ID A0A3Q3A2A1_KRYMA Unreviewed; 1035 AA.
AC A0A3Q3A2A1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000009905.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000009905.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}. Sarcoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004326}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004326}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675,
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 AlphaFoldDB; A0A3Q3A2A1; -.
DR STRING; 37003.ENSKMAP00000009905; -.
DR Ensembl; ENSKMAT00000010064.1; ENSKMAP00000009905.1; ENSKMAG00000007392.1.
DR GeneTree; ENSGT00940000159895; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0033017; C:sarcoplasmic reticulum 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:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02083; P-type_ATPase_SERCA; 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; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005782; P-type_ATPase_IIA.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF149; CALCIUM-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 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 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|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW 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:UP000264800};
KW Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
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 54..72
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 78..101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 292..315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 752..775
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 826..848
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 923..942
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 957..976
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 997..1023
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 3..71
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1035 AA; 113757 MW; DD2355A96281D1B1 CRC64;
MENAHTKSVE EVYSYFCVNE STGLSPEEVK RQREKWGLNG KSLWELVLEQ FEDLLVRILL
LAACISFVLA WFEEGEETIT AFVEPFVILL ILIANAIVGV WQERNAEDAI EALKEYEPEM
GKVYRQDRKT VQRIKARDIV PGDIVEVAVG DKVPADIRIC SIKSTTLRVD QSILTGESVS
VIKHTDPVPD PRAVNQDKKN MLFSGTNIAA GKAVGVVVAT GVNTEIGKIR DEMAATEQEK
TPLQQKLDEF GQQLSKVISL ICVAVWIINI GHFNDPVHGG SWIRGAVYYF KIAVALAVAA
IPEGLPAVIT TCLALGTRRM AKKNAIVRSL PSVETLGCTS VICSDKTGTL TTNQMSVCRM
FILHKADGES CSLSEFTISG STYAPEGEVF HDGKLVKCSQ YDGLVELATI CALCNDSSLD
FNEVKGVYEK VGEATETALT CLVEKMNVFD NDVHSLSKID RANACNSVIK QLMKKECTLE
FSRDRKSMSV YCTPNKSRSS MGKMFVKGAP EGVIERCTHV RVGNSKVPLS QGIKEKIMAV
IREYGTGRDT LRCLALATRD NPPKMDDMIL SDATKFTEYE SDLTFVGCVG MLDPPRQEVA
ASIKLCRQAG IRVIMITGDN KGTAVAICRR IGILTEDDDV ERMAFTGREF DELSSYAQRE
AVTQARCFAR VEPSHKSKIV EFLQGFDEIT AMTGDGVNDA PALKKAEIGI AMGSGTAVAK
SASEMVLADD NFSSIVAAVE EGRAIYNNMK QFIRYLISSN VGEVVCIFLT AALGFPEALI
PVQLLWVNLV TDGLPATALG FNPPDLDIME KPPRNAKEPL ISGWLFFRYL AIGGYVGAAT
VGAAAWWFSI SEDGPQITLY QLSHFLQCGP DNPDFEGLDC QVFESPYPMT MALSVLVTIE
MCNALNSLSE NQSLLRMPPW ENIWLLGAIC LSMSLHFLIL YVEPLPVIFQ ITPLDVTQWM
MVLKISLPVI LLDELLKFAA RNYLELGKRQ EKAAGKGCYL SACAKGISWP FVAVSLPLVL
WVYSTDTNVS AILWP
//
