UniProt: A0A103YM31

Database: UniProt
Entry: A0A103YM31_CYNCS

LinkDB:  A0A103YM31_CYNCS 
Original site:  A0A103YM31_CYNCS

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (18)   
   InterPro (12)   
   Pfam (4)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (27)   

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ID   A0A103YM31_CYNCS        Unreviewed;      1029 AA.
AC   A0A103YM31;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   28-JAN-2026, entry version 44.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=Ccrd_009968 {ECO:0000313|EMBL:KVI11614.1};
OS   Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC   Carduinae; Cynara.
OX   NCBI_TaxID=59895 {ECO:0000313|EMBL:KVI11614.1, ECO:0000313|Proteomes:UP000243975};
RN   [1] {ECO:0000313|EMBL:KVI11614.1, ECO:0000313|Proteomes:UP000243975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2C {ECO:0000313|EMBL:KVI11614.1};
RX   PubMed=26786968; DOI=10.1038/srep19427;
RA   Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA   Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA   Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT   "The genome sequence of the outbreeding globe artichoke constructed de novo
RT   incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL   Sci. Rep. 6:19427-19427(2016).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium. {ECO:0000256|RuleBase:RU361146}.
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 or into organelles. {ECO:0000256|ARBA:ARBA00053300}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);
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         Evidence={ECO:0000256|ARBA:ARBA00048694,
CC         ECO:0000256|RuleBase:RU361146};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIB subfamily. {ECO:0000256|ARBA:ARBA00006124,
CC       ECO:0000256|RuleBase:RU361146}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU361146}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KVI11614.1}.
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DR   EMBL; LEKV01000068; KVI11614.1; -; Genomic_DNA.
DR   STRING; 59895.A0A103YM31; -.
DR   Gramene; KVI11614; KVI11614; Ccrd_009968.
DR   OMA; ADGHARM; -.
DR   OrthoDB; 3352408at2759; -.
DR   Proteomes; UP000243975; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IEA:UniProtKB-EC.
DR   CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR   FunFam; 1.20.1110.10:FF:000039; Calcium-transporting ATPase; 1.
DR   FunFam; 2.70.150.10:FF:000006; Calcium-transporting ATPase; 1.
DR   FunFam; 3.40.1110.10:FF:000013; Calcium-transporting ATPase; 1.
DR   FunFam; 3.40.50.1000:FF:000018; Calcium-transporting ATPase; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR059000; ATPase_P-type_domA.
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   NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR24093:SF434; CALCIUM-TRANSPORTING ATPASE 13, PLASMA MEMBRANE-TYPE-RELATED; 1.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW   Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW   ECO:0000256|RuleBase:RU361146};
KW   Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU361146}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243975};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361146};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361146};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361146}.
FT   TRANSMEM        153..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        193..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        398..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        824..842
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        848..868
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        961..981
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        993..1011
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          109..181
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1029 AA;  113607 MW;  5BBF0A68B30A81C3 CRC64;
     MVSEIQSQFD IGAMLHNIST ITLTKAQKRW RLAYFSIYFS NTMLSIAKIS KKLSQYPISE
     IVAGPSYTAL KIIPKATNHP VDHSDXFSSI DQSELSDLVK NKDLEIVGKF NGVVGLAEAL
     QTNLENGING QDTDRRKIVF GSNTYKKPPP KGFFYFVVEA FKDTTILILL ACAALSLGFG
     IKEEGAKEGW YEGGSIFLAV FLVIAVSAVS NFRQERQFDR LSKISNNIKI DAIREGRRQK
     ISIFDVVVGD VVVLNIGDQI PADGLFIDGH SLLVDESSMT GESDHIDIDA IRHPFLISGS
     KVADGNGQML VISVGMNTAW GKMMSSITGD SNEQTPLQSR LNKLTSSIGK VGLAVAFLVL
     VVMLIRYFTG NTEDEDGNRE YNGRRTNTNE ILNSVTXIFA AAVTIVVVAI PEGLPLAVTL
     TLAYSMKRMM ADQAMVRKLS ACETMGSATV ICTDKTGTLT MNLMKVTKFW LGLDHIEDDS
     SIDAKVLQLY HQGVGLNTTG SVYKSASGNT SEYSGSPTEK AILSWAVTNL GMDMEKLKQD
     STILHVETFN SEKKRSGVLI RKKEDNTIHV HWKGAAEMVL AMCSNYYQKT GLKKSLNHDE
     KTRIEKIIEG MAASSLRCIA FAHMQIPENE LKHNEDGTNY KTLNEEGLTL LGIVGIKDPC
     RPGVKEAIDQ CRSAGVDIKM ITGDNVFTAK AIATECGILK GDQLVSKGEV VEGEEFRNYT
     DEERMEKVDI IRVMARSSPF DKLLMVQCLK KKGHVVAVTG DGTNDAPALK EADIGLSMGI
     QGTEVAKESS DIVILDDDFA SVAVVLRWGR CVYNNIQKFI QFQLTVNVAA LVINFVAAVS
     AGEVPLTAVQ LLWVNLIMDT LGALALATEK PTKELMNKPP VGRVAPLITN VMWRNLLAQS
     LYQIAVLLTF QFKGRSIFNV NERVKNTIIF NTFVLCQVFN EFNARKLEKR NVFEGLHKNR
     LFMGIIGATI VLQVVMVEFL KNFADTEKLN WEQWGICIAI AALSWPIGWF VKLIPVPDKP
     FLSYMRGWI
//

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