ID AT1A4_HUMAN Reviewed; 1029 AA. AC Q13733; Q504T2; Q7Z4I9; Q8TBN8; Q8WXA7; Q8WXH7; Q8WY13; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 3. DT 27-MAR-2024, entry version 208. DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-4 {ECO:0000305}; DE Short=Na(+)/K(+) ATPase alpha-4 subunit; DE EC=7.2.2.13 {ECO:0000250|UniProtKB:Q64541}; DE AltName: Full=Sodium pump subunit alpha-4; GN Name=ATP1A4 {ECO:0000312|HGNC:HGNC:14073}; Synonyms=ATP1AL2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND ACTIVITY REGULATION. RC TISSUE=Testis; RX PubMed=16175638; DOI=10.1002/mrd.20383; RA Hlivko J.T., Chakraborty S., Hlivko T.J., Sengupta A., James P.F.; RT "The human Na,K-ATPase alpha 4 isoform is a ouabain-sensitive alpha isoform RT that is expressed in sperm."; RL Mol. Reprod. Dev. 73:101-115(2006). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis, and Urinary bladder; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69 AND 138-1029 (ISOFORM 1). RX PubMed=12119109; DOI=10.1016/s0378-1119(02)00647-9; RA Keryanov S., Gardner K.L.; RT "Physical mapping and characterization of the human Na,K-ATPase isoform, RT ATP1A4."; RL Gene 292:151-166(2002). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-220 (ISOFORM 1), AND VARIANT RP ASP-83. RC TISSUE=Testis; RX PubMed=7809153; DOI=10.1073/pnas.91.26.12952; RA Shamraj O.I., Lingrel J.B.; RT "A putative fourth Na+,K(+)-ATPase alpha-subunit gene is expressed in RT testis."; RL Proc. Natl. Acad. Sci. U.S.A. 91:12952-12956(1994). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 549-1017 (ISOFORM 1). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). CC -!- FUNCTION: This is the catalytic component of the active enzyme, which CC catalyzes the hydrolysis of ATP coupled with the exchange of sodium and CC potassium ions across the plasma membrane. This action creates the CC electrochemical gradient of sodium and potassium ions, providing the CC energy for active transport of various nutrients. Plays a role in sperm CC motility. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + CC Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC EC=7.2.2.13; Evidence={ECO:0000250|UniProtKB:Q64541}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18354; CC Evidence={ECO:0000250|UniProtKB:Q64541}; CC -!- ACTIVITY REGULATION: Specifically inhibited by an endogenous cardiac CC glycoside, ouabain. {ECO:0000269|PubMed:16175638}. CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an CC additional regulatory subunit. {ECO:0000305}. CC -!- INTERACTION: CC Q13733-2; P78358: CTAG1B; NbExp=3; IntAct=EBI-12356439, EBI-1188472; CC Q13733-2; Q9NPQ8-4: RIC8A; NbExp=3; IntAct=EBI-12356439, EBI-9091816; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16175638}; CC Multi-pass membrane protein {ECO:0000269|PubMed:16175638}. Note=In CC mature sperm, located in the principle piece of the sperm flagellum. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13733-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13733-2; Sequence=VSP_007364; CC -!- TISSUE SPECIFICITY: Specifically expressed in testis. Found in very low CC levels in skeletal muscle. Expressed in mature sperm (at protein CC level). CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) CC family. Type IIC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ07964.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC05228.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF506797; AAQ07964.1; ALT_INIT; mRNA. DR EMBL; AL121987; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF421887; AAL35818.1; -; Genomic_DNA. DR EMBL; AF310646; AAK72396.2; -; Genomic_DNA. DR EMBL; AF430843; AAK72396.2; JOINED; Genomic_DNA. DR EMBL; AF390027; AAK72396.2; JOINED; Genomic_DNA. DR EMBL; AY039031; AAK72396.2; JOINED; Genomic_DNA. DR EMBL; AF459737; AAL66357.1; -; mRNA. DR EMBL; AF352828; AAM20793.1; -; Genomic_DNA. DR EMBL; AH002997; AAA60941.1; -; Genomic_DNA. DR EMBL; AK098076; BAC05228.1; ALT_INIT; mRNA. DR EMBL; BC028297; AAH28297.1; -; mRNA. DR EMBL; BC094801; AAH94801.1; -; mRNA. DR CCDS; CCDS1197.1; -. [Q13733-1] DR CCDS; CCDS44255.1; -. [Q13733-2] DR RefSeq; NP_001001734.1; NM_001001734.1. [Q13733-2] DR RefSeq; NP_653300.2; NM_144699.3. [Q13733-1] DR AlphaFoldDB; Q13733; -. DR SMR; Q13733; -. DR BioGRID; 106970; 35. DR IntAct; Q13733; 9. DR MINT; Q13733; -. DR STRING; 9606.ENSP00000357060; -. DR ChEMBL; CHEMBL2095186; -. DR DrugBank; DB09020; Bisacodyl. DR DrugBank; DB09479; Rubidium Rb-82. DR DrugBank; DB16690; Tegoprazan. DR DrugCentral; Q13733; -. DR iPTMnet; Q13733; -. DR MetOSite; Q13733; -. DR PhosphoSitePlus; Q13733; -. DR SwissPalm; Q13733; -. DR BioMuta; ATP1A4; -. DR DMDM; 23830899; -. DR jPOST; Q13733; -. DR MassIVE; Q13733; -. DR MaxQB; Q13733; -. DR PaxDb; 9606-ENSP00000357060; -. DR PeptideAtlas; Q13733; -. DR ProteomicsDB; 59668; -. [Q13733-1] DR ProteomicsDB; 59669; -. [Q13733-2] DR Antibodypedia; 55096; 19 antibodies from 5 providers. DR DNASU; 480; -. DR Ensembl; ENST00000368081.9; ENSP00000357060.4; ENSG00000132681.17. [Q13733-1] DR Ensembl; ENST00000470705.1; ENSP00000433094.1; ENSG00000132681.17. [Q13733-2] DR GeneID; 480; -. DR KEGG; hsa:480; -. DR MANE-Select; ENST00000368081.9; ENSP00000357060.4; NM_144699.4; NP_653300.2. DR UCSC; uc001fve.5; human. [Q13733-1] DR AGR; HGNC:14073; -. DR CTD; 480; -. DR DisGeNET; 480; -. DR GeneCards; ATP1A4; -. DR HGNC; HGNC:14073; ATP1A4. DR HPA; ENSG00000132681; Tissue enhanced (placenta, testis, urinary bladder). DR MIM; 607321; gene. DR neXtProt; NX_Q13733; -. DR OpenTargets; ENSG00000132681; -. DR PharmGKB; PA65; -. DR VEuPathDB; HostDB:ENSG00000132681; -. DR eggNOG; KOG0203; Eukaryota. DR GeneTree; ENSGT00940000162378; -. DR HOGENOM; CLU_002360_4_1_1; -. DR InParanoid; Q13733; -. DR OMA; NGQEYSM; -. DR OrthoDB; 203629at2759; -. DR PhylomeDB; Q13733; -. DR TreeFam; TF312838; -. DR PathwayCommons; Q13733; -. DR Reactome; R-HSA-5578775; Ion homeostasis. DR Reactome; R-HSA-936837; Ion transport by P-type ATPases. DR Reactome; R-HSA-9679191; Potential therapeutics for SARS. DR SignaLink; Q13733; -. DR BioGRID-ORCS; 480; 13 hits in 1149 CRISPR screens. DR ChiTaRS; ATP1A4; human. DR GeneWiki; ATP1A4; -. DR GenomeRNAi; 480; -. DR Pharos; Q13733; Tclin. DR PRO; PR:Q13733; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q13733; Protein. DR Bgee; ENSG00000132681; Expressed in left testis and 88 other cell types or tissues. DR ExpressionAtlas; Q13733; baseline and differential. DR GO; GO:0042995; C:cell projection; IBA:GO_Central. DR GO; GO:0045121; C:membrane raft; ISS:ARUK-UCL. DR GO; GO:0097733; C:photoreceptor cell cilium; IDA:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0120200; C:rod photoreceptor outer segment; IDA:ARUK-UCL. DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IPI:ARUK-UCL. DR GO; GO:0097225; C:sperm midpiece; IDA:ARUK-UCL. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IGI:ARUK-UCL. DR GO; GO:0019900; F:kinase binding; ISS:ARUK-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IGI:ARUK-UCL. DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:ARUK-UCL. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0009566; P:fertilization; IEA:Ensembl. DR GO; GO:0030317; P:flagellated sperm motility; IDA:UniProtKB. DR GO; GO:0030007; P:intracellular potassium ion homeostasis; IBA:GO_Central. DR GO; GO:0006883; P:intracellular sodium ion homeostasis; IBA:GO_Central. DR GO; GO:0006811; P:monoatomic ion transport; NAS:ARUK-UCL. DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central. DR GO; GO:0071805; P:potassium ion transmembrane transport; IGI:ARUK-UCL. DR GO; GO:0006813; P:potassium ion transport; TAS:UniProtKB. DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central. DR GO; GO:0030641; P:regulation of cellular pH; IDA:UniProtKB. DR GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl. DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central. DR GO; GO:0035725; P:sodium ion transmembrane transport; IGI:ARUK-UCL. DR GO; GO:0006814; P:sodium ion transport; TAS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL. 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:SF3; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA-4; 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; 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. DR Genevisible; Q13733; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cell membrane; Ion transport; Magnesium; KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium; KW Potassium transport; Reference proteome; Sodium; Sodium transport; KW Sodium/potassium transport; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..1029 FT /note="Sodium/potassium-transporting ATPase subunit alpha- FT 4" FT /id="PRO_0000046303" FT TOPO_DOM 1..95 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 96..116 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 117..139 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 140..160 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 161..296 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 297..316 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 317..328 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 329..346 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 347..778 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 779..798 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 799..808 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 809..829 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 830..849 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 850..872 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 873..924 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 925..944 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 945..957 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 958..976 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 977..991 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 992..1012 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 1013..1029 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 90..92 FT /note="Interaction with phosphoinositide-3 kinase" FT /evidence="ECO:0000250" FT REGION 223..242 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..34 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 223..240 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 384 FT /note="4-aspartylphosphate intermediate" FT /evidence="ECO:0000250" FT BINDING 723 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 727 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT MOD_RES 949 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000250" FT VAR_SEQ 1..864 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007364" FT VARIANT 83 FT /note="G -> D (in dbSNP:rs6427504)" FT /evidence="ECO:0000269|PubMed:7809153" FT /id="VAR_048375" FT VARIANT 297 FT /note="E -> K (in dbSNP:rs17368402)" FT /id="VAR_048376" FT VARIANT 541 FT /note="M -> R (in dbSNP:rs16831482)" FT /id="VAR_048377" FT VARIANT 586 FT /note="M -> I (in dbSNP:rs7528360)" FT /id="VAR_048378" FT CONFLICT 155 FT /note="S -> W (in Ref. 5; AAA60941)" FT /evidence="ECO:0000305" FT CONFLICT 991..1017 FT /note="ITWWLCAIPYSILIFVYDEIRKLLIRQ -> WSFALTAQAGVKWRILGLLQP FT LPPRFK (in Ref. 6; BAC05228)" FT /evidence="ECO:0000305" SQ SEQUENCE 1029 AA; 114166 MW; 69958248424D2C0B CRC64; MGLWGKKGTV APHDQSPRRR PKKGLIKKKM VKREKQKRNM EELKKEVVMD DHKLTLEELS TKYSVDLTKG HSHQRAKEIL TRGGPNTVTP PPTTPEWVKF CKQLFGGFSL LLWTGAILCF VAYSIQIYFN EEPTKDNLYL SIVLSVVVIV TGCFSYYQEA KSSKIMESFK NMVPQQALVI RGGEKMQINV QEVVLGDLVE IKGGDRVPAD LRLISAQGCK VDNSSLTGES EPQSRSPDFT HENPLETRNI CFFSTNCVEG TARGIVIATG DSTVMGRIAS LTSGLAVGQT PIAAEIEHFI HLITVVAVFL GVTFFALSLL LGYGWLEAII FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDMTVYEADT TEEQTGKTFT KSSDTWFMLA RIAGLCNRAD FKANQEILPI AKRATTGDAS ESALLKFIEQ SYSSVAEMRE KNPKVAEIPF NSTNKYQMSI HLREDSSQTH VLMMKGAPER ILEFCSTFLL NGQEYSMNDE MKEAFQNAYL ELGGLGERVL GFCFLNLPSS FSKGFPFNTD EINFPMDNLC FVGLISMIDP PRAAVPDAVS KCRSAGIKVI MVTGDHPITA KAIAKGVGII SEGTETAEEV AARLKIPISK VDASAAKAIV VHGAELKDIQ SKQLDQILQN HPEIVFARTS PQQKLIIVEG CQRLGAVVAV TGDGVNDSPA LKKADIGIAM GISGSDVSKQ AADMILLDDN FASIVTGVEE GRLIFDNLKK SIMYTLTSNI PEITPFLMFI ILGIPLPLGT ITILCIDLGT DMVPAISLAY ESAESDIMKR LPRNPKTDNL VNHRLIGMAY GQIGMIQALA GFFTYFVILA ENGFRPVDLL GIRLHWEDKY LNDLEDSYGQ QWTYEQRKVV EFTCQTAFFV TIVVVQWADL IISKTRRNSL FQQGMRNKVL IFGILEETLL AAFLSYTPGM DVALRMYPLK ITWWLCAIPY SILIFVYDEI RKLLIRQHPD GWVERETYY //