ID A0A0A0KPC0_CUCSA Unreviewed; 1007 AA.
AC A0A0A0KPC0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=Csa_6G526450 {ECO:0000313|EMBL:KGN49511.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN49511.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN49511.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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DR EMBL; CM002927; KGN49511.1; -; Genomic_DNA.
DR RefSeq; XP_004134538.1; XM_004134490.2.
DR AlphaFoldDB; A0A0A0KPC0; -.
DR SMR; A0A0A0KPC0; -.
DR STRING; 3659.A0A0A0KPC0; -.
DR EnsemblPlants; KGN49511; KGN49511; Csa_6G526450.
DR GeneID; 101205642; -.
DR Gramene; KGN49511; KGN49511; Csa_6G526450.
DR KEGG; csv:101205642; -.
DR eggNOG; KOG0207; Eukaryota.
DR OMA; PNSWISG; -.
DR OrthoDB; 7279at2759; -.
DR Proteomes; UP000029981; Chromosome 6.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR CDD; cd00371; HMA; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 2.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR00003; copper ion binding protein; 2.
DR PANTHER; PTHR46594:SF6; HMA DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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; SSF55008; HMA, heavy metal-associated domain; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 309..332
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 378..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 412..429
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 561..585
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 605..627
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 941..964
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 970..990
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 57..123
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 139..205
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1007 AA; 108235 MW; FF2DCA88D8D75561 CRC64;
MAPGLRDLQL AHVAADDRRL PAISAADDIP EDLEDVRLLD SYERQEENLG QIRDGMNRVQ
VTVSGMTCAA CSNSVEAALR GVNGVLMASV ALLQNRADVV FDPSLVKEED IKEAIEDAGF
EAEIIPETTS VGKKSHGTLV GQFTIGGMTC AACVNSVEGI LKDLPGVRRA VVALATSLGE
VEYDPTITSK DDIVNAIEDA GFEASFVQSS EQDKILLTVA GIAGEVDVQF LEAILSNLKG
VKRFLFDSTS GRLEIVFDPE VVGPRSLVDE IEGRSNRKFK LHVTSPYTRL TSKDVEEANN
MFRLFISSLF LSVLIFLQRV ICPHIPLIYS LLLWRCGPFL MDDWLKWALV TVVQFVIGKR
FYVAAARALR NGSTNMDVLV ALGTTASYVY SVCALLYGAV TGFWSPTYFE TSAMLITFVL
LGKYLECLAK GKTSDAIKKL VELAPATALL LIRDKGGNLI EEREIDALLI QPGDVLKVLP
GTKIPADGVV VWGSSYVNES MVTGESIPVL KEVSLNVIGG TINFHGALHI RATKVGSDAV
LNQIISLVET AQMSKAPIQK FADFVASIFV PTVVAMALCT LFGWYVGGIL GAYPAEWLPE
NGNYFVFSLM FAIAVVVIAC PCALGLATPT AVMVATGVGA SNGVLIKGGD ALERAQKVKY
VIFDKTGTLT QGKATVTTAK IFTEISRGDF LKLVASAEAS SEHPLGKAIV EYARHFHFFD
EPSATKNVEN QSKESSGWLF DVTDFSALPG QGIQCTIEGK RILVGNRKLM NERGISIAPH
VDNFVIELEE SAKTGILVAC DDNLIGVVGI ADPLKREAAV VVEGLVKMGV SPVMVTGDNW
RTARAVAKEL GIQDVRAEVM PAGKAEVIQN FQKDGSTVAM VGDGINDSPA LAASDIGIAI
GAGTDIAIEA ADFVLMRNNL EDVITAIDLS RKTFNRIRLN YVFAMAYNVI AIPIAAGVFF
PSLGVKLPPW AAGACMALSS VSVVCSSLLL RRYKRPRLTT ILEITVE
//
