UniProt: A0A4W5NDR9

Database: UniProt
Entry: A0A4W5NDR9_9TELE

LinkDB:  A0A4W5NDR9_9TELE 
Original site:  A0A4W5NDR9_9TELE

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Ontology (5)   
   GO (5)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (17)   
   InterPro (11)   
   Pfam (4)   
   PROSITE (1)   
   SMART (1)   
All databases (25)   

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ID   A0A4W5NDR9_9TELE        Unreviewed;      1000 AA.
AC   A0A4W5NDR9;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN   Name=ATP1A1 {ECO:0000313|Ensembl:ENSHHUP00000048078.1};
OS   Hucho hucho (huchen).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Hucho.
OX   NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000048078.1, ECO:0000313|Proteomes:UP000314982};
RN   [1] {ECO:0000313|Proteomes:UP000314982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Macqueen D.J., Gundappa M.K.;
RT   "Genome assembly of Danube salmon.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSHHUP00000048078.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   AlphaFoldDB; A0A4W5NDR9; -.
DR   Ensembl; ENSHHUT00000049828.1; ENSHHUP00000048078.1; ENSHHUG00000026354.1.
DR   GeneTree; ENSGT00940000154840; -.
DR   Proteomes; UP000314982; 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   CDD; cd02608; P-type_ATPase_Na-K_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; 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; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43294:SF8; 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; 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: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:UP000314982};
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        65..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        99..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        260..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        290..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        818..841
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        889..906
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        927..946
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        952..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   DOMAIN          11..85
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          184..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1000 AA;  110945 MW;  0D9B60D0AC5F269B CRC64;
     MDDLKKEVDL DDHKLTLDEL NRKYGTDLAR GLSSVRAKEI LLRDGPNTLT PPRTTPEWVK
     FCKQLFGGFC MLLWIGAVLC FMAHIIQVTS EEEPTNANLY LGLVLAVVVI ITGCFSYYQE
     AKSSKIMDSF KNLVPQQALV VRDGEKKNIN TEEVVVGDIV EVKGGDRIPA DLRIVSASGC
     KVDNSSLTGE SEPQTRSPDF SNDNPLETRN IAFFSTNCVE GTARGIVINT GDHTIMGRIA
     ALAMSLESGQ TPLGIEIDHF IEIITGVSVF FGMTFLILSV ILGYGWLPSI IFLIGIIVAN
     VPEGLLATVT VCLTLTAKRM AKKNCLVKNL EAVETLGSTS TICSDKTGTL TQNRMTVAHM
     WFDNQIHDAD TTENQSGTSF DKSSATWAAL ARVAGLCNRA VFLAEQNNIP ILKRDVSGDA
     SETALLKCIE LCCGSVKDMR EKYSKVVEIP FNSTNKYQLS IHENNMAGES NHLLVMKGAP
     ERILDSCSTI LLHGKEHPLD DEIKESFQKA YEVLGGLGER VLGFCHFQLP DDQFPEGFDF
     DCEDVNFPTE NLCFVGLMSM IDPPRAAVPD AVSKCRCAGI KVIMVTGDHP ITAKAIAKGV
     GIISEGNETV EEIAARLKIP VSEVNPRDAK ACVVHGGELK DMTAEQLDDI LKHHTEIVFA
     RTSPQQKLII VEGCQRQGAI VAVTGDGVND SPALRKADIG VAMGIAGSDV SKQAADMILL
     DDNFASIVTG VEEGRLIFDN LKKSITYTLS SKIPEMTPFL FLLLANIPLA LGTVTILCID
     LGTDMIPAIS LAYEQAENDI MKRQPRNPKT DRLVNERLIS VAYGQFGVML AAAGFFTYFV
     IMAENGFYPM DLLGIRLDWE NQYINDMEDS YGQQWTYESR KIIEFTCHTA YFATVVIAQW
     AVLIVCKTRK NSYFQQGLMK HTHTFTLNSF SFLFYSPLST CLSFTFTSNL FIFYFLVFFL
     RPFWWVCAFP YTLLIFIYDE VRKYIMRRNP GGWVYQETYY
//

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