ID A0A3B1J529_ASTMX Unreviewed; 1025 AA.
AC A0A3B1J529;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000036454.1, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000036454.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004415}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004415}. Cell membrane
CC {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein
CC {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; A0A3B1J529; -.
DR Ensembl; ENSAMXT00000032353.1; ENSAMXP00000036454.1; ENSAMXG00000033172.1.
DR GeneTree; ENSGT00940000154840; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000033172; Expressed in brain and 13 other cell types or tissues.
DR GO; GO:0042383; C:sarcolemma; 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 GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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:SF9; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA-1; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000018467};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW Sodium/potassium transport {ECO:0000256|ARBA:ARBA00022607};
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 98..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 131..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 292..316
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 322..345
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 851..874
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 915..934
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 955..982
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 988..1006
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 43..117
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1025 AA; 113037 MW; FD67BAE0E901021D CRC64;
MGRGGGRDQY ELAATSEQGG KKKNKNKKKD KDMDELKKEV DLDDHKLSLD ELHRKYGTDL
SRGLSSSRAQ EILARDGPNA LTPPPTTPEW VKFCKQMFGG FSMLLWTGAV LCFLAYGIQA
AMEDEPANDN LYLGVVLSAV VIITGCFSYY QEAKSSKIMD SFKNLVPQQA LVIRDGEKNH
INAEDVVLGD LVEVKGGDRI PADLRIISAH GCKVDNSSLT GESEPQTRSP DFSNDNPLET
RNIAFFSTNC VEGTARGIVI STGDRTVMGR IATLASGLEV GRTPISIEIE HFIHIITGVA
VFLGLSFFIL SLVLGYSWLE AVIFLIGIIV ANVPEGLLAT VTVCLTLTAK RMAKKNCLVK
NLEAVETLGS TSTICSDKTG TLTQNRMTVA HMWFDNQIHE ADTTENQSGT TFDRSSTTWA
CLARVAGLCN RAVFLAEQTD VPILKRDVAG DASESALLKC IELCCGSVKE MREKYSKAAE
IPFNSTNKYQ LSVHKNPNAT PESKYLLVMK GAPERILDRC STIMFQGKEQ PLDDEMRDAF
QNAYLELGGL GERVLGFCHY NLPEEQFPEG FQFDTDDVNF PTENLCFVGL MSMIDPPRAA
VPDAVGKCRS AGIKVIMVTG DHPITAKAIA KGVGIISEGN ETVEDIAARL NIPINEVNPR
DAKACVVHGG DLKDLSAEQL DDILKHHTEI VFARTSPQQK LIIVEGCQRQ GAIVAVTGDG
VNDSPALKKA DIGVAMGIAG SDVSKQAADM ILLDDNFASI VTGVEEGRLI FDNLKKSIAY
TLTSNIPEIT PFLFFIIANI PLPLGTVTIL CIDLGTDMVP AISLAYEAAE SDIMKRQPRN
PKTDKLVNER LISIAYGQIG MIQALAGFFT YFVILAENGF LPSRLLGIRV HWDDKYTNDL
EDSYGQQWTY EQRKIVEFTC HTAFFTSIVV VQWADLIICK TRRNSVFQQG MKNKILIFGL
FEETALAAFL SYCPGMGVAL RMYPLKPNWW FCAFPYSLLI FIYDEIRKLI LRRNPGGWVE
RETYY
//
