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ACA6_ORYSJ
ID   ACA6_ORYSJ              Reviewed;        1021 AA.
AC   Q65X71;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable calcium-transporting ATPase 6, plasma membrane-type {ECO:0000305};
DE            Short=OsACA6 {ECO:0000303|PubMed:24286292};
DE            EC=7.2.2.10;
DE   AltName: Full=Ca(2+)-ATPase isoform 6 {ECO:0000305};
GN   Name=ACA6 {ECO:0000303|PubMed:24286292};
GN   OrderedLocusNames=Os05g0495600, LOC_Os05g41580; ORFNames=OJ1579_G03.12;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=24286292; DOI=10.1111/febs.12656;
RA   Singh A., Kanwar P., Yadav A.K., Mishra M., Jha S.K., Baranwal V.,
RA   Pandey A., Kapoor S., Tyagi A.K., Pandey G.K.;
RT   "Genome-wide expressional and functional analysis of calcium transport
RT   elements during abiotic stress and development in rice.";
RL   FEBS J. 281:894-915(2014).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC       ATP coupled with the translocation of calcium from the cytosol out of
CC       the cell, into the endoplasmic reticulum, or into organelles.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.10;
CC   -!- ACTIVITY REGULATION: Activated by calmodulin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- DOMAIN: The N-terminus contains an autoinhibitory calmodulin-binding
CC       domain, which binds calmodulin in a calcium-dependent fashion.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIB subfamily. {ECO:0000305}.
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DR   EMBL; AC112160; AAU44048.1; -; Genomic_DNA.
DR   EMBL; AP014961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q65X71; -.
DR   SMR; Q65X71; -.
DR   STRING; 4530.OS05T0495600-00; -.
DR   PRIDE; Q65X71; -.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_2_1; -.
DR   InParanoid; Q65X71; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR024750; Ca_ATPase_N_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006408; P-type_ATPase_IIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   Pfam; PF12515; CaATP_NAI; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Calcium; Calcium transport; Calmodulin-binding; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..1021
FT                   /note="Probable calcium-transporting ATPase 6, plasma
FT                   membrane-type"
FT                   /id="PRO_0000247305"
FT   TOPO_DOM        1..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..384
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        807..827
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        828..829
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        830..850
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        879..899
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        900..942
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        943..963
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        974..994
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        995..1021
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        441
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         740
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         744
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1021 AA;  112681 MW;  DF3898A63D2F210F CRC64;
     MEGGRSWSIE SYLNEYFDIP AKNPPGEARR RWRRAVGLIV RNRRRRFGRF SDVDAIDEAQ
     RRKILVRVKQ YHLPPELIEE GFCISPDELA AIANMREDYT MLRMHGGING ISRKIKASLE
     DGAKETDIAT RQMLYGANRH AEKPPRSFWM FVWDALHDLT LIILVVCALV SIVVGLATKG
     WPMGIYDGFG IILSILLVVL VTATSDYQQA RKFMELDREK QKIYIRVTRD KKTKEVLVHD
     LVVGDILHLS IGDVVPADGL FISGDCLMID ESSLSGESEP VNISEERPFL HAGNKVVDGA
     AKMLVTAVGT RTEWGKIMGT LNGDGVDETP LQVKLNGVAT IIGQIGLVFA VLTFLVLLAR
     FLADKGMHVG LLNWSANDAL TIVNYFAIAV TIIVVAVPEG LPLAVTLSLA FAMKKLMHDK
     ALVRHLAACE TMGSASCICT DKTGTLTTNH MIVDKVWIGD VKFVGDKKNS ELKSTISERV
     MAILIQGIFV NTASEVVKGD DGKNTILGLA TETALLEFGL SLEEHLYDDY NKLTRIKVDP
     FNSVKKKMSV TIQLPNGGIR TFCKGASEII LEQCNTIHNT DGNIVPLSEM QKHNVLNIIN
     SFASEALRTL CIAFKDMDEF PNDQPISDDG YTLIAVFGIK DPVRPGVKDA VRTCMAAGIR
     VRMVTGDNIN TAKAIAKECG ILTEDGIAIE GQQLNNKSSD ELKELLPKIQ VIARSLPMDK
     YKLVTSLKSM YQEVVAVTGD GTNDAPALHE SDIGLAMGIT GTEVAKESAD VIIMDDNFET
     IVNVARWGRA VYLNIQKFVQ FQLTVNIVAL IVNFVSACII GSAPLTAVQL LWVNMIMDTL
     GALALATEPP NDEMMKRPPV RRGDNFITRI MWRNILGQGL YQLLVLATLM VIGKKLLSIE
     GPQSDKTINT LIFNSFVFCQ VFNEINCREM EKINVLQGIF RNWIFVGILT ATVIFQVIIV
     EFLGTFANTV PLSGELWLLS VVIGSISMII SVILKCIPVE FNKTNTKPHG YELIPEGPEI
     L
 
 
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