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Database: UniProt
Entry: Q91ZA3
LinkDB: Q91ZA3
Original site: Q91ZA3 
ID   PCCA_MOUSE              Reviewed;         724 AA.
AC   Q91ZA3; Q80VU5; Q922N3;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 2.
DT   03-SEP-2014, entry version 102.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   PubMed=11461925; DOI=10.1074/jbc.M105467200;
RA   Miyazaki T., Ohura T., Kobayashi M., Shigematsu Y., Yamaguchi S.,
RA   Suzuki Y., Hata I., Aoki Y., Yang X., Minjares C., Haruta I., Uto H.,
RA   Ito Y., Muller U.;
RT   "Fatal propionic acidemia in mice lacking propionyl-CoA carboxylase
RT   and its rescue by postnatal, liver-specific supplementation via a
RT   transgene.";
RL   J. Biol. Chem. 276:35995-35999(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Embryo, and Mammary tumor;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-115; LYS-146;
RP   LYS-184; LYS-196; LYS-258; LYS-324; LYS-381; LYS-403; LYS-498;
RP   LYS-509; LYS-554 AND LYS-644, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-146; LYS-150;
RP   LYS-196; LYS-324 AND LYS-492, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- CATALYTIC ACTIVITY: ATP + propanoyl-CoA + HCO(3)(-) = ADP +
CC       phosphate + (S)-methylmalonyl-CoA.
CC   -!- COFACTOR: Biotin.
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- DISEASE: Note=Propionic acidemia due to recessively inherited
CC       deficiency of PCCase activity often causes life-threatening
CC       ketosis and acidosis.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC   -!- SIMILARITY: Contains 1 biotin carboxylation domain.
CC   -!- SIMILARITY: Contains 1 biotinyl-binding domain.
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DR   EMBL; AY046947; AAL02364.1; -; mRNA.
DR   EMBL; BC006915; AAH06915.1; -; mRNA.
DR   EMBL; BC049802; AAH49802.1; -; mRNA.
DR   CCDS; CCDS27350.1; -.
DR   RefSeq; NP_659093.2; NM_144844.2.
DR   UniGene; Mm.23876; -.
DR   ProteinModelPortal; Q91ZA3; -.
DR   SMR; Q91ZA3; 59-724.
DR   IntAct; Q91ZA3; 4.
DR   MINT; MINT-1844797; -.
DR   PhosphoSite; Q91ZA3; -.
DR   REPRODUCTION-2DPAGE; Q91ZA3; -.
DR   MaxQB; Q91ZA3; -.
DR   PaxDb; Q91ZA3; -.
DR   PRIDE; Q91ZA3; -.
DR   Ensembl; ENSMUST00000038374; ENSMUSP00000038763; ENSMUSG00000041650.
DR   GeneID; 110821; -.
DR   KEGG; mmu:110821; -.
DR   UCSC; uc007vbe.2; mouse.
DR   CTD; 5095; -.
DR   MGI; MGI:97499; Pcca.
DR   eggNOG; COG4770; -.
DR   GeneTree; ENSGT00550000074675; -.
DR   HOGENOM; HOG000008989; -.
DR   HOVERGEN; HBG000555; -.
DR   InParanoid; Q91ZA3; -.
DR   KO; K01965; -.
DR   OMA; HTVVASN; -.
DR   OrthoDB; EOG7RZ5PH; -.
DR   PhylomeDB; Q91ZA3; -.
DR   TreeFam; TF354220; -.
DR   Reactome; REACT_189100; Defective HLCS causes multiple carboxylase deficiency.
DR   Reactome; REACT_206176; Biotin transport and metabolism.
DR   UniPathway; UPA00945; UER00908.
DR   ChiTaRS; PCCA; mouse.
DR   NextBio; 364725; -.
DR   PRO; PR:Q91ZA3; -.
DR   ArrayExpress; Q91ZA3; -.
DR   Bgee; Q91ZA3; -.
DR   Genevestigator; Q91ZA3; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004658; F:propionyl-CoA carboxylase activity; IMP:MGI.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF00289; CPSase_L_chain; 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; Ligase;
KW   Mitochondrion; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     48       Mitochondrion (By similarity).
FT   CHAIN        49    724       Propionyl-CoA carboxylase alpha chain,
FT                                mitochondrial.
FT                                /FTId=PRO_0000002838.
FT   DOMAIN       58    505       Biotin carboxylation.
FT   DOMAIN      177    374       ATP-grasp.
FT   DOMAIN      656    723       Biotinyl-binding.
FT   ACT_SITE    349    349       By similarity.
FT   BINDING     173    173       ATP (By similarity).
FT   BINDING     257    257       ATP (By similarity).
FT   BINDING     292    292       ATP (By similarity).
FT   MOD_RES      61     61       N6-acetyllysine; alternate.
FT   MOD_RES      61     61       N6-succinyllysine; alternate.
FT   MOD_RES     115    115       N6-succinyllysine.
FT   MOD_RES     146    146       N6-acetyllysine; alternate.
FT   MOD_RES     146    146       N6-succinyllysine; alternate.
FT   MOD_RES     150    150       N6-acetyllysine.
FT   MOD_RES     184    184       N6-succinyllysine.
FT   MOD_RES     196    196       N6-acetyllysine; alternate.
FT   MOD_RES     196    196       N6-succinyllysine; alternate.
FT   MOD_RES     248    248       Phosphoserine.
FT   MOD_RES     258    258       N6-succinyllysine.
FT   MOD_RES     324    324       N6-acetyllysine; alternate.
FT   MOD_RES     324    324       N6-succinyllysine; alternate.
FT   MOD_RES     381    381       N6-succinyllysine.
FT   MOD_RES     403    403       N6-succinyllysine.
FT   MOD_RES     492    492       N6-acetyllysine.
FT   MOD_RES     498    498       N6-succinyllysine.
FT   MOD_RES     509    509       N6-succinyllysine.
FT   MOD_RES     554    554       N6-succinyllysine.
FT   MOD_RES     644    644       N6-succinyllysine.
FT   MOD_RES     690    690       N6-biotinyllysine (By similarity).
FT   CONFLICT    497    497       T -> A (in Ref. 1; AAL02364).
FT   CONFLICT    542    542       H -> R (in Ref. 2; AAH06915).
FT   CONFLICT    555    561       WELSVKL -> VGALGKV (in Ref. 1; AAL02364).
SQ   SEQUENCE   724 AA;  79922 MW;  249189EDF9F99274 CRC64;
     MAGQWVRTVA LLAARRHWRR SSQQQLLGTL KHAPVYSYQC LVVSRSLSSV EYEPKEKTFD
     KILIANRGEI ACRVIKTCKK MGIKTVAIHS DVDASSVHVK MADEAVCVGP APTSKSYLNM
     DAIMEAIKKT RAQAVHPGYG FLSENKEFAK RLAAEDVTFI GPDTHAIQAM GDKIESKLLA
     KRAKVNTIPG FDGVVKDADE AVRIAREIGY PVMIKASAGG GGKGMRIAWD DEETRDGFRF
     SSQEAASSFG DDRLLIEKFI DNPRHIEIQV LGDKHGNALW LNERECSIQR RNQKVVEEAP
     SIFLDPETRQ AMGEQAVALA KAVKYSSAGT VEFLVDSQKN FYFLEMNTRL QVEHPVTECI
     TGLDLVQEMI LVAKGYPLRH KQEDIPISGW AVECRVYAED PYKSFGLPSI GRLSQYQEPI
     HLPGVRVDSG IQPGSDISIY YDPMISKLVT YGSDRAEALK RMEDALDNYV IRGVTHNIPL
     LREVIINTRF VKGDISTKFL SDVYPDGFKG HTLTLSERNQ LLAIASSVFV ASQLRAQRFQ
     EHSRVPVIRP DVAKWELSVK LHDEDHTVVA SNNGPAFTVE VDGSKLNVTS TWNLASPLLS
     VNVDGTQRTV QCLSREAGGN MSIQFLGTVY KVHILTKLAA ELNKFMLEKV PKDTSSTLCS
     PMPGVVVAVS VKPGDMVAEG QEICVIEAMK MQNSMTAGKM GKVKLVHCKA GDTVGEGDLL
     VELE
//
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