| Tag | Content |
|---|
| CPLM ID | CPLM-014701 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Carbonic anhydrase 5B, mitochondrial |
Protein Synonyms/Alias | Carbonate dehydratase VB; Carbonic anhydrase VB; CA-VB |
Gene Name | Ca5b |
Gene Synonyms/Alias | Car5b |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 195 | KHHKELQKLVDTLPS | acetylation | [1] | | 249 | SVTWIIKKQPVEVDH | 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 | Reversible hydration of carbon dioxide. |
Sequence Annotation | REGION 235 236 Substrate binding (By similarity).
METAL 130 130 Zinc; catalytic (By similarity).
METAL 132 132 Zinc; catalytic (By similarity).
METAL 155 155 Zinc; catalytic (By similarity). |
Keyword | Complete proteome; Lyase; Metal-binding; Mitochondrion; Reference proteome; Transit peptide; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 317 AA |
Protein Sequence | MTVMSHLRVS LQVSSCTLLW RRFRVPRLVP LRSCSLYTCT YRTRNRALPP LWENLDLVPA 60
GDRQSPINIR WRDSVYDPGL KPLTISYDPA TCLHIWNNGY SFLVEFEDTT DKSVIEGGPL 120
EHNYRLKQFH FHWGAIDAWG SEHTVDSKCY PAELHLVHWN AVKFESFEDA ALEENGLAVI 180
GVFLKLGKHH KELQKLVDTL PSIKHKDTLV KFGSFDPSCL MPTCPDYWTY SGSLTTPPLS 240
ESVTWIIKKQ PVEVDHDQLE QFRTLLFTSE GEKEKRMVDN FRPLQPLMNR TVRSSFRHDY 300
VLNIQVKPEP TASEVSP 317 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. GO:0004089; F:carbonate dehydratase activity; IEA:EC. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006730; P:one-carbon metabolic process; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |