ATP9A_HUMAN
ID ATP9A_HUMAN Reviewed; 1047 AA.
AC O75110; E1P5Y3; E1P5Y4; Q5TFW5; Q5TFW6; Q5TFW9; Q6ZMF3; Q9NQK6; Q9NQK7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Probable phospholipid-transporting ATPase IIA;
DE EC=7.6.2.1 {ECO:0000305|PubMed:30213940};
DE AltName: Full=ATPase class II type 9A;
GN Name=ATP9A {ECO:0000303|PubMed:30213940, ECO:0000312|HGNC:HGNC:13540};
GN Synonyms=ATPIIA, KIAA0611;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-1047 (ISOFORM SHORT).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-1047 (ISOFORM LONG).
RC TISSUE=Hepatoma;
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=21914794; DOI=10.1074/jbc.m111.281006;
RA Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M., Nakayama K.,
RA Shin H.W.;
RT "ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes
RT to the trans-Golgi network in a CDC50 protein-independent manner.";
RL J. Biol. Chem. 286:38159-38167(2011).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27733620; DOI=10.1091/mbc.e16-08-0586;
RA Tanaka Y., Ono N., Shima T., Tanaka G., Katoh Y., Nakayama K., Takatsu H.,
RA Shin H.W.;
RT "The phospholipid flippase ATP9A is required for the recycling pathway from
RT the endosomes to the plasma membrane.";
RL Mol. Biol. Cell 27:3883-3893(2016).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MON2 AND DOP1B, AND
RP SUBCELLULAR LOCATION.
RX PubMed=30213940; DOI=10.1038/s41467-018-06114-3;
RA McGough I.J., de Groot R.E.A., Jellett A.P., Betist M.C., Varandas K.C.,
RA Danson C.M., Heesom K.J., Korswagen H.C., Cullen P.J.;
RT "SNX3-retromer requires an evolutionary conserved MON2:DOPEY2:ATP9A complex
RT to mediate Wntless sorting and Wnt secretion.";
RL Nat. Commun. 9:3737-3737(2018).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30947313; DOI=10.1371/journal.pone.0213069;
RA Naik J., Hau C.M., Ten Bloemendaal L., Mok K.S., Hajji N., Wehman A.M.,
RA Meisner S., Muncan V., Paauw N.J., de Vries H.E., Nieuwland R.,
RA Paulusma C.C., Bosma P.J.;
RT "The P4-ATPase ATP9A is a novel determinant of exosome release.";
RL PLoS ONE 14:e0213069-e0213069(2019).
CC -!- FUNCTION: Plays a role in regulating membrane trafficking of cargo
CC proteins, namely endosome to plasma membrane recycling and endosome to
CC trans-Golgi network retrograde transport (PubMed:27733620,
CC PubMed:30213940). In complex with MON2 and DOP1B, regulates SNX3
CC retromer-mediated endosomal sorting of WLS, a transporter of Wnt
CC morphogens in developing tissues. Participates in the formation of
CC endosomal carriers that direct WLS trafficking back to Golgi, away from
CC lysosomal degradation (PubMed:30213940). Appears to be implicated in
CC intercellular communication by negatively regulating the release of
CC exosomes (PubMed:30947313). The flippase activity towards membrane
CC lipids and its role in membrane asymmetry remains to be proved
CC (PubMed:30947313). {ECO:0000269|PubMed:27733620,
CC ECO:0000269|PubMed:30213940, ECO:0000269|PubMed:30947313}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000305|PubMed:30213940};
CC -!- SUBUNIT: Heterotrimer with MON2 and DOP1B; this complex regulates SNX3-
CC retromer mediated endosomal sorting of WLS.
CC {ECO:0000269|PubMed:30213940}.
CC -!- SUBCELLULAR LOCATION: Early endosome membrane
CC {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:27733620,
CC ECO:0000269|PubMed:30213940}; Multi-pass membrane protein
CC {ECO:0000255}. Recycling endosome membrane
CC {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:27733620}; Multi-pass
CC membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:27733620,
CC ECO:0000269|PubMed:30213940}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30947313}; Multi-pass
CC membrane protein. Note=Efficient exit from the endoplasmic reticulum
CC does not require TMEM30A, nor TMEM30B (PubMed:21914794). Transiently
CC expressed in the plasma membrane (PubMed:30947313).
CC {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:30947313}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=O75110-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O75110-2; Sequence=VSP_000432;
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD18775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL035684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75597.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75598.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75599.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75600.1; -; Genomic_DNA.
DR EMBL; AB014511; BAA31586.1; -; mRNA.
DR EMBL; AK172802; BAD18775.1; ALT_INIT; mRNA.
DR CCDS; CCDS33489.1; -. [O75110-1]
DR RefSeq; NP_006036.1; NM_006045.2. [O75110-1]
DR AlphaFoldDB; O75110; -.
DR SMR; O75110; -.
DR BioGRID; 115389; 91.
DR IntAct; O75110; 35.
DR MINT; O75110; -.
DR STRING; 9606.ENSP00000342481; -.
DR TCDB; 3.A.3.8.16; the p-type atpase (p-atpase) superfamily.
DR iPTMnet; O75110; -.
DR PhosphoSitePlus; O75110; -.
DR SwissPalm; O75110; -.
DR BioMuta; ATP9A; -.
DR EPD; O75110; -.
DR jPOST; O75110; -.
DR MassIVE; O75110; -.
DR MaxQB; O75110; -.
DR PaxDb; O75110; -.
DR PeptideAtlas; O75110; -.
DR PRIDE; O75110; -.
DR ProteomicsDB; 49763; -. [O75110-1]
DR ProteomicsDB; 49764; -. [O75110-2]
DR Antibodypedia; 28658; 68 antibodies from 16 providers.
DR DNASU; 10079; -.
DR Ensembl; ENST00000338821.6; ENSP00000342481.5; ENSG00000054793.14. [O75110-1]
DR GeneID; 10079; -.
DR KEGG; hsa:10079; -.
DR MANE-Select; ENST00000338821.6; ENSP00000342481.5; NM_006045.3; NP_006036.1.
DR UCSC; uc002xwg.2; human. [O75110-1]
DR CTD; 10079; -.
DR DisGeNET; 10079; -.
DR GeneCards; ATP9A; -.
DR HGNC; HGNC:13540; ATP9A.
DR HPA; ENSG00000054793; Low tissue specificity.
DR MIM; 609126; gene.
DR neXtProt; NX_O75110; -.
DR OpenTargets; ENSG00000054793; -.
DR PharmGKB; PA25171; -.
DR VEuPathDB; HostDB:ENSG00000054793; -.
DR eggNOG; KOG0210; Eukaryota.
DR GeneTree; ENSGT00940000159181; -.
DR InParanoid; O75110; -.
DR OMA; HNVTPSF; -.
DR PhylomeDB; O75110; -.
DR TreeFam; TF300590; -.
DR BRENDA; 7.6.2.1; 2681.
DR PathwayCommons; O75110; -.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; O75110; -.
DR BioGRID-ORCS; 10079; 17 hits in 1069 CRISPR screens.
DR ChiTaRS; ATP9A; human.
DR GenomeRNAi; 10079; -.
DR Pharos; O75110; Tbio.
DR PRO; PR:O75110; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O75110; protein.
DR Bgee; ENSG00000054793; Expressed in middle temporal gyrus and 213 other tissues.
DR ExpressionAtlas; O75110; baseline and differential.
DR Genevisible; O75110; HS.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; 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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0002020; F:protease binding; IPI:ARUK-UCL.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:1903542; P:negative regulation of exosomal secretion; IMP:UniProtKB.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:2001135; P:regulation of endocytic recycling; IMP:UniProtKB.
DR GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030356; ATP9A.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PANTHER; PTHR24092:SF49; PTHR24092:SF49; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 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; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell membrane; Endosome;
KW Golgi apparatus; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1047
FT /note="Probable phospholipid-transporting ATPase IIA"
FT /id="PRO_0000046375"
FT TOPO_DOM 2..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..332
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..841
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..862
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 863..874
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 875..893
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 894..923
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 924..942
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 943..949
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 950..972
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 973..978
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 979..999
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1000..1006
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1007..1030
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1031..1047
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 391
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9HD20"
FT BINDING 785
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT BINDING 789
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q8NB49"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 149..269
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_000432"
FT CONFLICT 186
FT /note="F -> S (in Ref. 4; BAD18775)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="L -> P (in Ref. 4; BAD18775)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="S -> P (in Ref. 4; BAD18775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1047 AA; 118583 MW; 80C307CF5A396755 CRC64;
MTDNIPLQPV RQKKRMDSRP RAGCCEWLRC CGGGEARPRT VWLGHPEKRD QRYPRNVINN
QKYNFFTFLP GVLFNQFKYF FNLYFLLLAC SQFVPEMRLG ALYTYWVPLG FVLAVTVIRE
AVEEIRCYVR DKEVNSQVYS RLTARGTVKV KSSNIQVGDL IIVEKNQRVP ADMIFLRTSE
KNGSCFLRTD QLDGETDWKL RLPVACTQRL PTAADLLQIR SYVYAEEPNI DIHNFVGTFT
REDSDPPISE SLSIENTLWA GTVVASGTVV GVVLYTGREL RSVMNTSNPR SKIGLFDLEV
NCLTKILFGA LVVVSLVMVA LQHFAGRWYL QIIRFLLLFS NIIPISLRVN LDMGKIVYSW
VIRRDSKIPG TVVRSSTIPE QLGRISYLLT DKTGTLTQNE MIFKRLHLGT VAYGLDSMDE
VQSHIFSIYT QQSQDPPAQK GPTLTTKVRR TMSSRVHEAV KAIALCHNVT PVYESNGVTD
QAEAEKQYED SCRVYQASSP DEVALVQWTE SVGLTLVGRD QSSMQLRTPG DQILNFTILQ
IFPFTYESKR MGIIVRDEST GEITFYMKGA DVVMAGIVQY NDWLEEECGN MAREGLRVLV
VAKKSLAEEQ YQDFEARYVQ AKLSVHDRSL KVATVIESLE MEMELLCLTG VEDQLQADVR
PTLETLRNAG IKVWMLTGDK LETATCTAKN AHLVTRNQDI HVFRLVTNRG EAHLELNAFR
RKHDCALVIS GDSLEVCLKY YEYEFMELAC QCPAVVCCRC APTQKAQIVR LLQERTGKLT
CAVGDGGNDV SMIQESDCGV GVEGKEGKQA SLAADFSITQ FKHLGRLLMV HGRNSYKRSA
ALSQFVIHRS LCISTMQAVF SSVFYFASVP LYQGFLIIGY STIYTMFPVF SLVLDKDVKS
EVAMLYPELY KDLLKGRPLS YKTFLIWVLI SIYQGSTIMY GALLLFESEF VHIVAISFTS
LILTELLMVA LTIQTWHWLM TVAELLSLAC YIASLVFLHE FIDVYFIATL SFLWKVSVIT
LVSCLPLYVL KYLRRRFSPP SYSKLTS
