AT1A4_HUMAN
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 03-AUG-2022, entry version 200.
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};
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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; 33.
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; Q13733; -.
DR PeptideAtlas; Q13733; -.
DR PRIDE; Q13733; -.
DR ProteomicsDB; 59668; -. [Q13733-1]
DR ProteomicsDB; 59669; -. [Q13733-2]
DR Antibodypedia; 55096; 15 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 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; NSRVKFD; -.
DR OrthoDB; 388324at2759; -.
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; 12 hits in 1069 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 86 other tissues.
DR ExpressionAtlas; Q13733; baseline and differential.
DR Genevisible; Q13733; HS.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
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 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:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
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:0006811; P: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; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
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
