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PDP1_BOVIN
ID   PDP1_BOVIN              Reviewed;         538 AA.
AC   P35816;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial;
DE            Short=PDP 1;
DE            EC=3.1.3.43;
DE   AltName: Full=Protein phosphatase 2C;
DE   AltName: Full=Pyruvate dehydrogenase phosphatase catalytic subunit 1;
DE            Short=PDPC 1;
DE   Flags: Precursor;
GN   Name=PDP1; Synonyms=PDP, PPM2C;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8396421; DOI=10.1021/bi00086a002;
RA   Lawson J.E., Niu X.-D., Browning K.S., Trong H.L., Yan J., Reed L.J.;
RT   "Molecular cloning and expression of the catalytic subunit of bovine
RT   pyruvate dehydrogenase phosphatase and sequence similarity with protein
RT   phosphatase 2C.";
RL   Biochemistry 32:8987-8993(1993).
RN   [2]
RP   SUBUNIT.
RX   PubMed=9395502; DOI=10.1074/jbc.272.50.31625;
RA   Lawson J.E., Park S.H., Mattison A.R., Yan J., Reed L.J.;
RT   "Cloning, expression, and properties of the regulatory subunit of bovine
RT   pyruvate dehydrogenase phosphatase.";
RL   J. Biol. Chem. 272:31625-31629(1997).
CC   -!- FUNCTION: Catalyzes the dephosphorylation and concomitant reactivation
CC       of the alpha subunit of the E1 component of the pyruvate dehydrogenase
CC       complex.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha
CC         subunit] = L-seryl-[pyruvate dehydrogenase E1 alpha subunit] +
CC         phosphate; Xref=Rhea:RHEA:12669, Rhea:RHEA-COMP:13689, Rhea:RHEA-
CC         COMP:13690, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.43;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of a catalytic (PDP1) and a regulatory (PDPR)
CC       subunit. {ECO:0000269|PubMed:9395502}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA30697.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L18966; AAA30697.1; ALT_INIT; mRNA.
DR   PIR; A48692; A48692.
DR   RefSeq; NP_001193282.1; NM_001206353.1.
DR   RefSeq; XP_005215704.1; XM_005215647.3.
DR   RefSeq; XP_005215707.1; XM_005215650.3.
DR   RefSeq; XP_010810497.1; XM_010812195.2.
DR   PDB; 3MQ3; X-ray; 2.80 A; A=72-538.
DR   PDB; 6V0T; X-ray; 2.10 A; A=72-538.
DR   PDBsum; 3MQ3; -.
DR   PDBsum; 6V0T; -.
DR   AlphaFoldDB; P35816; -.
DR   SMR; P35816; -.
DR   STRING; 9913.ENSBTAP00000043214; -.
DR   PaxDb; P35816; -.
DR   PeptideAtlas; P35816; -.
DR   PRIDE; P35816; -.
DR   Ensembl; ENSBTAT00000000233; ENSBTAP00000000233; ENSBTAG00000000199.
DR   GeneID; 280891; -.
DR   KEGG; bta:280891; -.
DR   CTD; 54704; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000199; -.
DR   VGNC; VGNC:32713; PDP1.
DR   eggNOG; KOG0700; Eukaryota.
DR   GeneTree; ENSGT00940000156368; -.
DR   HOGENOM; CLU_021928_0_0_1; -.
DR   InParanoid; P35816; -.
DR   OrthoDB; 461546at2759; -.
DR   BRENDA; 3.1.3.43; 908.
DR   EvolutionaryTrace; P35816; -.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000000199; Expressed in occipital lobe and 103 other tissues.
DR   ExpressionAtlas; P35816; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004741; F:[pyruvate dehydrogenase (lipoamide)] phosphatase activity; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0016311; P:dephosphorylation; TAS:UniProtKB.
DR   GO; GO:1904184; P:positive regulation of pyruvate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   PANTHER; PTHR13832; PTHR13832; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; SSF81606; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Calcium; Direct protein sequencing; Hydrolase;
KW   Magnesium; Metal-binding; Mitochondrion; Protein phosphatase;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..71
FT                   /note="Mitochondrion"
FT   CHAIN           72..538
FT                   /note="[Pyruvate dehydrogenase [acetyl-transferring]]-
FT                   phosphatase 1, mitochondrial"
FT                   /id="PRO_0000025418"
FT   DOMAIN          109..525
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         144
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         418
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         516
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         202
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P0J1"
FT   HELIX           82..89
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:3MQ3"
FT   STRAND          94..97
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          107..117
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          119..122
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          125..135
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          138..149
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           150..166
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           170..182
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           205..222
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           232..253
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           258..269
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          270..272
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          274..280
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          283..291
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          293..299
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          305..309
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           319..327
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           331..333
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   TURN            334..336
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          337..339
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   TURN            344..346
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          347..351
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           356..358
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           362..369
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          400..405
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          410..416
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           418..421
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           426..437
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           478..487
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          490..492
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           499..504
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           508..514
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   STRAND          518..525
FT                   /evidence="ECO:0007829|PDB:6V0T"
FT   HELIX           527..533
FT                   /evidence="ECO:0007829|PDB:6V0T"
SQ   SEQUENCE   538 AA;  61184 MW;  1A1C219AD8C3DAE3 CRC64;
     MPAPTQLFFP LIRNCELSRI YGTACYCHHK HLCCSPPYIP QSRPRYTPHP AYATFYRPKE
     SWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE FDGKNVSSVL GFDSNQLPAN
     APIEDRRSAA TCLQTRGMLL GVFDGHAGCA CSQAVSERLF YYIAVSLLPH ETLLEIENAV
     ESGRALLPIL QWHKHPNDYF SKEASKLYFN SLRTYWQELI DLNTGESTDI DVKEALINAF
     KRLDNDISLE AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE
     EDGSWSAVTL SNDHNAQNER EVERLKLEHP KNEAKSVVKQ DRLLGLLMPF RAFGDVKFKW
     SIDLQKRVIE SGPDQLNDNE YTKFIPPNYY TPPYLTAEPE VTYHRLRPQD KFLVLATDGL
     WETMHRQDVV RIVGEYLTGM HHQQPIAVGG YKVTLGQMHG LLTERRAKMS SVFEDQNAAT
     HLIRHAVGNN EFGAVDHERL SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQEQ
 
 
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