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Database: UniProt
Entry: A0A2D0Q211_ICTPU
LinkDB: A0A2D0Q211_ICTPU
Original site: A0A2D0Q211_ICTPU 
ID   A0A2D0Q211_ICTPU        Unreviewed;      1026 AA.
AC   A0A2D0Q211;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN   Name=LOC108258575 {ECO:0000313|RefSeq:XP_017312768.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017312768.1};
RN   [1] {ECO:0000313|RefSeq:XP_017312768.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017312768.1};
RG   RefSeq;
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   RefSeq; XP_017312768.1; XM_017457279.3.
DR   AlphaFoldDB; A0A2D0Q211; -.
DR   STRING; 7998.ENSIPUP00000011159; -.
DR   GeneID; 108258575; -.
DR   KEGG; ipu:108258575; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000221080; Chromosome 26.
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; 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   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}; 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        99..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        133..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        294..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        324..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        856..877
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        916..935
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        956..973
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        988..1004
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   DOMAIN          45..119
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1026 AA;  113196 MW;  128E028535A8B9F1 CRC64;
     MGRGEGREQY ELAATSEQGG KKSKSKGKKD KDKDMDELKK EVDLDDHKLT PEELNRKYGS
     DLIRGLTVAR AKEIFERDGP NALTPPPTTP EWVKFCKQLF GGFSTLLWIG AILCFLAYGI
     QAASEDEPAN DNLYLGIVLS AVVMITGCFS YYQEAKSSKI MDSFKNLVPQ QALVIRDGEK
     MSINAEDVVV GDLVEVKGGD RIPADLRIIS AHGCKVDNSS LTGESEPQTR TPDFSNENPL
     ETRNIAFFST NCVEGTARGI VINTGDRTVM GRIATLASGL EVGRTPISIE IEHFIHIITG
     VAVFLGVSFF ILSLILGYSW LEAVIFLIGI IVANVPEGLL ATVTVCLTLT AKRMAKKNCL
     VKNLEAVETL GSTSTICSDK TGTLTQNRMT VAHMWFDNQI HEADTTENQS GTAFDRSSPT
     WAGLARIAGL CNRAVFLADQ ENVPILKRDT AGDASESALL KCIELCCGSV KEMRDKYTKI
     AEIPFNSTNK YQLSIHKNPS DGESKHLLVM KGAPERILDR CSTIMLQGKE QPLDDELKDA
     FQNAYLELGG LGERVLGFCH YSLPDDQFPE DFQFDTEDVN FPTENLCFLG LMSMIDPPRA
     AVPDAVGKCR SAGIKVIMVT GDHPITAKAI AKGVGIISEG NETVEDIAAR LNIPINEVNP
     RDAKACVVHG GDLKDLTPEQ LDDVLKHHTE IVFARTSPQQ KLIIVEGCQR QGAIVAVTGD
     GVNDSPALKK ADIGVAMGIA GSDVSKQAAD MILLDDNFAS IVTGVEEGRL IFDNLKKSIA
     YTLTSNIPEI TPFLFFIIAN IPLPLGTVTI LCIDLGTDMV PAISLAYEAA ESDIMKRQPR
     NPKTDKLVNE RLISMAYGQI GMIQALAGFF TYFVILAENG FLPSTLLGIR VFWDDKYMND
     LEDSYGQQWT YEQRKIVEFT CHTAFFISIV VVQWADLIIC KTRRNSVFQQ GMKNKILIFG
     LFEETALAAF LSYCPGMDVA LRMYPLKPNW WFCAFPYSLL IFIYDEIRKL IIRRSPGGWV
     ERETYY
//
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