AMPL_MOUSE
ID AMPL_MOUSE Reviewed; 519 AA.
AC Q9CPY7; Q3TFS5; Q4FJV1; Q4FK15; Q99P44; Q9CWN8;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cytosol aminopeptidase {ECO:0000305};
DE EC=3.4.11.1 {ECO:0000250|UniProtKB:P00727};
DE AltName: Full=Cysteinylglycine-S-conjugate dipeptidase {ECO:0000250|UniProtKB:P00727};
DE EC=3.4.13.23 {ECO:0000250|UniProtKB:P00727};
DE AltName: Full=Leucine aminopeptidase 3 {ECO:0000312|MGI:MGI:1914238};
DE Short=LAP-3;
DE AltName: Full=Leucyl aminopeptidase {ECO:0000312|MGI:MGI:1914238};
DE AltName: Full=Peptidase S {ECO:0000312|MGI:MGI:1914238};
DE AltName: Full=Proline aminopeptidase {ECO:0000250|UniProtKB:P28839};
DE EC=3.4.11.5 {ECO:0000250|UniProtKB:P28839};
DE AltName: Full=Prolyl aminopeptidase;
GN Name=Lap3 {ECO:0000312|MGI:MGI:1914238}; Synonyms=Lapep;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Zhuang D.Z., Gunnarsson D., Toffia O., Lind M., Lundgren P., Selstam G.;
RT "Mammalian Lap-D proteins related to ovarian development and
RT differentiation.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Amnion, Bone marrow, Cerebellum, Embryo, Kidney, Lung, Placenta, and
RC Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP PROTEIN SEQUENCE OF 474-481, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180 AND SER-238, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-45; LYS-61; LYS-103; LYS-221;
RP LYS-455; LYS-476 AND LYS-489, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221; LYS-455 AND LYS-489, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Cytosolic metallopeptidase that catalyzes the removal of
CC unsubstituted N-terminal hydrophobic amino acids from various peptides.
CC The presence of Zn(2+) ions is essential for the peptidase activity,
CC and the association with other cofactors can modulate the substrate
CC spectificity of the enzyme. For instance, in the presence of Mn(2+), it
CC displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-
CC conjugates. Involved in the metabolism of glutathione and in the
CC degradation of glutathione S-conjugates, which may play a role in the
CC control of the cell redox status. {ECO:0000250|UniProtKB:P00727}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000250|UniProtKB:P00727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted
CC L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103;
CC EC=3.4.13.23; Evidence={ECO:0000250|UniProtKB:P00727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445;
CC Evidence={ECO:0000250|UniProtKB:P00727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine;
CC Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:61694;
CC Evidence={ECO:0000250|UniProtKB:P00727};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784;
CC Evidence={ECO:0000250|UniProtKB:P00727};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-
CC cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:145802, ChEBI:CHEBI:145803;
CC Evidence={ECO:0000250|UniProtKB:Q68FS4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569;
CC Evidence={ECO:0000250|UniProtKB:Q68FS4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000250|UniProtKB:P28839};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00727};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P00727};
CC Note=Binds two metal ions per subunit. Two metal binding sites with
CC different affinities are located in the enzyme active site and can be
CC occupied in vitro by different metals: site 1 is occupied by Zn(2+),
CC Mn(2+), Mg(2+) or Co(2+), while the tight binding site 2 can be
CC occupied by only Zn(2+) or Co(2+). One Zn(2+) ion is tightly bound to
CC site 2 and essential for enzyme activity in vivo, while site 1 can be
CC occupied by different metals to give different enzymatic activities.
CC Mn(2+) is required for Cys-Gly hydrolysis activity. A third metal
CC binding site may serve a structural role, possibly stabilizing part of
CC the interface between the N-terminal and the catalytic domain.
CC {ECO:0000250|UniProtKB:P00727};
CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P00727}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68FS4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CPY7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CPY7-2; Sequence=VSP_022632;
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB23958.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB25769.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB27726.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE39141.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE40823.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF334160; AAK13495.1; -; mRNA.
DR EMBL; CT010237; CAJ18445.1; -; mRNA.
DR EMBL; CT010301; CAJ18509.1; -; mRNA.
DR EMBL; AK002819; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK005334; BAB23958.1; ALT_INIT; mRNA.
DR EMBL; AK008600; BAB25769.1; ALT_INIT; mRNA.
DR EMBL; AK010502; BAB26987.1; -; mRNA.
DR EMBL; AK011604; BAB27726.1; ALT_INIT; mRNA.
DR EMBL; AK166958; BAE39141.1; ALT_INIT; mRNA.
DR EMBL; AK169032; BAE40823.1; ALT_INIT; mRNA.
DR EMBL; BC016536; AAH16536.1; -; mRNA.
DR CCDS; CCDS19274.1; -. [Q9CPY7-1]
DR RefSeq; NP_077754.3; NM_024434.6. [Q9CPY7-1]
DR AlphaFoldDB; Q9CPY7; -.
DR SMR; Q9CPY7; -.
DR BioGRID; 211856; 22.
DR IntAct; Q9CPY7; 1.
DR STRING; 10090.ENSMUSP00000040222; -.
DR MEROPS; M17.001; -.
DR iPTMnet; Q9CPY7; -.
DR PhosphoSitePlus; Q9CPY7; -.
DR SwissPalm; Q9CPY7; -.
DR REPRODUCTION-2DPAGE; IPI00828469; -.
DR CPTAC; non-CPTAC-3688; -.
DR CPTAC; non-CPTAC-3689; -.
DR EPD; Q9CPY7; -.
DR jPOST; Q9CPY7; -.
DR MaxQB; Q9CPY7; -.
DR PaxDb; Q9CPY7; -.
DR PeptideAtlas; Q9CPY7; -.
DR PRIDE; Q9CPY7; -.
DR ProteomicsDB; 296032; -. [Q9CPY7-1]
DR ProteomicsDB; 296033; -. [Q9CPY7-2]
DR Antibodypedia; 23080; 240 antibodies from 32 providers.
DR DNASU; 66988; -.
DR Ensembl; ENSMUST00000046122; ENSMUSP00000040222; ENSMUSG00000039682. [Q9CPY7-1]
DR GeneID; 66988; -.
DR KEGG; mmu:66988; -.
DR UCSC; uc008xiy.2; mouse. [Q9CPY7-1]
DR CTD; 51056; -.
DR MGI; MGI:1914238; Lap3.
DR VEuPathDB; HostDB:ENSMUSG00000039682; -.
DR eggNOG; KOG2597; Eukaryota.
DR GeneTree; ENSGT00530000063255; -.
DR HOGENOM; CLU_013734_1_2_1; -.
DR InParanoid; Q9CPY7; -.
DR OMA; MKNTGPR; -.
DR OrthoDB; 562530at2759; -.
DR PhylomeDB; Q9CPY7; -.
DR TreeFam; TF314954; -.
DR BioGRID-ORCS; 66988; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Lap3; mouse.
DR PRO; PR:Q9CPY7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CPY7; protein.
DR Bgee; ENSMUSG00000039682; Expressed in small intestine Peyer's patch and 270 other tissues.
DR ExpressionAtlas; Q9CPY7; baseline and differential.
DR Genevisible; Q9CPY7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:RHEA.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Aminopeptidase; Cytoplasm;
KW Direct protein sequencing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Phosphoprotein; Protease; Reference proteome; Zinc.
FT CHAIN 1..519
FT /note="Cytosol aminopeptidase"
FT /id="PRO_0000165826"
FT ACT_SITE 294
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT ACT_SITE 368
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 366
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT BINDING 366
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00727"
FT MOD_RES 45
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68FS4"
FT MOD_RES 61
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28838"
FT MOD_RES 221
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 221
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 455
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 455
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 476
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 489
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 489
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_022632"
FT CONFLICT 46
FT /note="D -> G (in Ref. 2; CAJ18509)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="F -> L (in Ref. 2; CAJ18445)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="A -> D (in Ref. 3; BAB26987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 56141 MW; 46729A9CE4C060A5 CRC64;
MYLLPLPAAA RVALRRLGVR GLWDRGLSTA DMTKGLVLGI YAKDKDDDLP QFTSAGESFN
KLVSGKLREM LNISGPPLKA GKTRTFYGLH QDFPSVVVVG LGKRSAGVDD QENWHEGKEN
IRAAVAAGCR QVQDLELPSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK VAVSAKLHGS
GDLEAWEKGV LFASGQNLAR HLMESPANEM TPTRFAEIIE KNLKSASSKT KVHIRPKSWI
EEQEMGSFLS VAKGSEEPPV FLEIHYMGSP NATEAPLVFV GKGITFDSGG ISIKASANMD
LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RARNGKTIQV
DNTDAEGRLI LADALCYAHT FNPKVIINAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE
ASVETGDRVW RMPLFEHYTR QVIDCQLADV NNLGKYRSAG ACTAAAFLRE FVTHTKWAHL
DIAGVMTNKD EIPYLRKGMS GRPTRTLIEF LLRFSKDSS
