UniProt: M7ZNL4

Database: UniProt
Entry: M7ZNL4_TRIUA

LinkDB:  M7ZNL4_TRIUA 
Original site:  M7ZNL4_TRIUA

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (12)   
   Pfam (6)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (28)   

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ID   M7ZNL4_TRIUA            Unreviewed;      1020 AA.
AC   M7ZNL4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=TRIUR3_19239 {ECO:0000313|EMBL:EMS53940.1};
OS   Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS53940.1};
RN   [1] {ECO:0000313|EMBL:EMS53940.1, ECO:0000313|Proteomes:UP000015106}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. G1812 {ECO:0000313|Proteomes:UP000015106};
RX   PubMed=23535596; DOI=10.1038/nature11997;
RA   Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA   Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA   Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA   Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA   Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA   Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA   Wang D., Zhang A., Wang J.;
RT   "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL   Nature 496:87-90(2013).
RN   [2] {ECO:0000313|EnsemblPlants:TuG1812G0400002986.01.T01}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2022) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium. {ECO:0000256|RuleBase:RU361146}.
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         Evidence={ECO:0000256|ARBA:ARBA00000363,
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}.
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DR   EMBL; KD188093; EMS53940.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7ZNL4; -.
DR   STRING; 4572.M7ZNL4; -.
DR   EnsemblPlants; TuG1812G0400002986.01.T01; TuG1812G0400002986.01.T01; TuG1812G0400002986.01.
DR   Gramene; TuG1812G0400002986.01.T01; TuG1812G0400002986.01.T01; TuG1812G0400002986.01.
DR   eggNOG; KOG0204; Eukaryota.
DR   OMA; QICADEM; -.
DR   OrthoDB; 847at2759; -.
DR   Proteomes; UP000015106; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 1.
DR   Gene3D; 1.20.5.170; -; 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; 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   NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR24093:SF493; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR   Pfam; PF12515; CaATP_NAI; 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   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
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   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|RuleBase:RU361146};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015106};
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}; Transport {ECO:0000256|RuleBase:RU361146}.
FT   TRANSMEM        174..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        204..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        356..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        397..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        888..908
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        924..941
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        962..982
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        994..1015
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          117..191
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1020 AA;  110255 MW;  07B34F47B633FCFB CRC64;
     MESYLNENFG GVKPKHSSHE ALGRWRKVVG VVKNPKRRFR FTANLGKRSE AAAMKRTNQE
     KLRVAVLVSK AALQFIHGLA PQSEYTVPAA VKAAGYGICA EELSSVVESH DIKKLKAHGG
     TEGLLSKVST SESDGVSTSK DKLASRQEIF GINKFAETEA RSFWVFVWEA LQDMTLMILA
     ACAFFSLVVG IATEGWPKGA HDGLGIVASI LLVVFVTATS DYRQSLQFKD LDKEKKKITV
     QVTRSGYRQK LSIYELLVGD IVHLSIGDQV PADGLFVSGF SLLINESSLT GESEPVAVNA
     ENPFLLSGTK VQDGSCKMLV TTVGMRTQWG KLMATLSEGG DDETPLQVKL NGVATIIGKI
     GLVFAVVTFA VLTESLFRRK IMDGSYLSWS GDDALELLEF FAIAVTIVVV AVPEGLPLAV
     TLSLAFAMKK MMNDKALVRH LAACETMGSA TSICSDKTGT LTTNHMTVVK ACICGKIKEV
     DKSSNTKSLF SELPDSVMTM LSQSIFNNTG GDVVINQDGK REILGTPTET AILELGLSLG
     GDFQAVRKAT TLLKVEPFNS AKKRMGVVIQ LPGGAFRAHC KGASEIILAS CSKYLNDQGN
     AVPLDSATIA HLNATIESFA NEALRTLCLA YIEVAEGFSA NDAIPEEGYT CIGIVGIKDP
     VRPGVKESVA ICRSAGITVR MVTGDNINTA KAIARECGIL TEGGLAIEGP DFRTKSAEEM
     FKLIPKIQVM ARSSPLDKHT LVKNLRTTHE EVVAVTGDGT NDAPALHEAD IGLAMGIAGT
     EVAKESADVI ILDDNFSTIV TVAKWGRSVY INIQKFVQFQ LTVNVVALVV NFSSACLTGS
     APLTAVQLLW VNMIMDTLGA LALATEPPND ELMKRTPVGR KGNFISNIMW RNIMGQAIYQ
     FFVIWYLQTE GKTLFELKGD NSDLVLNTLI FNCFVFCQVF NEVSSREMER INVFKGILDN
     NVFVAVLGST VVFQIIIVQF LGDFANTTPL SLREWFSCIV IGFIGMPIAA IVKLFPVGSQ
//

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