ATC1_ANOGA
ID ATC1_ANOGA Reviewed; 1018 AA.
AC Q7PPA5; A7UU43; A7UU44; A7UU45;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 5.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Calcium-transporting ATPase sarcoplasmic/endoplasmic reticulum type;
DE EC=7.2.2.10;
DE AltName: Full=Calcium pump;
DE AltName: Full=Sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase {ECO:0000250|UniProtKB:P22700};
GN Name=SERCA {ECO:0000250|UniProtKB:P22700};
GN Synonyms=Ca-P60A {ECO:0000250|UniProtKB:P22700}; ORFNames=AGAP006186;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of calcium. {ECO:0000305}.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Sarcoplasmic reticulum membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=C; Synonyms=E, D;
CC IsoId=Q7PPA5-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q7PPA5-2; Sequence=VSP_030291;
CC Name=B;
CC IsoId=Q7PPA5-3; Sequence=VSP_030292;
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000305}.
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DR EMBL; AAAB01008960; EAA10790.5; -; Genomic_DNA.
DR EMBL; AAAB01008960; EDO63821.1; -; Genomic_DNA.
DR EMBL; AAAB01008960; EDO63822.1; -; Genomic_DNA.
DR EMBL; AAAB01008960; EDO63823.1; -; Genomic_DNA.
DR EMBL; AAAB01008960; EDO63824.1; -; Genomic_DNA.
DR RefSeq; XP_001688815.1; XM_001688763.1.
DR RefSeq; XP_001688816.1; XM_001688764.1.
DR RefSeq; XP_001688817.1; XM_001688765.1.
DR RefSeq; XP_001688818.1; XM_001688766.1.
DR RefSeq; XP_316251.4; XM_316251.4.
DR AlphaFoldDB; Q7PPA5; -.
DR SMR; Q7PPA5; -.
DR STRING; 7165.AGAP006186-PC; -.
DR PaxDb; Q7PPA5; -.
DR GeneID; 1276852; -.
DR KEGG; aga:AgaP_AGAP006186; -.
DR CTD; 1276852; -.
DR VEuPathDB; VectorBase:AGAP006186; -.
DR eggNOG; KOG0202; Eukaryota.
DR InParanoid; Q7PPA5; -.
DR OMA; PLWNNMM; -.
DR OrthoDB; 100699at2759; -.
DR PhylomeDB; Q7PPA5; -.
DR Proteomes; UP000007062; Chromosome 2L.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Calcium; Calcium transport;
KW Endoplasmic reticulum; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Sarcoplasmic reticulum; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1018
FT /note="Calcium-transporting ATPase sarcoplasmic/endoplasmic
FT reticulum type"
FT /id="PRO_0000233305"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 70..88
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TRANSMEM 89..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 110..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TRANSMEM 253..272
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 273..294
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TRANSMEM 295..312
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 313..756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TRANSMEM 757..776
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 777..786
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TRANSMEM 787..807
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 808..827
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TRANSMEM 828..850
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 851..896
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TRANSMEM 897..916
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250"
FT TOPO_DOM 917..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TRANSMEM 930..948
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250"
FT TOPO_DOM 949..963
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT TRANSMEM 964..984
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250"
FT TOPO_DOM 985..1018
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT ACT_SITE 350
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 303
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 706
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 767
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 770
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 798
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 799
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT BINDING 907
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04191"
FT VAR_SEQ 993..1018
FT /note="GESYIKNMHGLVLAWAVFFAYIIWGP -> VNPDFH (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_030291"
FT VAR_SEQ 993..1018
FT /note="GESYIKNMHGLVLAWAVFFAYIIWGP -> ANEVIKTWE (in isoform
FT B)"
FT /evidence="ECO:0000305"
FT /id="VSP_030292"
SQ SEQUENCE 1018 AA; 111859 MW; 4682B896CC48E90E CRC64;
MEDGHSKTVD EVLSHFRVDP ERGLSLDQVK EYQKKYGPNE LPAEEGKTLW QLVLEQFDDL
LVKILLLAAI ISFVLALFEE HEGVEAFVEP FVILLILIAN AVVGVWQERN AESAIEALKE
YEPEMGKVIR GDKSGVQKIR AKEIVPGDVV EVSVGDKIPA DIRLIKIYST TIRIDQSILT
GESVSVIKHT DAVPDPRAVN QDKKNILFSG TNVAAGKARG VVIGTGLNTA IGKIRTEMSE
TEEIKTPLQQ KLDEFGEQLS KVISLICVAV WAINIGHFND PAHGGSWIKG AVYYFKIAVA
LAVAAIPEGL PAVITTCLAL GTRRMAKKNA IVRSLPSVET LGCTSVICSD KTGTLTTNQM
SVSRMFIFEK IEGNDSSFTE FEISGSTYEP IGEVTLNGQR IKAADYETLH ELGTICIMCN
DSAIDFNETK KVFEKVGEAT ETALIVLAEK LNPFNVAKQG LDRRSSAICV RQEIETKWKK
EFTLEFSRDR KSMSSYCTPL KASKLGNGPK LFCKGAPEGV LERCTHARVG STKVPLTQTL
KQRILDLTRT YGTGRDTLRC LALATADSPM KPDDMDLNDS TKFYTYEVNL TFVGVVGMLD
PPRKEVQDSI VRCRAAGIRV IVITGDNKAT AEAICRRIGV FGEDEDTTGK SYSGREFDDL
SVSEQREACS RARLFSRVEP AHKSKIVEFL QSMNEISAMT GDGVNDAPAL KKAEIGIAMG
SGTAVAKSAA EMVLADDNFS SIVAAVEEGR AIYNNMKQFI RYLISSNIGE VVSIFLTAAL
GLPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMTKPP RKADEGLISG WLFFRYMAIG
GYVGCATVGG AAWWFMFSET GPQLSYWQLT HHLSCLGGGE EFKGIDCKIF NDPHPMTMAL
SVLVTIEMLN AMNSLSENQS LVQMPPWCNI WLIASMCLSF ALHFVILYVD VLSTVFQVTP
LDGNEWMTVM KFSLPVVLLD EILKFVARRI SDGESYIKNM HGLVLAWAVF FAYIIWGP
