| Tag | Content |
|---|
| CPLM ID | CPLM-004270 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Propionyl-CoA carboxylase alpha chain, mitochondrial |
Protein Synonyms/Alias | PCCase subunit alpha; Propanoyl-CoA:carbon dioxide ligase subunit alpha |
Gene Name | Pcca |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 209 | PGFDGVLKDADEAVR | acetylation | [1] | | 657 | KLAAELNKFMLEKVP | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | |
Sequence Annotation | DOMAIN 71 518 Biotin carboxylation.
DOMAIN 190 387 ATP-grasp.
DOMAIN 669 736 Biotinyl-binding.
ACT_SITE 362 362 By similarity.
BINDING 186 186 ATP (By similarity).
BINDING 270 270 ATP (By similarity).
BINDING 305 305 ATP (By similarity).
MOD_RES 703 703 N6-biotinyllysine (By similarity). |
Keyword | ATP-binding; Biotin; Complete proteome; Direct protein sequencing; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 737 AA |
Protein Sequence | MAGLWVRTVA LLAARRHWRR SSQQLLWTLK RAPRSSQQLL WTLKRAPVYS QQCLVVSRSL 60
SSVEYEPKEK TFDKILIANR GEIACRVIKT CRKMGIRTVA IHSDVDASSV HVKMADEAVC 120
VGPAPTSKSY LNMDAIMEAI KKTGAQAVHP GYGFLSENKE FAKCLAAEDV TFIGPDTHAI 180
QAMGDKIESK LLAKRAKVNT IPGFDGVLKD ADEAVRIARE IGYPVMIKAS AGGGGKGMRI 240
PWDDEETRDG FRFSSQEAAS SFGDDRLLIE KFIDNPRHIE IQVLGDKHGN ALWLNERECS 300
IQRRNQKVVE EAPSIFLDPE TRRAMGEQAV AWPKAVKYSS AGTVEFLVDS QKNFYFLEMN 360
TRLQVEHPVT ECITGLDLVQ EMILVAKGYP LRHKQEDIPI SGWAVECRVY AEDPYKSFGL 420
PSIGRLSQYQ EPIHLPGVRV DSGIQPGSDI SIYHDPMISK LVTYGSDRAE ALKRMEDALD 480
SYVIRGVTHN IPLLREVIIN TRFVKGDIST KFLSDVYPDG FKGHMLTPSE RDQLLAIASS 540
LFVASQLRAQ RFQEHSRVPV IRPDVAKWEL SVKLHDEDHT VVASNNGPTF NVEVDGSKLN 600
VTSTWNLASP LLSVNVDGTQ RTVQCLSPDA GGNMSIQFLG TVYKVHILTK LAAELNKFML 660
EKVPKDTSSV LRSPKPGVVV AVSVKPGDMV AEGQEICVIE AMKMQNSMTA GKMGKVKLVH 720
CKAGDTVGEG DLLVELE 737 |
Gene Ontology | GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. GO:0005739; C:mitochondrion; IDA:RGD. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004075; F:biotin carboxylase activity; IEA:InterPro. GO:0046872; F:metal ion binding; IEA:InterPro. GO:0004658; F:propionyl-CoA carboxylase activity; TAS:RGD. GO:0009063; P:cellular amino acid catabolic process; TAS:RGD. GO:0009062; P:fatty acid catabolic process; TAS:RGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |