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Database: UniProt
Entry: A0AAD4JNL9_PERFH
LinkDB: A0AAD4JNL9_PERFH
Original site: A0AAD4JNL9_PERFH 
ID   A0AAD4JNL9_PERFH        Unreviewed;      1036 AA.
AC   A0AAD4JNL9;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 8.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   ORFNames=C2S53_020326 {ECO:0000313|EMBL:KAH6837181.1};
OS   Perilla frutescens var. hirtella (Perilla citriodora) (Perilla setoyensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Elsholtzieae; Perilla.
OX   NCBI_TaxID=608512 {ECO:0000313|EMBL:KAH6837181.1, ECO:0000313|Proteomes:UP001190926};
RN   [1] {ECO:0000313|EMBL:KAH6837181.1, ECO:0000313|Proteomes:UP001190926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PC099 {ECO:0000313|Proteomes:UP001190926};
RX   PubMed=34535649;
RA   Zhang Y., Shen Q., Leng L., Zhang D., Chen S., Shi Y., Ning Z., Chen S.;
RT   "Incipient diploidization of the medicinal plant Perilla within 10,000
RT   years.";
RL   Nat. Commun. 12:0-0(2021).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC       calcium. {ECO:0000256|RuleBase:RU361146}.
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:KAH6837181.1}.
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DR   EMBL; SDAM02000019; KAH6837181.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAD4JNL9; -.
DR   Proteomes; UP001190926; 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; 1.20.5.170:FF:000026; Calcium-transporting ATPase; 1.
DR   FunFam; 2.70.150.10:FF:000006; Calcium-transporting ATPase; 1.
DR   FunFam; 3.40.1110.10:FF:000011; Calcium-transporting ATPase; 1.
DR   FunFam; 3.40.50.1000:FF:000011; Calcium-transporting ATPase; 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; IPR059000; ATPase_P-type_domA.
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; 4.
DR   PANTHER; PTHR24093:SF448; 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   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
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   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:UP001190926};
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        171..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        353..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        394..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        953..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   TRANSMEM        990..1009
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361146"
FT   DOMAIN          116..188
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   1036 AA;  113505 MW;  037B8FFEE8E38B15 CRC64;
     MDDYLKKNFD VDAKRPSEEA LQRWRSAVWL VKNPRRRFRM VADLAKRAEA ERKRRKIQEK
     IRVALYVQKA ALYFIDAVDR TSNQKIPDDV KQAGYNVSAD DLASIVRSHD LKRLDSHGGV
     DGIAKKLSVS VENGLPSSEI STRQKFYGEN KFIEKPPRPL WMFIWDAMQD MTLIMLMVCA
     VISVGVGIAT EGWPKGMYDG IGIILCIILV VVVTAISDYK QSLQFRELDK EKRNVVVQVT
     RDGSRQKVSI YDLVVGDIVN LSIGDQVPAD GLYVSGYSLY IDESSLSGES EPVHIEKGRP
     FLLSGTKVQE GSGKIIVTSV GMRTEWGRLM VTLSEGGEDE TPLQVKLNGV ATVIGKIGLV
     FAVLTFVVLT ARYLTVKAID GEITSWSMKD VVSLLNFFAV AVTILVVAVP EGLPLAVTLS
     LAFAMKKLMN DRALIRHLSA CETMGSATCI CTDKTGTLTT NHMVVTKVWL CGEESRVDSR
     KPENVMNSSI SQKVKNALID ALFLNTAADV VHGKGGKMEI LGSPTETALL EFGLLFQRDF
     KGRRQESRII KVEPFNSVKK RMSVLVEGAG GGGARAFIKG ASEIILEMCD KVVGKDGETV
     SISEEQRKNI TTAINGFACE ALRTLCLAYR DMETTSSNEA IPEEKYTLIA LVGIKDPLRP
     GVKEAVETCL AAGIMVRMVT GDNINTAKAI AKECGILTSD GVAIEGSELR DKTADQMKDI
     LPKLQVMARS LPLDKHKLVS MLRKEYEEVV AVTGDGTNDA PALHEADIGL AMGIAGTEVA
     KESADVVIMD DNFATILNVA KWGRSVYINI QKFVQFQLTV NIVALMTNFV CACVSGSAPL
     TAVQLLWVNM IMDTLGALAL ATEPPHDGLM KQAPVGRHAN IITRVMWRNI IGQSMYQLIV
     LGLLNYDGKR LLNLNAPDSD ATLRSLIFNT FVFCQVFNEI NSRDMEKINI FKGIFSSWIF
     IMIMVSTVGF QVIMVQVLCN YAGTVPLSGN LWAVSVLVGA TGLLVGTLIK CMPLPNIQIT
     NHHDGYEPLP SGPDLA
//
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