GenomeNet

Database: UniProt
Entry: A0A3B4THU6_SERDU
LinkDB: A0A3B4THU6_SERDU
Original site: A0A3B4THU6_SERDU 
ID   A0A3B4THU6_SERDU        Unreviewed;      1034 AA.
AC   A0A3B4THU6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE            EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN   Name=ATP2A1 {ECO:0000313|Ensembl:ENSSDUP00000005766.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000005766.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000005766.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3B4THU6; -.
DR   STRING; 41447.ENSSDUP00000005766; -.
DR   Ensembl; ENSSDUT00000005879.1; ENSSDUP00000005766.1; ENSSDUG00000004172.1.
DR   GeneTree; ENSGT00940000159895; -.
DR   Proteomes; UP000261420; 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; 2.
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; 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|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}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU361146};
KW   Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {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   1034 AA;  113847 MW;  FDA1739B7BC1BE2F CRC64;
     MENAHTKSVE EVYSYFCVNE STGLSLDEVK RQKEKWGLNG KSLWELVVEQ FEDLLVRILL
     LAACISFVLA WFEEGEETIT AFVEPFVILL ILIANAIVGV WQERNAEDAI EALKEYEPEM
     GKVYRQDRKT VQRIKARDIV PGDIVEVAVG DKVPADIRIC SIKSTTLRVD QSILTGESIS
     VIKHTDPVPD PRAVNQDKKN MLFSGTNIAA GKAVGVVVAT GVNTEIGKIR DEMAATEQEK
     TPLQQKLDEF GEQLSKVISL ICVAVWIINI GHFNDPVHGG SWIRGAVYYF KIAVALAVAA
     IPEGLPAVIT TCLALGTRRM AKKNAIVRSL PSVETLGCTS VICSDKTGTL TTNQMSVCRM
     FTVNKAEGDS CSLSEFTITG STYAPEGEDG KQVKSSQHDA LVELATICAL CNDSSLDFNE
     VKGVYEKVGE ATETALTCLV EKMNVFDTEV HNLSKIDRAN ACNSVIKQLM RKEFTLEFSR
     DRKSMSVYCT PNKSRSSMGK MFVKGAPEGV IERCTHVRVG NSKVALSKEI KEKIMSVIRE
     YGTGRDTLRC LALATRDSPP KMEDMILSDT AKFSEYESDL TFVGCVGMLD PPRQEVAASI
     MLCRQAGIRV IMITGDNKGT AVAICRRIGI LTEEDDIERM AFTGREFDEL SPYTQREAVT
     HARCFARVEP SHKSKIVEFL QGFDEITAMT GDGVNDAPAL KKAEIGIAMG SGTAVAKSAS
     EMVLADDNFS SIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL GFPEALIPVQ
     LLWVNLVTDG LPATALGFNP PDLDIMEKPP RNAKEPLISG WLFFRYLAIG GYVGAATVGA
     AAWWFTVSDD GPQLTLYQLS HFLQCGPENP EFDGLDCHVF ESPYPMTMAL SVLVTIEMCN
     NRLLSEDGER TSLLRMPPWE NVWLLGAICL SMSLHFLILY VEPLPVIFQI TPLDTTQWMM
     VLKISLPVIL LDELLKFMAR NYLDFGKQLE KPAGKGCSLS ACADGISWPF VAISLPLVLW
     IYSTDTNVSA MLWP
//
DBGET integrated database retrieval system