UniProt: A0A075A647

Database: UniProt
Entry: A0A075A647_9TREM

LinkDB:  A0A075A647_9TREM 
Original site:  A0A075A647_9TREM

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Ontology (5)   
   GO (5)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (17)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
   SMART (1)   
All databases (26)   

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ID   A0A075A647_9TREM        Unreviewed;      1003 AA.
AC   A0A075A647;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN   ORFNames=T265_12551 {ECO:0000313|EMBL:KER33797.1};
OS   Opisthorchis viverrini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX   NCBI_TaxID=6198 {ECO:0000313|EMBL:KER33797.1, ECO:0000313|Proteomes:UP000054324};
RN   [1] {ECO:0000313|EMBL:KER33797.1, ECO:0000313|Proteomes:UP000054324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA   Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA   Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA   Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT   "Opisthorchis viverrini - life in the bile duct.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362084};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIC subfamily. {ECO:0000256|ARBA:ARBA00006934,
CC       ECO:0000256|RuleBase:RU362084}.
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DR   EMBL; KL596622; KER33797.1; -; Genomic_DNA.
DR   RefSeq; XP_009162539.1; XM_009164275.1.
DR   AlphaFoldDB; A0A075A647; -.
DR   STRING; 6198.A0A075A647; -.
DR   GeneID; 20326719; -.
DR   KEGG; ovi:T265_12551; -.
DR   CTD; 20326719; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000054324; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro.
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; IPR005775; P-type_ATPase_IIC.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01106; ATPase-IIC_X-K; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR   PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:RU362084};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU362084};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362084};
KW   Metal-binding {ECO:0000256|RuleBase:RU362084};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362084};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU362084};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW   ECO:0000256|RuleBase:RU362084};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362084};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362084}; Transport {ECO:0000256|RuleBase:RU362084}.
FT   TRANSMEM        79..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        275..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        305..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        825..854
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        897..917
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        938..958
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        964..981
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   DOMAIN          26..100
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1003 AA;  111169 MW;  27C1E4FFF1715576 CRC64;
     MFKKSDGGEK KGGPDESALK AEVKMEEHQV DLEELCGRLG TDLVQGLDES LAKKRLEECG
     PNAVTPPKTI PEWVRLLKCM LGGFSILLWI GSILCFIAGT IEYTTVRFPQ NDNLYLGGVL
     AAVVLISGLF TYYQESKSSK IMESFRTMVP QTALVIRNGE RHIISAEQLV VGDLVDVKGG
     DRVPADLRVI YASNLKVDNS SLTGESEPQT RSTQCTQVNP LETKNLLFFS TNVVEGSGRG
     VVVRTGNDTV MGRIARLTTT IENQQTPLGR ELSHFIRIIT IAAATIGVSC TSASLYFGYS
     WIEATLFLLG IIVAMVPEGL LPTVTVALAL TARQMAIKNC LVRNLEAVET LGSTSCICSD
     KTGTLTQNRM TVAHLWCDGI VIDADEDDDV VIEPHEHTWN ALSRVAMLCN RAVFKSHEAN
     APISRRGCIG DASEVGLMKY FEDRVGSTMQ FRSTHEKVAE IPFNSTQKFQ VSIHRNETEN
     SHFVLVMKGA PEKILELCST IMIHGEDQEL TDQMRQAFND AYLRLGAMGE RVLGFCDYEL
     PASQYDETYC FDTEEVNFPL DGLRFVGLIS LIDPPRASVP QAVAKCRQAG ILVVMVTGDH
     PITAKAIAKS VGILSPHSKT IEDIAQERGI DIKQVDPREA NACIVHGSDL RAMTPQQLDQ
     MLLQYEEFVF ARTSPQQKLA IVEGFQRQGR FVAVTGDGVN DSPALKKADI GVAMGIAGSD
     VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSKIPELLPF ILFMLLKIPL
     VLGTVTILCI DLGTDMFPAI SMAYEGPESD LMKRKPRHPK KDRLVNMRLV TMAFCQIGAI
     QAAAGFFAAF VVLADNGFLP GILFGISQNW NSRNYNDLPD SYGQEWTYGQ RMTLQKAAYT
     SFFVAVVIAQ WADLVICKTR RLSIFQQGMF NHKLSTSLFF EITVAWVLQY IPGVNKAIQL
     EPMVYQWWTP ALPFALLILA YDEVRKWIIR KRPNGWLERE TYY
//

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