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PYC_RAT
ID   PYC_RAT                 Reviewed;        1178 AA.
AC   P52873; Q5RKM0; Q64555;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 182.
DE   RecName: Full=Pyruvate carboxylase, mitochondrial;
DE            EC=6.4.1.1 {ECO:0000250|UniProtKB:P11498};
DE   AltName: Full=Pyruvic carboxylase;
DE            Short=PCB;
DE   Flags: Precursor;
GN   Name=Pc;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8522203; DOI=10.1016/0378-1119(95)00557-m;
RA   Lehn D.A., Moran S.M., Macdonald M.J.;
RT   "The sequence of the rat pyruvate carboxylase-encoding cDNA.";
RL   Gene 165:331-332(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Liver;
RX   PubMed=8687410; DOI=10.1042/bj3160631;
RA   Jitrapakdee S., Booker G.W., Cassady A.I., Wallace J.C.;
RT   "Cloning, sequencing and expression of rat liver pyruvate carboxylase.";
RL   Biochem. J. 316:631-637(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [4]
RP   PROTEIN SEQUENCE OF 21-35; 1134-1137 AND 1139-1158.
RC   TISSUE=Liver;
RX   PubMed=3178228; DOI=10.1016/0003-9861(88)90258-5;
RA   Thampy K.G., Huang W.Y., Wakil S.J.;
RT   "A rapid purification method for rat liver pyruvate carboxylase and amino
RT   acid sequence analyses of NH2-terminal and biotin peptide.";
RL   Arch. Biochem. Biophys. 266:270-276(1988).
RN   [5]
RP   PROTEIN SEQUENCE OF 244-263; 329-355; 407-428 AND 943-964, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (DEC-2006) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1003, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving
CC       the ATP-dependent carboxylation of the covalently attached biotin in
CC       the first step and the transfer of the carboxyl group to pyruvate in
CC       the second. Catalyzes in a tissue specific manner, the initial
CC       reactions of glucose (liver, kidney) and lipid (adipose tissue, liver,
CC       brain) synthesis from pyruvate. {ECO:0000250|UniProtKB:P11498}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC         + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1;
CC         Evidence={ECO:0000250|UniProtKB:P11498};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20845;
CC         Evidence={ECO:0000250|UniProtKB:P11498};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000250|UniProtKB:P11498};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P11498};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:P11498};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000250|UniProtKB:P11498}.
CC   -!- SUBUNIT: Homotetramer. Interacts (via the biotin carboxylation domain)
CC       with SIRT4. {ECO:0000250|UniProtKB:P11498}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P11498}.
CC   -!- PTM: Acetylation of Lys-748 might play a role in catalytic activity
CC       regulation. {ECO:0000250|UniProtKB:Q05920}.
CC   -!- MISCELLANEOUS: This enzyme performs an important anaplerotic function
CC       in replenishing citric acid cycle intermediates that exit the
CC       mitochondrion for consumption in various pathways.
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DR   EMBL; U32314; AAA96256.1; -; mRNA.
DR   EMBL; U36585; AAC52668.1; -; mRNA.
DR   EMBL; BC085680; AAH85680.1; -; mRNA.
DR   PIR; S68252; JC4391.
DR   RefSeq; NP_036876.2; NM_012744.2.
DR   RefSeq; XP_006230754.1; XM_006230692.3.
DR   RefSeq; XP_006230755.1; XM_006230693.2.
DR   RefSeq; XP_006230756.1; XM_006230694.3.
DR   AlphaFoldDB; P52873; -.
DR   SMR; P52873; -.
DR   BioGRID; 247176; 6.
DR   IntAct; P52873; 3.
DR   MINT; P52873; -.
DR   STRING; 10116.ENSRNOP00000026316; -.
DR   CarbonylDB; P52873; -.
DR   iPTMnet; P52873; -.
DR   PhosphoSitePlus; P52873; -.
DR   World-2DPAGE; 0004:P52873; -.
DR   jPOST; P52873; -.
DR   PaxDb; P52873; -.
DR   PRIDE; P52873; -.
DR   GeneID; 25104; -.
DR   KEGG; rno:25104; -.
DR   UCSC; RGD:3262; rat.
DR   CTD; 5091; -.
DR   RGD; 3262; Pc.
DR   VEuPathDB; HostDB:ENSRNOG00000019372; -.
DR   eggNOG; KOG0369; Eukaryota.
DR   HOGENOM; CLU_000395_1_0_1; -.
DR   InParanoid; P52873; -.
DR   PhylomeDB; P52873; -.
DR   TreeFam; TF300535; -.
DR   BRENDA; 6.4.1.1; 5301.
DR   Reactome; R-RNO-196780; Biotin transport and metabolism.
DR   Reactome; R-RNO-70263; Gluconeogenesis.
DR   UniPathway; UPA00138; -.
DR   PRO; PR:P52873; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000019372; Expressed in adult mammalian kidney and 19 other tissues.
DR   ExpressionAtlas; P52873; baseline and differential.
DR   Genevisible; P52873; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0009374; F:biotin binding; IDA:RGD.
DR   GO; GO:0031406; F:carboxylic acid binding; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IDA:RGD.
DR   GO; GO:0006094; P:gluconeogenesis; IDA:RGD.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IDA:RGD.
DR   GO; GO:0044794; P:positive regulation by host of viral process; ISO:RGD.
DR   GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IMP:CACAO.
DR   GO; GO:0006090; P:pyruvate metabolic process; IDA:RGD.
DR   GO; GO:0019076; P:viral release from host cell; ISO:RGD.
DR   GO; GO:0019074; P:viral RNA genome packaging; ISO:RGD.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01235; pyruv_carbox; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Biotin; Direct protein sequencing;
KW   Gluconeogenesis; Ligase; Lipid biosynthesis; Lipid metabolism; Manganese;
KW   Metal-binding; Mitochondrion; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein; Pyruvate; Reference proteome; Transit peptide.
FT   TRANSIT         1..20
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1178
FT                   /note="Pyruvate carboxylase, mitochondrial"
FT                   /id="PRO_0000002842"
FT   DOMAIN          36..486
FT                   /note="Biotin carboxylation"
FT   DOMAIN          156..353
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          563..832
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   DOMAIN          1109..1178
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         571..575
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         572
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         644
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         741
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         771
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         773
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         908
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         35
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         39
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         79
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         148
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         152
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         241
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         297
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         316
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         319
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         434
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         442
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         589
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         661
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         717
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         741
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         748
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         892
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         969
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         988
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         988
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         992
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         1003
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1061
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         1090
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11498"
FT   MOD_RES         1124
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05920"
FT   MOD_RES         1144
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
FT   CONFLICT        21..22
FT                   /note="TA -> SG (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26..27
FT                   /note="SP -> PL (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30..31
FT                   /note="RR -> LL (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        35
FT                   /note="K -> P (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="S -> P (in Ref. 1; AAA96256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        866
FT                   /note="I -> D (in Ref. 1; AAA96256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        977
FT                   /note="R -> G (in Ref. 1; AAA96256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1135
FT                   /note="Q -> A (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1153
FT                   /note="M -> T (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1178 AA;  129777 MW;  782CDFEF3380DB2D CRC64;
     MLKFQTVRGG LRLLGVRRSS TAPVASPNVR RLEYKPIKKV MVANRGEIAI RVFRACTELG
     IRTVAVYSEQ DTGQMHRQKA DEAYLIGRGL APVQAYLHIP DIIKVAKENG VDAVHPGYGF
     LSERADFAQA CQDAGVRFIG PSPEVVRKMG DKVEARAIAI AAGVPVVPGT NSPINSLHEA
     HEFSNTYGFP IIFKAAYGGG GRGMRVVHSY EELEENYTRA YSEALAAFGN GALFVEKFIE
     KPRHIEVQIL GDQYGNILHL YERDCSIQRR HQKVVEIAPA THLDPQLRSR LTSDSVKLAK
     QVGYENAGTV EFLVDKHGKH YFIEVNSRLQ VEHTVTEEIT DVDLVHAQIH VSEGRSLPDL
     GLRQENIRIN GCAIQCRVTT EDPARSFQPD TGRIEVFRSG EGMGIRLDNA SAFQGAVISP
     HYDSLLVKVI AHGKDHPTAA TKMSRALAEF RVRGVKTNIP FLQNVLNNQQ FLAGIVDTQF
     IDENPELFQL RPAQNRAQKL LHYLGHVMVN GPTTPIPVKV SPSPVDPIVP VVPIGPPPAG
     FRDILLREGP EGFARAVRNH QGLLLMDTTF RDAHQSLLAT RVRTHDLKKI APYVAHNFNN
     LFSIENWGGA TFDVAMRFLY ECPWRRLQEL RELIPNIPFQ MLLRGANAVG YTNYPDNVVF
     KFCEVAKENG MDVFRIFDSL NYLPNMLLGM EAAGSAGGVV EAAISYTGDV ADPSRTKYSL
     EYYMGLAEEL VRAGTHILCI KDMAGLLKPA ACTMLVSSLR DRFPDLPLHI HTHDTSGSGV
     AAMLACAQAG ADVVDVAVDS MSGMTSQPSM GALVACTKGT PLDTEVPLER VFDYSEYWEG
     ARGLYAAFDC TATMKSGNSD VYENEIPGGQ YTNLHFQAHS MGLGSKFKEV KKAYVEANQM
     LGDLIKVTPS SKIVGDLAQF MVQNGLSRAE AEAQAEELSF PRSVVEFLQG YIGIPHGGFP
     EPFRSKVLKD LPRIEGRPGA SLPPLNLKEL EKDLIDRHGE EVTPEDVLSA AMYPDVFAQF
     KDFTATFGPL DSLNTRLFLQ GPKIAEEFEV ELERGKTLHI KALAVSDLNR AGQRQVFFEL
     NGQLRSILVK DTQAMKEMHF HPKALKDVKG QIGAPMPGKV IDVKVAAGAK VVKGQPLCVL
     SAMKMETVVT SPMEGTIRKV HVTKDMTLEG DDLILEIE
 
 
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