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ACA1_ORYSJ
ID   ACA1_ORYSJ              Reviewed;        1043 AA.
AC   Q8RUN1; A0A0P0VCM3; Q0JG69;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Calcium-transporting ATPase 1, plasma membrane-type {ECO:0000305};
DE            Short=OsACA1 {ECO:0000303|PubMed:24286292};
DE            EC=7.2.2.10;
DE   AltName: Full=Ca(2+)-ATPase isoform 1 {ECO:0000305};
GN   Name=ACA1 {ECO:0000303|PubMed:24286292};
GN   OrderedLocusNames=Os01g0939100, LOC_Os01g71240;
GN   ORFNames=B1150F11.11, P0504E02.35;
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=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
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=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
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; AP003269; BAB89725.1; -; Genomic_DNA.
DR   EMBL; AP003412; BAB90248.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF07259.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS76138.1; -; Genomic_DNA.
DR   EMBL; AK070064; BAG91749.1; -; mRNA.
DR   RefSeq; XP_015621941.1; XM_015766455.1.
DR   AlphaFoldDB; Q8RUN1; -.
DR   SMR; Q8RUN1; -.
DR   STRING; 4530.OS01T0939100-01; -.
DR   PaxDb; Q8RUN1; -.
DR   PRIDE; Q8RUN1; -.
DR   EnsemblPlants; Os01t0939100-01; Os01t0939100-01; Os01g0939100.
DR   GeneID; 4326507; -.
DR   Gramene; Os01t0939100-01; Os01t0939100-01; Os01g0939100.
DR   KEGG; osa:4326507; -.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_2_1; -.
DR   InParanoid; Q8RUN1; -.
DR   OMA; PNDAMMK; -.
DR   OrthoDB; 115892at2759; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   Genevisible; Q8RUN1; OS.
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; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
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..1043
FT                   /note="Calcium-transporting ATPase 1, plasma membrane-type"
FT                   /id="PRO_0000247302"
FT   TOPO_DOM        1..178
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        377..395
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        824..844
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        845
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        846..866
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        891..911
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        912..955
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        956..976
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        998..1018
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1019..1043
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1023..1043
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        460
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         761
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         765
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1043 AA;  112842 MW;  A16B82561803AF56 CRC64;
     MSFIRKKSME FLKSFEVPAK NPSEEAQRRW RDAVGTLVKN RRRRFRMVPD LDKRSQAETQ
     RRKIQEKLRV ALFVQKAALQ FIDAVRKTEH PLPELARQCG FSVSAEELAS IVRGHDTKSL
     RFHNGVDGIA RKVAVSLADG VKSDDAGLRA EVYGANQYTE KPPRTFWMFL WDASQDMTLL
     LLAFCAAVSV AIGLATEGWP SGMYDGVGIM LTILLVVMIT AASDYKQSLQ FRDLDKEKKK
     IDVQVTRDGY RQKVSIYDIV VGDIVHLSIG DQVPADGLFI DGYSFVVDES NLSGESEPVH
     VSTANRFLLG GTKVQDGSAR MLVTAVGMRT EWGNLMETLS QGGEDETPLQ VKLNGVATII
     GKIGLAFAVL TFTVLMARFL LGKAGAPGGL LRWRMVDALA VLNFFAVAVT IIVVAVPEGL
     PLAVTLSLAF AMKKLMQERA LVRHLSACET MGSASCICTD KTGTLTTNHM VVEKIWASGA
     AQTMSNAKGF DQLTSSMSET FAKVLLEGVF HCSGSEVVRG KDGRHTIMGT PTETAILEFG
     LAVEKRARIE HTGAGKLKVE PFNSVKKTMA VVIASPSAGG RPRAFLKGAS EVVLSRCSLV
     LDGTGNVEKL TDAKAKRVAS AIDAFACEAL RTLCLAYQDV DGGGGDIPGE GYTLIAVFGI
     KDPLRPGVRE AVATCHAAGI NVRMVTGDNI NTAKAIAREC GILTDDGIAI EGPEFRNKDP
     DQMREIIPKI QVMARSLPLD KHTLVTNLRG MFNEVVAVTG DGTNDAPALH EADIGLAMGI
     AGTEVAKENA DVIIMDDNFS TIINVAKWGR SVYINIQKFV QFQLTVNVVA LMVNFISASF
     TGSAPLTIVQ LLWVNLIMDT LGALALATEP PNDAMMKRPP VGRGDNFITK VMWRNIVGQS
     IYQLVVLGVL LLRGKSLLQI NGPQADSLLN TFVFNTFVFC QVFNEVNSRE MEKINVFSGI
     FSSWIFSAVV GVTAGFQVIM VELLGTFANT VHLSGKLWLT SVLIGSVGLV IGAILKCIPV
     ESGSDASDRH DGYRPIPTGP SAV
 
 
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