| Tag | Content |
|---|
| CPLM ID | CPLM-017418 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Carboxypeptidase A6 |
Protein Synonyms/Alias | Carboxypeptidase B |
Gene Name | CPA6 |
Gene Synonyms/Alias | CPAH |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 388 | SSMDWAYKNGIPYAF | ubiquitination | [1] |
|
Reference | [1] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] |
Functional Description | May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II. |
Sequence Annotation | REGION 196 199 Substrate binding (By similarity).
REGION 271 272 Substrate binding (By similarity).
REGION 325 326 Substrate binding (By similarity).
ACT_SITE 398 398 Nucleophile (By similarity).
METAL 196 196 Zinc; catalytic (By similarity).
METAL 199 199 Zinc; catalytic (By similarity).
METAL 324 324 Zinc; catalytic (By similarity).
BINDING 254 254 Substrate (By similarity).
CARBOHYD 89 89 N-linked (GlcNAc...) (Potential).
CARBOHYD 153 153 N-linked (GlcNAc...) (Potential).
CARBOHYD 427 427 N-linked (GlcNAc...) (Potential).
DISULFID 265 288 By similarity. |
Keyword | Alternative splicing; Carboxypeptidase; Chromosomal rearrangement; Cleavage on pair of basic residues; Complete proteome; Disease mutation; Disulfide bond; Epilepsy; Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism; Protease; Reference proteome; Secreted; Signal; Zinc; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 437 AA |
Protein Sequence | MKCLGKRRGQ AAAFLPLCWL FLKILQPGHS HLYNNRYAGD KVIRFIPKTE EEAYALKKIS 60
YQLKVDLWQP SSISYVSEGT VTDVHIPQNG SRALLAFLQE ANIQYKVLIE DLQKTLEKGS 120
SLHTQRNRRS LSGYNYEVYH SLEEIQNWMH HLNKTHSGLI HMFSIGRSYE GRSLFILKLG 180
RRSRLKRAVW IDCGIHAREW IGPAFCQWFV KEALLTYKSD PAMRKMLNHL YFYIMPVFNV 240
DGYHFSWTND RFWRKTRSRN SRFRCRGVDA NRNWKVKWCD EGASMHPCDD TYCGPFPESE 300
PEVKAVANFL RKHRKHIRAY LSFHAYAQML LYPYSYKYAT IPNFRCVESA AYKAVNALQS 360
VYGVRYRYGP ASTTLYVSSG SSMDWAYKNG IPYAFAFELR DTGYFGFLLP EMLIKPTCTE 420
TMLAVKNITM HLLKKCP 437 |
Gene Ontology | GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. GO:0004181; F:metallocarboxypeptidase activity; NAS:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |