PDPR_BOVIN
ID PDPR_BOVIN Reviewed; 878 AA.
AC O46504;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial;
DE Short=PDPr;
DE Flags: Precursor;
GN Name=PDPR;
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], PROTEIN SEQUENCE OF 32-45; 216-229; 350-362;
RP 370-377; 385-399; 419-442; 445-474; 490-497 AND 656-665, AND 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).
RN [2]
RP FUNCTION.
RX PubMed=8643510; DOI=10.1073/pnas.93.10.4953;
RA Yan J., Lawson J.E., Reed L.J.;
RT "Role of the regulatory subunit of bovine pyruvate dehydrogenase
RT phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4953-4956(1996).
CC -!- FUNCTION: Decreases the sensitivity of PDP1 to magnesium ions, and this
CC inhibition is reversed by the polyamine spermine.
CC {ECO:0000269|PubMed:8643510}.
CC -!- SUBUNIT: Heterodimer of a catalytic (PDP1) and a regulatory (PDPR)
CC subunit. {ECO:0000269|PubMed:9395502}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
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DR EMBL; AF026954; AAC48785.1; -; mRNA.
DR RefSeq; NP_777206.1; NM_174781.2.
DR AlphaFoldDB; O46504; -.
DR SMR; O46504; -.
DR STRING; 9913.ENSBTAP00000021895; -.
DR PaxDb; O46504; -.
DR PRIDE; O46504; -.
DR GeneID; 286844; -.
DR KEGG; bta:286844; -.
DR CTD; 55066; -.
DR eggNOG; KOG2844; Eukaryota.
DR InParanoid; O46504; -.
DR OrthoDB; 137947at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..878
FT /note="Pyruvate dehydrogenase phosphatase regulatory
FT subunit, mitochondrial"
FT /id="PRO_0000328739"
SQ SEQUENCE 878 AA; 98857 MW; A8658C5605164E6D CRC64;
MLPRLLAVVR GPGSCRGWRE GSPARGSASA TVAPPVALPA QAQVVVCGGG IMGTSVAYHL
SKMGWKDVVL LEQGRLAAGS TRFCAGILST ARHLAIEQKM ADYSNKLYHQ LEQETGIQTG
YTRTGSIFLA QTQDRLISLK RINSRLNVIG IPCEIISPKK VAELHPLLNV HDLVGAMHVP
EDAVVSSADV ALALASAASQ SGVQIYDRTS ILHVMVKKGQ VAGVETDKGQ IQCQYFVNCA
GQWAYELGLC SEEPVSIPLH ACEHFYLLTR PWETPLPSST PTVVDADGRI YIRNWQGGIL
SGGFEKNPKP IFTEGKNQLE IQNLQEDWDH FEPLLSSLLR RMPQLETLEI VKLVNCPETF
TPDMRCIMGE SPSVRGYFVL VGMNSAGLSF GGGAGKYLAE WMVYGYPSEN VWELDLKRFG
ALQSSRTFLR HRVMEVMPLL YDLKVPRWDF QTGRQLRTSP LYDRLDAQGA RWMEKHGFER
PKYFIPPDKD LLALEQSKTF YKPDWFEIVE SEVKCCKEAV CVIDMSSFTK FEITSTGDQA
LEILQYLFSN DLDVPVGHIV HTGMLNERGG YENDCSIARL SKRSFFMISP TDQQVHCWAW
LKKYMPEDSN LILEDVTWKY TALNLIGPRT VDVLSELSYA PMTPDHFPSL FCKEMSVGYA
NGIRVMSMTH TGEPGFMLYI PIEYALHVYN EVMSVGQKYG IRNAGYYALR SLRIEKFFAF
WGQDLNTLTT PLECGGESRV KLDKGVDFIG RDALLQQRQN GVYNRLTMFI LDDHDTDLDL
WPWWGEPIYR NGRYVGKTTS SAYGYTLERH VCLGFVHNFS EDTGEEQVVT ADFINRGEYE
IDIAGHRFQA KAKLYPVPSL LTHKRRKEDV ELSDLHGK