LOCUS NP_001035806 1178 aa linear PRI 04-DEC-2023
DEFINITION pyruvate carboxylase, mitochondrial precursor [Homo sapiens].
ACCESSION NP_001035806
VERSION NP_001035806.1
DBSOURCE REFSEQ: accession NM_001040716.2
KEYWORDS RefSeq; MANE Select.
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 1178)
AUTHORS Maryami F, Rismani E, Davoudi-Dehaghani E, Khalesi N, Talebi S,
Mahdian R and Zeinali S.
TITLE In silico Analysis of Two Novel Variants in the Pyruvate
Carboxylase (PC) Gene Associated with the Severe Form of PC
Deficiency
JOURNAL Iran Biomed J 27 (5), 307-319 (2023)
PUBMED 37873728
REMARK GeneRIF: In silico Analysis of Two Novel Variants in the Pyruvate
Carboxylase (PC) Gene Associated with the Severe Form of PC
Deficiency.
REFERENCE 2 (residues 1 to 1178)
AUTHORS Wang C, Zhao D, Shu X, Wang K, Wang T, Lin X, Zhang D, Xia T, Qian
S, Tang M, Yang W, Hu A and Zhao Q.
TITLE Protective effects of all-trans retinoic acid against gastric
premalignant lesions by repressing exosomal LncHOXA10-pyruvate
carboxylase axis
JOURNAL J Cancer Res Clin Oncol 148 (1), 121-135 (2022)
PUBMED 34632533
REMARK GeneRIF: Protective effects of all-trans retinoic acid against
gastric premalignant lesions by repressing exosomal
LncHOXA10-pyruvate carboxylase axis.
REFERENCE 3 (residues 1 to 1178)
AUTHORS Gondas,E., Hives,M., Kliment,J., Kmetova Sivonova,M., Dobrota,D.
and Murin,R.
TITLE The ubiquitous expression of pyruvate carboxylase among human
prostate tumors
JOURNAL Bratisl Lek Listy 123 (7), 487-490 (2022)
PUBMED 35907054
REMARK GeneRIF: The ubiquitous expression of pyruvate carboxylase among
human prostate tumors.
REFERENCE 4 (residues 1 to 1178)
AUTHORS Schworer S, Pavlova NN, Cimino FV, King B, Cai X, Sizemore GM and
Thompson CB.
TITLE Fibroblast pyruvate carboxylase is required for collagen production
in the tumour microenvironment
JOURNAL Nat Metab 3 (11), 1484-1499 (2021)
PUBMED 34764457
REMARK GeneRIF: Fibroblast pyruvate carboxylase is required for collagen
production in the tumour microenvironment.
REFERENCE 5 (residues 1 to 1178)
AUTHORS Igelmann S, Lessard F, Uchenunu O, Bouchard J, Fernandez-Ruiz A,
Rowell MC, Lopes-Paciencia S, Papadopoli D, Fouillen A, Ponce KJ,
Huot G, Mignacca L, Benfdil M, Kalegari P, Wahba HM, Pencik J,
Vuong N, Quenneville J, Guillon J, Bourdeau V, Hulea L, Gagnon E,
Kenner L, Moriggl R, Nanci A, Pollak MN, Omichinski JG, Topisirovic
I and Ferbeyre G.
TITLE A hydride transfer complex reprograms NAD metabolism and bypasses
senescence
JOURNAL Mol Cell 81 (18), 3848-3865 (2021)
PUBMED 34547241
REFERENCE 6 (residues 1 to 1178)
AUTHORS Walker ME, Baker E, Wallace JC and Sutherland GR.
TITLE Assignment of the human pyruvate carboxylase gene (PC) to 11q13.4
by fluorescence in situ hybridisation
JOURNAL Cytogenet Cell Genet 69 (3-4), 187-189 (1995)
PUBMED 7698008
REFERENCE 7 (residues 1 to 1178)
AUTHORS Wang,D. and De Vivo,D.
TITLE Pyruvate Carboxylase Deficiency
JOURNAL (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE, Bean LJH,
Gripp KW and Amemiya A (Eds.);
GENEREVIEWS(R);
(1993)
PUBMED 20301764
REFERENCE 8 (residues 1 to 1178)
AUTHORS Peng L, Hertz L, Huang R, Sonnewald U, Petersen SB, Westergaard N,
Larsson O and Schousboe A.
TITLE Utilization of glutamine and of TCA cycle constituents as
precursors for transmitter glutamate and GABA
JOURNAL Dev Neurosci 15 (3-5), 367-377 (1993)
PUBMED 7805591
REMARK Review article
REFERENCE 9 (residues 1 to 1178)
AUTHORS Lamhonwah,A.M., Quan,F. and Gravel,R.A.
TITLE Sequence homology around the biotin-binding site of human
propionyl-CoA carboxylase and pyruvate carboxylase
JOURNAL Arch Biochem Biophys 254 (2), 631-636 (1987)
PUBMED 3555348
REFERENCE 10 (residues 1 to 1178)
AUTHORS Freytag,S.O. and Collier,K.J.
TITLE Molecular cloning of a cDNA for human pyruvate carboxylase.
Structural relationship to other biotin-containing carboxylases and
regulation of mRNA content in differentiating preadipocytes
JOURNAL J Biol Chem 259 (20), 12831-12837 (1984)
PUBMED 6548474
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from AP003176.2, DA542083.1,
CN267865.1, BC011617.2 and AP000485.5.
This sequence is a reference standard in the RefSeqGene project.
Summary: This gene encodes pyruvate carboxylase, which requires
biotin and ATP to catalyse the carboxylation of pyruvate to
oxaloacetate. The active enzyme is a homotetramer arranged in a
tetrahedron which is located exclusively in the mitochondrial
matrix. Pyruvate carboxylase is involved in gluconeogenesis,
lipogenesis, insulin secretion and synthesis of the
neurotransmitter glutamate. Mutations in this gene have been
associated with pyruvate carboxylase deficiency. Alternatively
spliced transcript variants with different 5' UTRs, but encoding
the same protein, have been found for this gene. [provided by
RefSeq, Jul 2008].
Transcript Variant: This variant (3) also results from the use of a
more distal promoter, however, it contains an additional 5'
non-coding exon, hence has a longer 5' UTR compared to transcript
variant 1. Transcript variants 1-3 encode the same protein.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: SRR1803612.145698.1,
SRR1803617.27410.1 [ECO:0000332]
RNAseq introns :: mixed sample support SAMEA1965299,
SAMEA1966682 [ECO:0006172]
##Evidence-Data-END##
##RefSeq-Attributes-START##
gene product(s) localized to mito. :: reported by MitoCarta
MANE Ensembl match :: ENST00000393960.7/
ENSP00000377532.1
RefSeq Select criteria :: based on conservation,
expression, longest protein
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..1178
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="11"
/map="11q13.2"
Protein 1..1178
/product="pyruvate carboxylase, mitochondrial precursor"
/EC_number="6.4.1.1"
/note="pyruvate carboxylase, mitochondrial; pyruvic
carboxylase"
/calculated_mol_wt=127340
transit_peptide 1..20
/calculated_mol_wt=2312
mat_peptide 21..1178
/product="pyruvate carboxylase, mitochondrial"
/calculated_mol_wt=127340
Region 33..1178
/region_name="PRK12999"
/note="pyruvate carboxylase; Reviewed"
/db_xref="CDD:237263"
Site 35
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 39
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 79
/site_type="acetylation"
/note="N6-acetyllysine, alternate.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 148
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 152
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 241
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 297
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 319
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 434
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 589
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 661
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 717
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 748
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 892
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 969
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 992
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 1003
/site_type="phosphorylation"
/note="Phosphothreonine.
/evidence=ECO:0000250|UniProtKB:P52873; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 1061
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 1090
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0007744|PubMed:19608861; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
Site 1124
/site_type="acetylation"
/note="N6-acetyllysine.
/evidence=ECO:0000250|UniProtKB:Q05920; propagated from
UniProtKB/Swiss-Prot (P11498.2)"
CDS 1..1178
/gene="PC"
/gene_synonym="PCB"
/coded_by="NM_001040716.2:290..3826"
/db_xref="CCDS:CCDS8152.1"
/db_xref="GeneID:5091"
/db_xref="HGNC:HGNC:8636"
/db_xref="MIM:608786"
ORIGIN
1 mlkfrtvhgg lrllgirrts tapaaspnvr rleykpikkv mvanrgeiai rvfractelg
61 irtvaiyseq dtgqmhrqka deayligrgl apvqaylhip diikvakenn vdavhpgygf
121 lseradfaqa cqdagvrfig pspevvrkmg dkvearaiai aagvpvvpgt dapitslhea
181 hefsntygfp iifkaayggg grgmrvvhsy eeleenytra ysealaafgn galfvekfie
241 kprhievqil gdqygnilhl yerdcsiqrr hqkvveiapa ahldpqlrtr ltsdsvklak
301 qvgyenagtv eflvdrhgkh yfievnsrlq vehtvteeit dvdlvhaqih vaegrslpdl
361 glrqenirin gcaiqcrvtt edparsfqpd tgrievfrsg egmgirldna safqgavisp
421 hydsllvkvi ahgkdhptaa tkmsralaef rvrgvktnia flqnvlnnqq flagtvdtqf
481 idenpelfql rpaqnraqkl lhylghvmvn gpttpipvka spsptdpvvp avpigpppag
541 frdillregp egfaravrnh pglllmdttf rdahqsllat rvrthdlkki apyvahnfsk
601 lfsmenwgga tfdvamrfly ecpwrrlqel relipnipfq mllrganavg ytnypdnvvf
661 kfcevakeng mdvfrvfdsl nylpnmllgm eaagsaggvv eaaisytgdv adpsrtkysl
721 qyymglaeel vragthilci kdmagllkpt actmlvsslr drfpdlplhi hthdtsgagv
781 aamlacaqag advvdvaads msgmtsqpsm galvactrgt pldtevpmer vfdyseyweg
841 arglyaafdc tatmksgnsd vyeneipggq ytnlhfqahs mglgskfkev kkayveanqm
901 lgdlikvtps skivgdlaqf mvqnglsrae aeaqaeelsf prsvveflqg yigvphggfp
961 epfrskvlkd lprvegrpga slppldlqal ekelvdrhge evtpedvlsa amypdvfahf
1021 kdftatfgpl dslntrlflq gpkiaeefev elergktlhi kalavsdlnr agqrqvffel
1081 ngqlrsilvk dtqamkemhf hpkalkdvkg qigapmpgkv idikvvagak vakgqplcvl
1141 samkmetvvt spmegtvrkv hvtkdmtleg ddlileie
//
