP hydrolysis and phosphoenzyme turnover of
RT   the Spf1 (sensitivity to Pichia farinosa killer toxin) P5-ATPase.";
RL   J. Biol. Chem. 287:30477-30484(2012).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=22918956; DOI=10.1091/mbc.e11-12-0994;
RA   Krumpe K., Frumkin I., Herzig Y., Rimon N., Oezbalci C., Bruegger B.,
RA   Rapaport D., Schuldiner M.;
RT   "Ergosterol content specifies targeting of tail-anchored proteins to
RT   mitochondrial outer membranes.";
RL   Mol. Biol. Cell 23:3927-3935(2012).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   ATPASE ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF ASP-487.
RX   PubMed=24392018; DOI=10.1371/journal.pone.0085519;
RA   Cohen Y., Megyeri M., Chen O.C., Condomitti G., Riezman I.,
RA   Loizides-Mangold U., Abdul-Sada A., Rimon N., Riezman H., Platt F.M.,
RA   Futerman A.H., Schuldiner M.;
RT   "The yeast p5 type ATPase, spf1, regulates manganese transport into the
RT   endoplasmic reticulum.";
RL   PLoS ONE 8:E85519-E85519(2013).
RN   [12]
RP   ATPASE ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, ACTIVE SITE,
RP   AND MUTAGENESIS OF ASP-487.
RX   PubMed=30785834; DOI=10.1091/mbc.e18-06-0365;
RA   Soerensen D.M., Holen H.W., Pedersen J.T., Martens H.J., Silvestro D.,
RA   Stanchev L.D., Costa S.R., Guenther Pomorski T., Lopez-Marques R.L.,
RA   Palmgren M.;
RT   "The P5A ATPase Spf1p is stimulated by phosphatidylinositol 4-phosphate and
RT   influences cellular sterol homeostasis.";
RL   Mol. Biol. Cell 30:1069-1084(2019).
RN   [13]
RP   ATPASE ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASP-487.
RX   PubMed=32353073; DOI=10.1371/journal.pone.0232476;
RA   Corradi G.R., Mazzitelli L.R., Petrovich G.D., Grenon P., Soerensen D.M.,
RA   Palmgren M., de Tezanos Pinto F., Adamo H.P.;
RT   "Reduction of the P5A-ATPase Spf1p phosphoenzyme by a Ca2+-dependent
RT   phosphatase.";
RL   PLoS ONE 15:e0232476-e0232476(2020).
RN   [14]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM
RP   AND NON-HYDROLYZABLE ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   AND DOMAIN.
RX   PubMed=32973005; DOI=10.1126/science.abc5809;
RA   McKenna M.J., Sim S.I., Ordureau A., Wei L., Harper J.W., Shao S., Park E.;
RT   "The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase.";
RL   Science 369:0-0(2020).
CC   -!- FUNCTION: Endoplasmic reticulum translocase required to remove
CC       mitochondrial transmembrane proteins mistargeted to the endoplasmic
CC       reticulum (PubMed:22918956, PubMed:32973005). Acts as a dislocase that
CC       mediates the ATP-dependent extraction of mislocalized mitochondrial
CC       transmembrane proteins from the endoplasmic reticulum membrane
CC       (PubMed:32973005). Specifically binds mitochondrial tail-anchored
CC       transmembrane proteins: has an atypically large substrate-binding
CC       pocket that recognizes and binds moderately hydrophobic transmembranes
CC       with short hydrophilic lumenal domains (PubMed:32973005).
CC       {ECO:0000269|PubMed:22918956, ECO:0000269|PubMed:32973005}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-with a C-terminal TM segment(out) + ATP + H2O =
CC         [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:66168, Rhea:RHEA-COMP:16963, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:90782, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:32973005};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:22745129, ECO:0000269|PubMed:32973005};
CC   -!- ACTIVITY REGULATION: The ATPase activity is stimulated by
CC       phosphatidylinositol 4-phosphate (PI4P). {ECO:0000269|PubMed:30785834}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:12058017, ECO:0000269|PubMed:22745129,
CC       ECO:0000269|PubMed:24392018, ECO:0000269|PubMed:30785834}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:32973005}. Note=Localizes to
CC       endoplasmic reticulum regions devoid of phosphatidylinositol 4-
CC       phosphate (PI4P) hydrolytic machinery. {ECO:0000269|PubMed:30785834}.
CC   -!- DOMAIN: Contains a large substrate-binding pocket that recognizes
CC       alpha-helical transmembranes, which alternately faces the endoplasmic
CC       reticulum lumen and cytosol, while remaining accessible to the lipid
CC       bilayer through a lateral opening (PubMed:32973005). The translocase
CC       alternates between two conformations: inward-open (E1) and outward-open
CC       (E2) states (PubMed:32973005). Undergoes a series of conformational
CC       changes with ATP-binding, phosphorylation of the Asp active site and
CC       subsequent dephosphorylation in a Post-Albers cycle (i.e., E1 -> E1-ATP
CC       -> E1P-ADP -> E1P -> E2P -> E2-Pi -> E1) (PubMed:32973005). A substrate
CC       transmembrane helix with a short, preferentially positively charged
CC       lumenal segment binds to the outward-open pocket and the E2P-to-E1
CC       transition flips the transmembrane by a switch from the outward-open to
CC       inward-open conformation (PubMed:32973005).
CC       {ECO:0000269|PubMed:32973005}.
CC   -!- DISRUPTION PHENOTYPE: Impaired mitochondrial transmembrane tail-
CC       anchored protein localization, characterized by mitochondrial
CC       transmembrane tail-anchored protein accumulation at the endoplasmic
CC       reticulum (PubMed:22918956). In addition, a wide spectrum of phenotypes
CC       is observed, including induction of the endoplasmic reticulum unfolded
CC       protein response, defects in lipid and sterol homeostasis, and
CC       dysregulated protein N-glycosylation, topogenesis and turnover
CC       (PubMed:12058017, PubMed:22918956, PubMed:24392018).
CC       {ECO:0000269|PubMed:12058017, ECO:0000269|PubMed:22918956,
CC       ECO:0000269|PubMed:24392018}.
CC   -!- MISCELLANEOUS: Present with 1870 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type V subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was initially thought to mediate ion transport such as calcium
CC       or manganese (PubMed:12058017, PubMed:24392018). However, different
CC       publications have shown that it does not act as an ion transporter
CC       (PubMed:22745129, PubMed:32353073, PubMed:32973005). Specifically binds
CC       moderately hydrophobic transmembrane with short hydrophilic lumenal
CC       domains that misinsert into the endoplasmic reticulum
CC       (PubMed:32973005). {ECO:0000269|PubMed:12058017,
CC       ECO:0000269|PubMed:22745129, ECO:0000269|PubMed:24392018,
CC       ECO:0000269|PubMed:32353073, ECO:0000269|PubMed:32973005}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Wrong place - Issue 234 of
CC       March 2021;
CC       URL="https://web.expasy.org/spotlight/back_issues/234/";
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DR   EMBL; U18530; AAB64508.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07622.1; -; Genomic_DNA.
DR   PIR; S50428; S50428.
DR   RefSeq; NP_010883.3; NM_001178846.3.
DR   PDB; 6XMP; EM; 3.50 A; A=1-1215.
DR   PDB; 6XMQ; EM; 3.70 A; A=1-1215.
DR   PDB; 6XMS; EM; 3.40 A; A=1-1215.
DR   PDB; 6XMT; EM; 3.30 A; A=1-1215.
DR   PDB; 6XMU; EM; 3.30 A; A=1-1215.
DR   PDBsum; 6XMP; -.
DR   PDBsum; 6XMQ; -.
DR   PDBsum; 6XMS; -.
DR   PDBsum; 6XMT; -.
DR   PDBsum; 6XMU; -.
DR   AlphaFoldDB; P39986; -.
DR   SMR; P39986; -.
DR   BioGRID; 36698; 483.
DR   DIP; DIP-6637N; -.
DR   IntAct; P39986; 3.
DR   STRING; 4932.YEL031W; -.
DR   TCDB; 3.A.3.10.3; the p-type atpase (p-atpase) superfamily.
DR   CarbonylDB; P39986; -.
DR   iPTMnet; P39986; -.
DR   MaxQB; P39986; -.
DR   PaxDb; P39986; -.
DR   PRIDE; P39986; -.
DR   EnsemblFungi; YEL031W_mRNA; YEL031W; YEL031W.
DR   GeneID; 856681; -.
DR   KEGG; sce:YEL031W; -.
DR   SGD; S000000757; SPF1.
DR   VEuPathDB; FungiDB:YEL031W; -.
DR   eggNOG; KOG0209; Eukaryota.
DR   GeneTree; ENSGT00550000075064; -.
DR   HOGENOM; CLU_001828_4_1_1; -.
DR   InParanoid; P39986; -.
DR   OMA; RNPMEKF; -.
DR   BioCyc; YEAST:G3O-30153-MON; -.
DR   Reactome; R-SCE-936837; Ion transport by P-type ATPases.
DR   PRO; PR:P39986; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P39986; protein.
DR   GO; GO:0005801; C:cis-Golgi network; IDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR   GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR   GO; GO:0140567; F:transmembrane protein dislocase activity; IDA:UniProtKB.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:SGD.
DR   GO; GO:0030026; P:cellular manganese ion homeostasis; IMP:SGD.
DR   GO; GO:0140569; P:extraction of mislocalized protein from ER membrane; IDA:UniProtKB.
DR   GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0043335; P:protein unfolding; IDA:UniProtKB.
DR   GO; GO:0055092; P:sterol homeostasis; IMP:SGD.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006544; P-type_TPase_V.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Endoplasmic reticulum; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Protein transport;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..1215
FT                   /note="Endoplasmic reticulum transmembrane helix
FT                   translocase"
FT                   /id="PRO_0000046349"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        28..43
FT                   /note="Helical; Name=TMa"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        44..56
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        57..76
FT                   /note="Helical; Name=TMb"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        77..188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        189..216
FT                   /note="Helical; Name=TM1"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        217
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        218..246
FT                   /note="Helical; Name=TM2"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        247..395
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        396..425
FT                   /note="Helical; Name=TM3"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        426..427
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        428..442
FT                   /note="Helical; Name=TM4a"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        446..464
FT                   /note="Helical; Name=TM4b"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        465..971
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        972..1011
FT                   /note="Helical; Name=TM5"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        1012..1017
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        1018..1035
FT                   /note="Helical; Name=TM6"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        1036..1055
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        1056..1084
FT                   /note="Helical; Name=TM7"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        1085..1099
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        1100..1121
FT                   /note="Helical; Name=TM8"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        1122..1133
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        1134..1151
FT                   /note="Helical; Name=TM9"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        1152..1168
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TRANSMEM        1169..1197
FT                   /note="Helical; Name=TM10"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   TOPO_DOM        1198..1215
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   REGION          156..185
FT                   /note="A-domain; part 1"
FT                   /evidence="ECO:0000303|PubMed:32973005"
FT   REGION          250..390
FT                   /note="A-domain; part 2"
FT                   /evidence="ECO:0000303|PubMed:32973005"
FT   REGION          466..495
FT                   /note="P-domain; part 1"
FT                   /evidence="ECO:0000303|PubMed:32973005"
FT   REGION          497..674
FT                   /note="N-domain"
FT                   /evidence="ECO:0000303|PubMed:32973005"
FT   REGION          677..837
FT                   /note="P-domain; part 2"
FT                   /evidence="ECO:0000303|PubMed:32973005"
FT   REGION          838..953
FT                   /note="Arm-like"
FT                   /evidence="ECO:0000303|PubMed:32973005"
FT   REGION          954..969
FT                   /note="P-domain; part 3"
FT                   /evidence="ECO:0000303|PubMed:32973005"
FT   ACT_SITE        487
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000305|PubMed:22745129,
FT                   ECO:0000305|PubMed:24392018, ECO:0000305|PubMed:30785834,
FT                   ECO:0000305|PubMed:32353073"
FT   BINDING         487..489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   BINDING         487
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   BINDING         582
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT   BINDING         634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   BINDING         699
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   BINDING         816..820
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   BINDING         816
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000305|PubMed:32973005"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         936
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         487
FT                   /note="D->N: Loss of ATPase activity."
FT                   /evidence="ECO:0000269|PubMed:22745129,
FT                   ECO:0000269|PubMed:24392018, ECO:0000269|PubMed:30785834,
FT                   ECO:0000269|PubMed:32353073"
FT   STRAND          12..20
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           29..43
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           58..73
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           75..77
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           79..85
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:6XMP"
FT   TURN            93..95
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          98..103
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          111..114
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:6XMP"
FT   STRAND          127..130
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   TURN            139..142
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   TURN            150..152
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           157..161
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           173..177
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           189..196
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           200..213
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           219..246
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:6XMS"
FT   STRAND          256..260
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          263..267
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          269..271
FT                   /evidence="ECO:0007829|PDB:6XMS"
FT   STRAND          277..280
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          291..297
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          299..303
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   TURN            304..308
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          314..316
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          319..322
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          324..326
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           333..337
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          344..349
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          361..363
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          365..371
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           373..375
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           377..387
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          392..395
FT                   /evidence="ECO:0007829|PDB:6XMP"
FT   HELIX           397..424
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           428..440
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           447..462
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           463..465
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          467..470
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           472..474
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           476..479
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          483..486
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   TURN            490..492
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          498..501
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          510..513
FT                   /evidence="ECO:0007829|PDB:6XMP"
FT   HELIX           523..531
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          539..541
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          543..545
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           547..556
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          562..564
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          569..571
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          574..579
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          584..586
FT                   /evidence="ECO:0007829|PDB:6XMU"
FT   STRAND          591..594
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          599..605
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           607..611
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           621..629
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          630..632
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          637..642
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           656..659
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          664..667
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          670..672
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           679..687
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   TURN            688..690
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          692..696
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           701..711
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          718..729
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          732..740
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          742..744
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   TURN            747..749
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           754..757
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   TURN            758..760
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          762..765
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           767..771
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   TURN            772..775
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           779..783
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          785..789
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           796..807
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          813..815
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          817..819
FT                   /evidence="ECO:0007829|PDB:6XMP"
FT   HELIX           821..826
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          827..833
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           838..853
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   TURN            956..961
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          963..968
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           973..1009
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   TURN            1010..1013
FT                   /evidence="ECO:0007829|PDB:6XMU"
FT   HELIX           1019..1034
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          1053..1055
FT                   /evidence="ECO:0007829|PDB:6XMS"
FT   HELIX           1056..1083
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           1100..1118
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   TURN            1124..1126
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           1130..1132
FT                   /evidence="ECO:0007829|PDB:6XMU"
FT   HELIX           1134..1151
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           1156..1161
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   HELIX           1170..1196
FT                   /evidence="ECO:0007829|PDB:6XMT"
FT   STRAND          1198..1200
FT                   /evidence="ECO:0007829|PDB:6XMP"
FT   TURN            1204..1206
FT                   /evidence="ECO:0007829|PDB:6XMT"
SQ   SEQUENCE   1215 AA;  135269 MW;  7A9960D34B91B5AE CRC64;
     MTKKSFVSSP IVRDSTLLVP KSLIAKPYVL PFFPLYATFA QLYFQQYDRY IKGPEWTFVY
     LGTLVSLNIL VMLMPAWNVK IKAKFNYSTT KNVNEATHIL IYTTPNNGSD GIVEIQRVTE
     AGSLQTFFQF QKKRFLWHEN EQVFSSPKFL VDESPKIGDF QKCKGHSGDL THLKRLYGEN
     SFDIPIPTFM ELFKEHAVAP LFVFQVFCVA LWLLDEFWYY SLFNLFMIIS MEAAAVFQRL
     TALKEFRTMG IKPYTINVFR NKKWVALQTN ELLPMDLVSI TRTAEESAIP CDLILLDGSA
     IVNEAMLSGE STPLLKESIK LRPSEDNLQL DGVDKIAVLH GGTKALQVTP PEHKSDIPPP
     PDGGALAIVT KTGFETSQGS LVRVMIYSAE RVSVDNKEAL MFILFLLIFA VIASWYVWVE
     GTKMGRIQSK LILDCILIIT SVVPPELPME LTMAVNSSLA ALAKFYVYCT EPFRIPFAGR
     IDVCCFDKTG TLTGEDLVFE GLAGISADSE NIRHLYSAAE APESTILVIG AAHALVKLED
     GDIVGDPMEK ATLKAVGWAV ERKNSNYREG TGKLDIIRRF QFSSALKRSA SIASHNDALF
     AAVKGAPETI RERLSDIPKN YDEIYKSFTR SGSRVLALAS KSLPKMSQSK IDDLNRDDVE
     SELTFNGFLI FHCPLKDDAI ETIKMLNESS HRSIMITGDN PLTAVHVAKE VGIVFGETLI
     LDRAGKSDDN QLLFRDVEET VSIPFDPSKD TFDHSKLFDR YDIAVTGYAL NALEGHSQLR
     DLLRHTWVYA RVSPSQKEFL LNTLKDMGYQ TLMCGDGTND VGALKQAHVG IALLNGTEEG
     LKKLGEQRRL EGMKMMYIKQ TEFMARWNQP QPPVPEPIAH LFPPGPKNPH YLKALESKGT
     VITPEIRKAV EEANSKPVEV IKPNGLSEKK PADLASLLLN SAGDAQGDEA PALKLGDASC
     AAPFTSKLAN VSAVTNIIRQ GRCALVNTIQ MYKILALNCL ISAYSLSIIY MAGVKFGDGQ
     ATVSGLLLSV CFLSISRGKP LEKLSKQRPQ SGIFNVYIMG SILSQFAVHI ATLVYITTEI
     YKLEPREPQV DLEKEFAPSL LNTGIFIIQL VQQVSTFAVN YQGEPFRENI RSNKGMYYGL
     LGVTGLALAS ATEFLPELNE AMKFVPMTDD FKIKLTLTLL LDFFGSWGVE HFFKFFFMDD
     KPSDISVQQV KIASK
 
 
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