ID A0A5A9PTS4_9TELE Unreviewed; 1244 AA.
AC A0A5A9PTS4;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=E1301_Tti003674 {ECO:0000313|EMBL:KAA0724406.1};
OS Triplophysa tibetana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Nemacheilidae; Triplophysa.
OX NCBI_TaxID=1572043 {ECO:0000313|EMBL:KAA0724406.1, ECO:0000313|Proteomes:UP000324632};
RN [1] {ECO:0000313|EMBL:KAA0724406.1, ECO:0000313|Proteomes:UP000324632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTIB1903HZAU {ECO:0000313|EMBL:KAA0724406.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAA0724406.1};
RX PubMed=30977968;
RA Yang X., Liu H., Ma Z., Zou Y., Zou M., Mao Y., Li X., Wang H., Chen T.,
RA Wang W., Yang R.;
RT "Chromosome-level genome assembly of Triplophysa tibetana, a fish adapted
RT to the harsh high-altitude environment of the Tibetan Plateau.";
RL Mol. Ecol. Resour. 19:1027-1036(2019).
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 -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIB subfamily. {ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361146}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA0724406.1}.
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DR EMBL; SOYY01000002; KAA0724406.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A9PTS4; -.
DR Proteomes; UP000324632; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
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; cd02081; P-type_ATPase_Ca_PMCA-like; 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; 3.
DR InterPro; IPR022141; ATP_Ca_trans_C.
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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR PANTHER; PTHR24093:SF523; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 1.
DR Pfam; PF12424; ATP_Ca_trans_C; 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; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
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|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000324632};
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 95..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 148..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 391..412
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 432..458
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 945..962
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 982..999
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1020..1041
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1053..1072
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 44..120
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 286..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1244 AA; 138893 MW; 4C931F9BDD64262B CRC64;
MARNSFRGSK YRAEVNHDGD FGCTLKELRS LMELRGTDGL QRIQECYGDV QELCSRLKSS
PTEGLSGDPD DIARRKEQFG KNFIPPKKSK TFLQLVWEAL QDVTLIILEV AAIISLGLSF
YRPPDTEREN CGRAAGGVED EGEAEAGWIE GAAILLSVVC VVLVTAFNDW SKEKQFRGLQ
SRIEQEQKFY VVRAGQVIQI PVAEIVVGDI ALVKYGDLLP ADGVVIQSND LKIDESSLTG
ECDHVKKTFD KDPMLLSGTH VMEGSGRMVV SAVGINSQTG IIFTLLGGGD DDDDDDEDKK
EKKERKKREK QEKIKEKERK MKENKDKKKS KKQDGTVKKK DRDGGRVEMD PLHGDNVSQD
EAKKSKMPKK EKSVLQGKLT KLAVQIGKAG LFMSAITVII LIVLFLVDTF WIQGLPWLKD
CTPIYIQFFV KFFIIGVTVL VVAVPEGLPL AVTISLAYSV KKMMKDNNLV RHLDACETMG
NATAICSDKT GTLTMNRMTV TQVYIEDKHY KKIPKQDSIS GKTRDLLVKG IAINCAYTSK
ILPPEKDGGL PRQVGNKTEC ALLGFCLDLG LSYQTVRDEF PEERWYKVYT FNSVRKSMST
VEKSSDGTYR MFTKGASEIL LKKCCKILSA NGETNVFKPR DREDIMNKVI EPMASEGLRT
ICLAYREFPV SDGEPDWDSE SDILTGLTCI CVVGIEDPVR PEVPDAIKNC QRAGITVRMV
TGDNINTARA IATKCGILHP GDDFLCIEGK EFNRRIRNEL GEIEQERIDK IWPKLRVLAR
SSPTDKHTLV KGIIDSTIIE QRQVVAVTGD GTNDGPALKK ADVGFAMGIA GTDVAKEASD
IILTDDNFSS IVKAVMWGRN VYDSISKFLQ FQLTVNVVAV IVAFTGACIT QDSPLKAVQM
LWVNLIMDTF ASLALATEPP TESLLLRKPY GRNKPLISRT MMKNILGHAV YQLTIIFTLL
FAGEHIFDID SGRYAPLHAP ASEHYTIVFN TFVMMQIFNE INARKIHGER NVFEGIFNNF
IFCTIVFGTF IIQIIIVQFG GKPFSCVRLT VDQWLWCVFL GFGSLLWGQF ITTIPTSRLK
FLVTAGHGTQ KEEIPEDELE EMEDLDEIDH AEMELRRGHV LWCRGLNRIQ TQIRVVNAFR
ESMSPYEGLE TAESRSSIHN FMSHPEFRIE DSMIAIPLID DTDPEDDAPT KRNAVTPSLL
PVLSIANQNN NATDSKAYHH HKDLAKTILP QTPGSPLHSL ETSL
//
