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Database: UniProt
Entry: A0A452Q9M0_URSAM
LinkDB: A0A452Q9M0_URSAM
Original site: A0A452Q9M0_URSAM 
ID   A0A452Q9M0_URSAM        Unreviewed;       969 AA.
AC   A0A452Q9M0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN   Name=ATP12A {ECO:0000313|Ensembl:ENSUAMP00000000703.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000000703.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000000703.1}
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}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362084}.
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DR   AlphaFoldDB; A0A452Q9M0; -.
DR   Ensembl; ENSUAMT00000000808.1; ENSUAMP00000000703.1; ENSUAMG00000000301.1.
DR   GeneTree; ENSGT00940000159259; -.
DR   OMA; FQDWSTK; -.
DR   Proteomes; UP000291022; 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:0008900; F:P-type potassium:proton transporter activity; IEA:UniProtKB-EC.
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:SF1; POTASSIUM-TRANSPORTING ATPASE ALPHA CHAIN 2; 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   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: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:UP000291022};
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        53..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        86..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        247..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        277..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        798..825
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        869..889
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        931..947
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   DOMAIN          1..72
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          172..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   969 AA;  106958 MW;  A1EEC9347AF60609 CRC64;
     KLSIKELEKK YGTNIITGLS STQAAELLAH NGPNALTPPK ETPEIIKFLK QMVGGFSLLL
     WIGAVLCCIA YGIQYSMNTS ASLDNVYLGC VLALVVILTG IFAYYQEAKS TNIMATFNKM
     IPQQALVIRD SEKKKIPAEQ LVVGDIVEIR GGDRIPADVR LLSVQGCKVD NSSLTGESEP
     QPRSSEFTHD SPLETKNIGF YSTTCLEGTA TGMVINTGDR TIIGQIASLA SGVGNEKTPI
     AIEIQHFVHI VAGVAVSIGI LFFIIAVSLK YEVLDSIIFL IGIIVANVPE GLLATVTVTL
     SLTAKRMAKK NCLVKNLEAV ETLGSTSIIC SDKTGTLTQN RMTVAHLWFD NQIFIADTSE
     DHSIFDQSSG TWASLSKIIT LCNRAEFRPG QESVPIMKRV VVGDASETAL LKFSEVILGD
     VMEIRKRNHK VAEIPFNSTN KFQLSIHKTD DPNDKRFLMV MKGAPERILE KCSTIMVNGQ
     EQPLDKNTAE AFHTAYMELG GLGERVLGFC HLYLPADKFP ETYTFDVDTM NFPTSNLCFV
     GLLSMIDPPR STVPDAVTKC RSAGIKVIMV TGDHPITAKA IAKSVGIISA NSETVEDIAK
     RLHIAVEQVN KDAKAAVVTG MELKDMSPEQ LDELLTNYSE IVFARTSPQQ KLIIVEGCQR
     QNAVVAVTGD GVNDSPALKK ADIGIAMGIA GSDAAKNAAD MILLDDNFAS IVTGVEEGRL
     IFDNLKKTIA YTLTKNIAEL CPFLIYIIAG LPLPIGTITI LFIDLGTDIV PSIALAYEKA
     ESDIMNRKPR HKKKDRLVNH QLAIYSYLHI GLMQAVGAFV VYFTVYAQEG FKPSFLINIR
     VEWENSNVND LEDSYGQQWT EYQRKYLEWT GYTAFFVGIM VQQIADLIIR KTRRNSIFQQ
     GLFRSPLPIG RDLALSLDAF RLIVLPSASR PQYWFVAVPF AILIWVYDEV RKLFIRLYPG
     SWWDKNMYY
//
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