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Database: UniProt
Entry: P14882
LinkDB: P14882
Original site: P14882 
ID   PCCA_RAT                Reviewed;         737 AA.
AC   P14882;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 3.
DT   16-JAN-2019, entry version 152.
DE   RecName: Full=Propionyl-CoA carboxylase alpha chain, mitochondrial;
DE            Short=PCCase subunit alpha;
DE            EC=6.4.1.3;
DE   AltName: Full=Propanoyl-CoA:carbon dioxide ligase subunit alpha;
DE   Flags: Precursor;
GN   Name=Pcca;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-33.
RC   TISSUE=Uterus;
RX   PubMed=15060005; DOI=10.1101/gr.1932304;
RA   Vitt U., Gietzen D., Stevens K., Wingrove J., Becha S., Bulloch S.,
RA   Burrill J., Chawla N., Chien J., Crawford M., Ison C., Kearney L.,
RA   Kwong M., Park J., Policky J., Weiler M., White R., Xu Y., Daniels S.,
RA   Jacob H., Jensen-Seaman M.I., Lazar J., Stuve L., Schmidt J.;
RT   "Identification of candidate disease genes by EST alignments, synteny,
RT   and expression and verification of Ensembl genes on rat chromosome
RT   1q43-54.";
RL   Genome Res. 14:640-650(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 34-737.
RX   PubMed=2745462;
RA   Browner M.F., Taroni F., Sztul E., Rosenberg L.E.;
RT   "Sequence analysis, biogenesis, and mitochondrial import of the alpha-
RT   subunit of rat liver propionyl-CoA carboxylase.";
RL   J. Biol. Chem. 264:12680-12685(1989).
RN   [3]
RP   SEQUENCE REVISION.
RA   Browner M.F., Taroni F., Sztul E., Rosenberg L.E.;
RL   Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 143-159; 353-387; 426-439; 475-485; 512-522 AND
RP   532-548, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Diao W.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + propanoyl-CoA = (S)-
CC         methylmalonyl-CoA + ADP + H(+) + phosphate;
CC         Xref=Rhea:RHEA:23720, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57327,
CC         ChEBI:CHEBI:57392, ChEBI:CHEBI:456216; EC=6.4.1.3;
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC   -!- PATHWAY: Metabolic intermediate metabolism; propanoyl-CoA
CC       degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
CC   -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing
CC       alpha subunits and six beta subunits (Probable). Interacts (via
CC       the biotin carboxylation domain) with SIRT4. Interacts with SIRT3
CC       and SIRT5 (By similarity). {ECO:0000250|UniProtKB:Q91ZA3,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Acetylated. {ECO:0000250|UniProtKB:Q91ZA3}.
CC   -!- DISEASE: Note=Propionic acidemia due to recessively inherited
CC       deficiency of PCCase activity often causes life-threatening
CC       ketosis and acidosis.
DR   EMBL; CK228512; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M22631; AAA88512.1; ALT_SEQ; mRNA.
DR   PIR; A34337; A34337.
DR   RefSeq; NP_062203.1; NM_019330.1.
DR   UniGene; Rn.6033; -.
DR   ProteinModelPortal; P14882; -.
DR   SMR; P14882; -.
DR   BioGrid; 601858; 1.
DR   iPTMnet; P14882; -.
DR   PhosphoSitePlus; P14882; -.
DR   jPOST; P14882; -.
DR   PRIDE; P14882; -.
DR   GeneID; 687008; -.
DR   KEGG; rno:687008; -.
DR   CTD; 5095; -.
DR   RGD; 3264; Pcca.
DR   HOGENOM; HOG000008989; -.
DR   HOVERGEN; HBG000555; -.
DR   InParanoid; P14882; -.
DR   KO; K01965; -.
DR   OrthoDB; 254436at2759; -.
DR   PhylomeDB; P14882; -.
DR   BioCyc; MetaCyc:MONOMER-8606; -.
DR   BRENDA; 6.4.1.3; 5301.
DR   UniPathway; UPA00945; UER00908.
DR   PRO; PR:P14882; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004658; F:propionyl-CoA carboxylase activity; TAS:RGD.
DR   GO; GO:0009063; P:cellular amino acid catabolic process; TAS:RGD.
DR   GO; GO:0009062; P:fatty acid catabolic process; TAS:RGD.
DR   Gene3D; 3.30.1490.20; -; 1.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
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   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Biotin; Complete proteome;
KW   Direct protein sequencing; Ligase; Mitochondrion; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Transit peptide.
FT   TRANSIT       1     61       Mitochondrion. {ECO:0000250}.
FT   CHAIN        62    737       Propionyl-CoA carboxylase alpha chain,
FT                                mitochondrial.
FT                                /FTId=PRO_0000002839.
FT   DOMAIN       71    518       Biotin carboxylation.
FT   DOMAIN      190    387       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      658    737       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   ACT_SITE    362    362       {ECO:0000250}.
FT   BINDING     186    186       ATP. {ECO:0000250}.
FT   BINDING     270    270       ATP. {ECO:0000250}.
FT   BINDING     305    305       ATP. {ECO:0000250}.
FT   MOD_RES      74     74       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES      74     74       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     128    128       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     159    159       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     159    159       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     163    163       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     197    197       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     209    209       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     209    209       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     261    261       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     271    271       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     337    337       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     337    337       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     394    394       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     416    416       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     505    505       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     511    511       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     522    522       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     567    567       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     657    657       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q91ZA3}.
FT   MOD_RES     703    703       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   737 AA;  81623 MW;  58D13E5033A1D024 CRC64;
     MAGLWVRTVA LLAARRHWRR SSQQLLWTLK RAPRSSQQLL WTLKRAPVYS QQCLVVSRSL
     SSVEYEPKEK TFDKILIANR GEIACRVIKT CRKMGIRTVA IHSDVDASSV HVKMADEAVC
     VGPAPTSKSY LNMDAIMEAI KKTGAQAVHP GYGFLSENKE FAKCLAAEDV TFIGPDTHAI
     QAMGDKIESK LLAKRAKVNT IPGFDGVLKD ADEAVRIARE IGYPVMIKAS AGGGGKGMRI
     PWDDEETRDG FRFSSQEAAS SFGDDRLLIE KFIDNPRHIE IQVLGDKHGN ALWLNERECS
     IQRRNQKVVE EAPSIFLDPE TRRAMGEQAV AWPKAVKYSS AGTVEFLVDS QKNFYFLEMN
     TRLQVEHPVT ECITGLDLVQ EMILVAKGYP LRHKQEDIPI SGWAVECRVY AEDPYKSFGL
     PSIGRLSQYQ EPIHLPGVRV DSGIQPGSDI SIYHDPMISK LVTYGSDRAE ALKRMEDALD
     SYVIRGVTHN IPLLREVIIN TRFVKGDIST KFLSDVYPDG FKGHMLTPSE RDQLLAIASS
     LFVASQLRAQ RFQEHSRVPV IRPDVAKWEL SVKLHDEDHT VVASNNGPTF NVEVDGSKLN
     VTSTWNLASP LLSVNVDGTQ RTVQCLSPDA GGNMSIQFLG TVYKVHILTK LAAELNKFML
     EKVPKDTSSV LRSPKPGVVV AVSVKPGDMV AEGQEICVIE AMKMQNSMTA GKMGKVKLVH
     CKAGDTVGEG DLLVELE
//
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