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ACA10_ARATH
ID   ACA10_ARATH             Reviewed;        1069 AA.
AC   Q9SZR1; Q9M0D3;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 189.
DE   RecName: Full=Calcium-transporting ATPase 10, plasma membrane-type;
DE            EC=7.2.2.10;
DE   AltName: Full=Ca(2+)-ATPase isoform 10;
GN   Name=ACA10; OrderedLocusNames=At4g29900; ORFNames=F27B13.140;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA   Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT   "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT   phosphorylation site database.";
RL   Plant Cell 16:2394-2405(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC       ATP coupled with the translocation of calcium from the cytosol into the
CC       endoplasmic reticulum. {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; Multi-pass membrane protein.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB43665.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL050352; CAB43665.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161575; CAB79748.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85690.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66062.1; -; Genomic_DNA.
DR   PIR; C85349; C85349.
DR   PIR; T08551; T08551.
DR   RefSeq; NP_001327988.1; NM_001341980.1.
DR   RefSeq; NP_194719.1; NM_119136.4.
DR   AlphaFoldDB; Q9SZR1; -.
DR   SMR; Q9SZR1; -.
DR   BioGRID; 14399; 4.
DR   STRING; 3702.AT4G29900.1; -.
DR   iPTMnet; Q9SZR1; -.
DR   SwissPalm; Q9SZR1; -.
DR   PaxDb; Q9SZR1; -.
DR   PRIDE; Q9SZR1; -.
DR   ProteomicsDB; 244346; -.
DR   EnsemblPlants; AT4G29900.1; AT4G29900.1; AT4G29900.
DR   EnsemblPlants; AT4G29900.2; AT4G29900.2; AT4G29900.
DR   GeneID; 829112; -.
DR   Gramene; AT4G29900.1; AT4G29900.1; AT4G29900.
DR   Gramene; AT4G29900.2; AT4G29900.2; AT4G29900.
DR   KEGG; ath:AT4G29900; -.
DR   Araport; AT4G29900; -.
DR   TAIR; locus:2123924; AT4G29900.
DR   eggNOG; KOG0204; Eukaryota.
DR   HOGENOM; CLU_002360_9_2_1; -.
DR   InParanoid; Q9SZR1; -.
DR   OMA; EIHIHWK; -.
DR   OrthoDB; 115892at2759; -.
DR   PhylomeDB; Q9SZR1; -.
DR   BioCyc; ARA:AT4G29900-MON; -.
DR   PRO; PR:Q9SZR1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SZR1; baseline and differential.
DR   Genevisible; Q9SZR1; AT.
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:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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; ISS:TAIR.
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   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; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Calcium; Calcium transport; Calmodulin-binding;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..1069
FT                   /note="Calcium-transporting ATPase 10, plasma membrane-
FT                   type"
FT                   /id="PRO_0000046416"
FT   TOPO_DOM        2..180
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..219
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..369
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        390..426
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        445..844
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        845..863
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        864..874
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        875..895
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        896..915
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        916..938
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        939..951
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        952..973
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        974..991
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        992..1013
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1014..1023
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1024..1045
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1046..1069
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          42..53
FT                   /note="Interaction with calmodulin"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        482
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         789
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         793
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   1069 AA;  116858 MW;  48CE4A4B218E2656 CRC64;
     MSGQFNNSPR GEDKDVEAGT SSFTEYEDSP FDIASTKNAP VERLRRWRQA ALVLNASRRF
     RYTLDLKREE DKKQMLRKMR AHAQAIRAAH LFKAAASRVT GIASPLPTPG GGDFGIGQEQ
     IVSISRDQNI GALQELGGVR GLSDLLKTNL EKGIHGDDDD ILKRKSAFGS NTYPQKKGRS
     FWRFVWEASQ DLTLIILIVA AVASLALGIK TEGIEKGWYD GISIAFAVLL VIVVTATSDY
     RQSLQFQNLN EEKRNIRLEV TRDGRRVEIS IYDIVVGDVI PLNIGDQVPA DGVLVAGHSL
     AVDESSMTGE SKIVQKNSTK HPFLMSGCKV ADGNGTMLVT GVGVNTEWGL LMASVSEDNG
     GETPLQVRLN GVATFIGIVG LTVAGVVLFV LVVRYFTGHT KNEQGGPQFI GGKTKFEHVL
     DDLVEIFTVA VTIVVVAVPE GLPLAVTLTL AYSMRKMMAD KALVRRLSAC ETMGSATTIC
     SDKTGTLTLN EMTVVECYAG LQKMDSPDSS SKLPSAFTSI LVEGIAHNTT GSVFRSESGE
     IQVSGSPTER AILNWAIKLG MDFDALKSES SAVQFFPFNS EKKRGGVAVK SPDSSVHIHW
     KGAAEIVLGS CTHYMDESES FVDMSEDKMG GLKDAIDDMA ARSLRCVAIA FRTFEADKIP
     TDEEQLSRWE LPEDDLILLA IVGIKDPCRP GVKNSVLLCQ QAGVKVRMVT GDNIQTAKAI
     ALECGILASD SDASEPNLIE GKVFRSYSEE ERDRICEEIS VMGRSSPNDK LLLVQSLKRR
     GHVVAVTGDG TNDAPALHEA DIGLAMGIQG TEVAKEKSDI IILDDNFESV VKVVRWGRSV
     YANIQKFIQF QLTVNVAALV INVVAAISAG EVPLTAVQLL WVNLIMDTLG ALALATEPPT
     DHLMDRAPVG RREPLITNIM WRNLFIQAMY QVTVLLILNF RGISILHLKS KPNAERVKNT
     VIFNAFVICQ VFNEFNARKP DEINIFRGVL RNHLFVGIIS ITIVLQVVIV EFLGTFASTT
     KLDWEMWLVC IGIGSISWPL AVIGKLIPVP ETPVSQYFRI NRWRRNSSG
 
 
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