AT133_HUMAN
ID AT133_HUMAN Reviewed; 1226 AA.
AC Q9H7F0; Q8NC11; Q96KS1;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 4.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Polyamine-transporting ATPase 13A3;
DE AltName: Full=ATPase family homolog up-regulated in senescence cells 1;
DE AltName: Full=Putrescine transporting ATPase {ECO:0000305|PubMed:33310703};
DE EC=7.6.2.16 {ECO:0000269|PubMed:33310703};
GN Name=ATP13A3 {ECO:0000303|PubMed:33310703, ECO:0000312|HGNC:HGNC:24113};
GN Synonyms=AFURS1 {ECO:0000303|PubMed:11867234};
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] (ISOFORM 2).
RX PubMed=11867234; DOI=10.1016/s0378-1119(01)00881-2;
RA Habtemichael N., Kovacs G.;
RT "Cloning the AFURS1 gene which is up-regulated in senescent human
RT parenchymal kidney cells.";
RL Gene 283:271-275(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 402-1226 (ISOFORM 1).
RC TISSUE=Coronary artery, and Placenta;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-817, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-817, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-817, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=27429841;
RA Madan M., Patel A., Skruber K., Geerts D., Altomare D.A., Iv O.P.;
RT "ATP13A3 and caveolin-1 as potential biomarkers for
RT difluoromethylornithine-based therapies in pancreatic cancers.";
RL Am. J. Cancer Res. 6:1231-1252(2016).
RN [13]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND TOPOLOGY.
RX PubMed=29505581; DOI=10.1371/journal.pone.0193228;
RA Soerensen D.M., Holemans T., van Veen S., Martin S., Arslan T.,
RA Haagendahl I.W., Holen H.W., Hamouda N.N., Eggermont J., Palmgren M.,
RA Vangheluwe P.;
RT "Parkinson disease related ATP13A2 evolved early in animal evolution.";
RL PLoS ONE 13:e0193228-e0193228(2018).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-498.
RX PubMed=33310703; DOI=10.1074/jbc.ra120.013908;
RA Hamouda N.N., Van den Haute C., Vanhoutte R., Sannerud R., Azfar M.,
RA Mayer R., Cortes Calabuig A., Swinnen J.V., Agostinis P., Baekelandt V.,
RA Annaert W., Impens F., Verhelst S.H.L., Eggermont J., Martin S.,
RA Vangheluwe P.;
RT "ATP13A3 is a major component of the enigmatic mammalian polyamine
RT transport system.";
RL J. Biol. Chem. 296:100182-100182(2021).
CC -!- FUNCTION: ATP-driven pump involved in endocytosis-dependent polyamine
CC transport. Uses ATP as an energy source to transfer polyamine precursor
CC putrescine from the endosomal compartment to the cytosol.
CC {ECO:0000269|PubMed:27429841, ECO:0000269|PubMed:33310703}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + putrescine(out) = ADP + H(+) + phosphate +
CC putrescine(in); Xref=Rhea:RHEA:29995, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:326268, ChEBI:CHEBI:456216; EC=7.6.2.16;
CC Evidence={ECO:0000269|PubMed:33310703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29996;
CC Evidence={ECO:0000305|PubMed:33310703};
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000269|PubMed:29505581}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:29505581};
CC Multi-pass membrane protein {ECO:0000255}. Late endosome membrane
CC {ECO:0000269|PubMed:29505581}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Mainly targeted to the recycling endosomes and to a
CC lesser extent to the early and late endosomes.
CC {ECO:0000269|PubMed:29505581}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H7F0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H7F0-2; Sequence=VSP_007314, VSP_036300, VSP_007315,
CC VSP_007316;
CC -!- TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:29505581}.
CC -!- INDUCTION: Up-regulated by polyamine biosynthesis inhibitor,
CC difluoromethylornithine (DFMO). {ECO:0000269|PubMed:27429841}.
CC -!- MISCELLANEOUS: [Isoform 2]: Dubious isoform produced through aberrant
CC splice sites. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14942.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14942.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC11398.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ306929; CAC84902.1; -; mRNA.
DR EMBL; AC108676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK024639; BAB14942.1; ALT_SEQ; mRNA.
DR EMBL; AK075094; BAC11398.1; ALT_INIT; mRNA.
DR CCDS; CCDS43187.1; -. [Q9H7F0-1]
DR RefSeq; NP_078800.3; NM_024524.3. [Q9H7F0-1]
DR RefSeq; XP_011511425.1; XM_011513123.2. [Q9H7F0-1]
DR AlphaFoldDB; Q9H7F0; -.
DR SMR; Q9H7F0; -.
DR BioGRID; 122719; 181.
DR IntAct; Q9H7F0; 23.
DR MINT; Q9H7F0; -.
DR STRING; 9606.ENSP00000416508; -.
DR iPTMnet; Q9H7F0; -.
DR PhosphoSitePlus; Q9H7F0; -.
DR SwissPalm; Q9H7F0; -.
DR BioMuta; ATP13A3; -.
DR DMDM; 223590262; -.
DR EPD; Q9H7F0; -.
DR jPOST; Q9H7F0; -.
DR MassIVE; Q9H7F0; -.
DR MaxQB; Q9H7F0; -.
DR PaxDb; Q9H7F0; -.
DR PeptideAtlas; Q9H7F0; -.
DR PRIDE; Q9H7F0; -.
DR ProteomicsDB; 81118; -. [Q9H7F0-1]
DR ProteomicsDB; 81119; -. [Q9H7F0-2]
DR Antibodypedia; 33892; 65 antibodies from 14 providers.
DR DNASU; 79572; -.
DR Ensembl; ENST00000439040.6; ENSP00000416508.1; ENSG00000133657.17. [Q9H7F0-1]
DR Ensembl; ENST00000645538.1; ENSP00000494471.1; ENSG00000133657.17. [Q9H7F0-1]
DR GeneID; 79572; -.
DR KEGG; hsa:79572; -.
DR UCSC; uc003fty.5; human. [Q9H7F0-1]
DR CTD; 79572; -.
DR DisGeNET; 79572; -.
DR GeneCards; ATP13A3; -.
DR HGNC; HGNC:24113; ATP13A3.
DR HPA; ENSG00000133657; Low tissue specificity.
DR MIM; 610232; gene.
DR neXtProt; NX_Q9H7F0; -.
DR OpenTargets; ENSG00000133657; -.
DR PharmGKB; PA134971145; -.
DR VEuPathDB; HostDB:ENSG00000133657; -.
DR eggNOG; KOG0208; Eukaryota.
DR GeneTree; ENSGT00940000155941; -.
DR HOGENOM; CLU_001828_0_0_1; -.
DR InParanoid; Q9H7F0; -.
DR OrthoDB; 172453at2759; -.
DR PhylomeDB; Q9H7F0; -.
DR TreeFam; TF300331; -.
DR PathwayCommons; Q9H7F0; -.
DR SignaLink; Q9H7F0; -.
DR BioGRID-ORCS; 79572; 6 hits in 1085 CRISPR screens.
DR ChiTaRS; ATP13A3; human.
DR GeneWiki; ATP13A3; -.
DR GenomeRNAi; 79572; -.
DR Pharos; Q9H7F0; Tbio.
DR PRO; PR:Q9H7F0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H7F0; protein.
DR Bgee; ENSG00000133657; Expressed in decidua and 205 other tissues.
DR ExpressionAtlas; Q9H7F0; baseline and differential.
DR Genevisible; Q9H7F0; HS.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0015417; F:ABC-type polyamine transporter activity; IBA:GO_Central.
DR GO; GO:0015594; F:ABC-type putrescine transporter activity; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:1902047; P:polyamine transmembrane transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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; IPR006544; P-type_TPase_V.
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 Pfam; PF12409; P5-ATPase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Endosome; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1226
FT /note="Polyamine-transporting ATPase 13A3"
FT /id="PRO_0000046425"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT INTRAMEM 29..49
FT /evidence="ECO:0000305|PubMed:29505581"
FT TOPO_DOM 50..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..232
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..448
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..940
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 941..961
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 962
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 984..999
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 1000..1020
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1021..1073
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 1074..1094
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1095..1105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 1106..1126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1127..1143
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:29505581"
FT TRANSMEM 1144..1164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1165..1226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29505581"
FT ACT_SITE 498
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9NQ11"
FT BINDING 498..500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 500
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 684
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 750
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 883..887
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 883
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P39986"
FT BINDING 887
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..277
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11867234"
FT /id="VSP_007314"
FT VAR_SEQ 278..279
FT /note="NE -> MS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11867234"
FT /id="VSP_036300"
FT VAR_SEQ 936..978
FT /note="FCVFKFMALYSIIQYFSVTLLYSILSNLGDFQFLFIDLAIILV -> SCELA
FT LFSIVTYSLDHFIISILISSMLVLFFSDFHNCAFYSLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11867234"
FT /id="VSP_007315"
FT VAR_SEQ 979..1226
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11867234"
FT /id="VSP_007316"
FT MUTAGEN 498
FT /note="D->N: Impairs the transport activity."
FT /evidence="ECO:0000269|PubMed:33310703"
FT CONFLICT 347
FT /note="E -> Q (in Ref. 1; CAC84902)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="T -> P (in Ref. 1; CAC84902)"
FT /evidence="ECO:0000305"
FT CONFLICT 784
FT /note="V -> F (in Ref. 3; BAC11398)"
FT /evidence="ECO:0000305"
FT CONFLICT 807
FT /note="E -> G (in Ref. 3; BAC11398)"
FT /evidence="ECO:0000305"
FT CONFLICT 964
FT /note="G -> R (in Ref. 3; BAC11398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1226 AA; 138043 MW; 8DD1C0451223C7AB CRC64;
MDREERKTIN QGQEDEMEIY GYNLSRWKLA IVSLGVICSG GFLLLLLYWM PEWRVKATCV
RAAIKDCEVV LLRTTDEFKM WFCAKIRVLS LETYPVSSPK SMSNKLSNGH AVCLIENPTE
ENRHRISKYS QTESQQIRYF THHSVKYFWN DTIHNFDFLK GLDEGVSCTS IYEKHSAGLT
KGMHAYRKLL YGVNEIAVKV PSVFKLLIKE VLNPFYIFQL FSVILWSTDE YYYYALAIVV
MSIVSIVSSL YSIRKQYVML HDMVATHSTV RVSVCRVNEE IEEIFSTDLV PGDVMVIPLN
GTIMPCDAVL INGTCIVNES MLTGESVPVT KTNLPNPSVD VKGIGDELYN PETHKRHTLF
CGTTVIQTRF YTGELVKAIV VRTGFSTSKG QLVRSILYPK PTDFKLYRDA YLFLLCLVAV
AGIGFIYTII NSILNEVQVG VIIIESLDII TITVPPALPA AMTAGIVYAQ RRLKKIGIFC
ISPQRINICG QLNLVCFDKT GTLTEDGLDL WGIQRVENAR FLSPEENVCN EMLVKSQFVA
CMATCHSLTK IEGVLSGDPL DLKMFEAIGW ILEEATEEET ALHNRIMPTV VRPPKQLLPE
STPAGNQEME LFELPATYEI GIVRQFPFSS ALQRMSVVAR VLGDRKMDAY MKGAPEAIAG
LCKPETVPVD FQNVLEDFTK QGFRVIALAH RKLESKLTWH KVQNISRDAI ENNMDFMGLI
IMQNKLKQET PAVLEDLHKA NIRTVMVTGD SMLTAVSVAR DCGMILPQDK VIIAEALPPK
DGKVAKINWH YADSLTQCSH PSAIDPEAIP VKLVHDSLED LQMTRYHFAM NGKSFSVILE
HFQDLVPKLM LHGTVFARMA PDQKTQLIEA LQNVDYFVGM CGDGANDCGA LKRAHGGISL
SELEASVASP FTSKTPSISC VPNLIREGRA ALITSFCVFK FMALYSIIQY FSVTLLYSIL
SNLGDFQFLF IDLAIILVVV FTMSLNPAWK ELVAQRPPSG LISGALLFSV LSQIIICIGF
QSLGFFWVKQ QPWYEVWHPK SDACNTTGSG FWNSSHVDNE TELDEHNIQN YENTTVFFIS
SFQYLIVAIA FSKGKPFRQP CYKNYFFVFS VIFLYIFILF IMLYPVASVD QVLQIVCVPY
QWRVTMLIIV LVNAFVSITV EESVDRWGKC CLPWALGCRK KTPKAKYMYL AQELLVDPEW
PPKPQTTTEA KALVKENGSC QIITIT
