Tag | Content |
---|
CPLM ID | CPLM-009721 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Neuroendocrine convertase 1 |
Protein Synonyms/Alias | NEC 1; Furin homolog; PC3; Prohormone convertase 1; Propeptide-processing protease; Proprotein convertase 1; PC1 |
Gene Name | Pcsk1 |
Gene Synonyms/Alias | Att-1; Nec-1; Nec1 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
---|
622 | NDRRGVEKMVNVVEK | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin and insulin. |
Sequence Annotation | REGION 122 410 Catalytic. REGION 739 751 Amphipathic (Potential). ACT_SITE 167 167 Charge relay system (By similarity). ACT_SITE 208 208 Charge relay system (By similarity). ACT_SITE 382 382 Charge relay system (By similarity). CARBOHYD 401 401 N-linked (GlcNAc...) (Potential). CARBOHYD 645 645 N-linked (GlcNAc...) (Potential). DISULFID 225 374 By similarity. DISULFID 317 347 By similarity. DISULFID 467 494 By similarity. |
Keyword | 3D-structure; Calcium; Cleavage on pair of basic residues; Complete proteome; Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome; Serine protease; Signal; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 753 AA |
Protein Sequence | MEQRGWTLQC TAFAFFCVWC ALNSVKAKRQ FVNEWAAEIP GGQEAASAIA EELGYDLLGQ 60 IGSLENHYLF KHKSHPRRSR RSALHITKRL SDDDRVTWAE QQYEKERSKR SVQKDSALDL 120 FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP VWEKGITGKG VVITVLDDGL EWNHTDIYAN 180 YDPEASYDFN DNDHDPFPRY DLTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM 240 LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG 300 SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY 360 TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL 420 ASNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRTWRN VPEKKECVVK DNNFEPRALK 480 ANGEVIVEIP TRACEGQENA IKSLEHVQFE ATIEYSRRGD LHVTLTSAVG TSTVLLAERE 540 RDTSPNGFKN WDFMSVHTWG ENPVGTWTLK ITDMSGRMQN EGRIVNWKLI LHGTSSQPEH 600 MKQPRVYTSY NTVQNDRRGV EKMVNVVEKR PTQKSLNGNL LVPKNSSSSN VEGRRDEQVQ 660 GTPSKAMLRL LQSAFSKNAL SKQSPKKSPS AKLSIPYESF YEALEKLNKP SKLEGSEDSL 720 YSDYVDVFYN TKPYKHRDDR LLQALMDILN EEN 753 |
Gene Ontology | GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. GO:0005615; C:extracellular space; IDA:BHF-UCL. GO:0005794; C:Golgi apparatus; IBA:RefGenome. GO:0034774; C:secretory granule lumen; TAS:Reactome. GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell. GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL. GO:0043043; P:peptide biosynthetic process; IDA:BHF-UCL. GO:0016486; P:peptide hormone processing; IDA:BHF-UCL. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |