ID O77070_PLAMG Unreviewed; 994 AA.
AC O77070;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
OS Placopecten magellanicus (Sea scallop).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC Placopecten.
OX NCBI_TaxID=6577 {ECO:0000313|EMBL:AAC63909.1};
RN [1] {ECO:0000313|EMBL:AAC63909.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cross-striated adductor muscle {ECO:0000313|EMBL:AAC63909.1};
RA Shi X., Chen M., Huvos P., Hardwicke P.M.D.;
RT "Amino acid sequence of a Ca2+-transporting ATPase from the sarcoplasmic
RT reticulum of the cross-striated part of the adductor muscle of the deep-sea
RT scallop: comparison to SERCA enzymes of other animals.";
RL Comp. Biochem. Physiol. B, Comp. Biochem. 120:359-374(1998).
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: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004326}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004326}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {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; AF022228; AAC63909.1; -; mRNA.
DR AlphaFoldDB; O77070; -.
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:SF127; CALCIUM-TRANSPORTING ATPASE SARCOPLASMIC_ENDOPLASMIC RETICULUM TYPE; 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 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW Calcium {ECO:0000256|RuleBase:RU361146};
KW Calcium transport {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 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 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 83..106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 291..320
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 759..780
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 792..811
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 832..856
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 931..949
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 3..76
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 994 AA; 109695 MW; 0F7EC7FD8568A79A CRC64;
MEYAHTKSTE EVLEYFNVEE SGLSEEQVKA NTEKYGPNEL PTEEGKPLWE LILEQFDDLL
VKILLLAAII SFVLVWFEES EEQVTAFVEP FVILTILICN AVVGVWQEKN AEDAIEALKE
YEPEIAKVVR KGHRGVQKIR ASLLVPGDIV EISVGDKIPA DVRILQIYST TLRIDQSILT
GESVSVIKHT DPIPDPRAVN QDKKNILFSG TNISAGKCKG IAIGTGLNTA IGKIRDEMME
TETEKTPLQQ KLDEFGTQLS KVITIICICV WAINIGHFND PAHGGSWMKG AIYYFKIAVA
LAVAAIPEGL PAVITTCLAL GTRRMAKKNA IVRSLPSVET LGCTSVICSD KTGTLTTNQM
SVCKMFVFNK VEGNGIQTQQ FEITGSTYAP EGDVYLGGKK VKTCDYEGLE EMATICAMCN
DSSVDYNDTK GLYEKVGEAT ETALTVLCEK MNFFNTSRGG MSLREQGTVC NHVIQQMWSK
EFTLEFSRDR KSMSVFCTPN KPTKVPGGSK MFAKGAPEGL LDRCTHVRVG KDKVPMSPAI
KNEIMKYTKI YGTGRDTLRC LALATIDAPP RREDMDLEDA RKFIQYETNM TFVGVVGMLD
PPRMEVFDSI KNCRKAGIRV IVITGDNKAT AEAICRRIGV FGENESTEGM SYTGREFDDL
SPEEQRLAVM KSRLFARVEP AHKSKIVEYL QGEGEISAMT GDGVNDAPAL KKAEIGIAMG
SGTAVAKSAS EMVLADDNFA TIVSAVEEGR AIYNNMKQFI RYLISSNIGE VVCIFLTAAL
GIPEALIPVQ LLWVNLVTDG LPATALGFNP PDMDIMKKPP RNAKEGLITG WLFFRYMAIG
GYVGCATVGA AAWWFMVYDK GPQLNYYQLT HHMQCLAEPK MFPGIDCKIF GAPEPMTMAL
SVLVTIEMLN ALNSLSENQS LLVMPPWCNK WLLGAMALSM GLHFCILYID IMSTIFQITP
LGFEEWFAVL KISFPVILID ETLKFFCARK FTDA
//
