ID Q4SZR9_TETNG Unreviewed; 863 AA.
AC Q4SZR9;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
DE Flags: Fragment;
GN ORFNames=GSTENG00009710001 {ECO:0000313|EMBL:CAF93863.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAF93863.1};
RN [1] {ECO:0000313|EMBL:CAF93863.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|EMBL:CAF93863.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope;
RG Whitehead Institute Centre for Genome Research;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Mn(2+)(in) = ADP + H(+) + Mn(2+)(out) + phosphate;
CC Xref=Rhea:RHEA:66820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29035, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000256|ARBA:ARBA00024272};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66821;
CC Evidence={ECO:0000256|ARBA:ARBA00024272};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
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DR EMBL; CAAE01011526; CAF93863.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4SZR9; -.
DR KEGG; tng:GSTEN00009710G001; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; cd02085; P-type_ATPase_SPCA; 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; 2.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR006413; P-type_ATPase_IIA_PMR1.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF2; CALCIUM-TRANSPORTING ATPASE TYPE 2C MEMBER 1; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 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; SFLDF00027; p-type_atpase; 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 Calcium {ECO:0000256|ARBA:ARBA00022568};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Ion transport {ECO:0000256|ARBA:ARBA00022568};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022568}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..863
FT /note="P-type Ca(2+) transporter"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004243649"
FT TRANSMEM 27..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 736..756
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 768..785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 805..822
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 834..856
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 687..859
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 108..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAF93863.1"
FT NON_TER 863
FT /evidence="ECO:0000313|EMBL:CAF93863.1"
SQ SEQUENCE 863 AA; 93386 MW; 404111F09355D75A CRC64;
QFKDPLILLL LASAVISVLM HQFDDAISIT VAIIIVVTVA FVQEYRSEKS LEELGKLVPP
ECHCVREGVL EHLLARELVP GDTVCLSVGE RVPADLRLFE STDLSVDESS LTGETTPSSK
HTFPQMGGAN RDAASCSNIA FMGTLVRCGR AKGIVIGTGE NSEFGEVFKM MQAEEAPKTP
LQKSMDLLGK QLSLYSFGII GVIMLVGWLQ GKSILDMFTI GVSLAVAAIP EGLPIVVTVT
LALGVMRMVK KRAIVKKLPI VETLGGCCSG TASTGDTPPL RERECVCVCV CVCVCVCVCV
FSGCCNVICS DKTGTLTKNE MTVAQMFTSD GLHAEVTGVG YSGAGEVILD GEVVHGFSCP
SITKIVEAGC VCNDSIIRNH TLLGRPTEGA LIALAMKMGL EGLQQEYVRL EEHPFTSEQK
WMAVRCVHRT LQDHPGLYFL KGAYEQVMRQ CSSYHSRGGA LPLGHQQREL YQQQLSYMGS
AGLRVLAFAS GPQLGNLTFL GLVGIIDPPR SGVKEAVATL IGSGVAVKMI TGDSQETAVS
IAARLGFYSK GSQCLSGDEV DALDLQQLSQ MVHRIAVFYR ASPRHKLKIV KSLQNVGAVV
AMTGDGVNDA VALKAADIGV AMGQTGTDVC KEAADMILVD DDFQTIMSAI EEGKGIYSNI
KNFVRFQLST SIAALTLISL VTLMNFPNPL NAMQILWINI IMDGPPAQSL GVEPVDRDVI
RKPPRNVKDS IITRSLIVKV LVSAFIIVCG TLFVFWRELR DNVITPRDTT MTFTCFVFFD
MFNALSSRSQ TRLVHEMGLC SNRTFCYAVL ASIMGQLLVI YFPPLQGVFQ TESLSLADLL
FLVVLTSSVC IVSELIKLVE RRR
//
