Search by BoMiProt ID - Bomi7437


Primary Information

BoMiProt ID Bomi7437
Protein Name Neuroendocrine convertase 1(NEC 1)/Prohormone convertase 1/Prohormone convertase 1(PC1)
Organism Bos taurus
Uniprot IdQ9GLR1
Milk FractionWhey
Ref Sequence Id NP_776837.1
Aminoacid Length 753
Molecular Weight 83807
Fasta Sequence https://www.uniprot.org/uniprot/Q9GLR1.fasta
Gene Name PCSK1
Gene Id 281967
Protein Existence Status reviewed

Secondary Information

Protein Function serine endoprotease is involved in the processing of a variety of proneuropeptides and prohormones.PC1/3 recognizes and cleaves precursor proteins C-terminally to a pair of basic residues. PC1/3 prefers to cleave after a Lys-Arg dibasic site, but it is also able to cleave other dibasic sites including Arg-Arg, Arg-Lys, and Arg-X-X-Arg (where X is any amino acid), or even after a single Arg residue.
Biochemical Properties catalyze proteolytic cleavage C-terminally to basic residue motifs.composed of three common domain structures, a prodomain(P domain), a catalytic domain, and a P domain (also called homo B or middle domain), and a unique C-terminal region, which can be composed of several subdomains.The catalytic domain includes the catalytic triad Asp167-His208-Ser382. The P domain contributes to calcium and pH requirements and to enzyme stability, whereas the C-terminal regions are important for intracellular trafficking and subcellular localization. RRGD motif present in the P domain is critical for proper proPC1/3 processing and further sorting to the secretory granules.
PTMs glycosylation on Asn
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q9GLR1|NEC1_BOVIN Neuroendocrine convertase 1 OS=Bos taurus OX=9913 GN=PCSK1 PE=2 SV=1 MGRRAWTLQCTAFSLFCAWCAMNSVKAKKQFVNEWAAEIPGGPEAASAIAQELGYDLLGQ IGSLENHYLFKHRNHPRRSRRSALHITKRLSDDDRVIWAEQQYEKERSKRSVLRDSALDL FNDPMWNQQWYLQDTRMTATLPKLDLHVIPVWQKGITGKGVVITVLDDGLEWN*173HTDIYAN YDPEASYDFNDNDHDPFPRYDLINENKHGTRCAGEIAMQANNHKCGVGVAYNSKVGGIRM LDGIVTDAIEASLIGFNPGHVDIYSASWGPNDDGKTVEGPGRLAQKAFEYGVKQGRQGKG SIFVWASGNGGRQGDNCDCDGYTDSIYTISINSASQQGLSPWYAEKCSSTLATSYSSGDY TDQRITSADLHNDCTETHTGTSASAPLAAGIFALALEANPN*401LTWRDMQHLVVWTSEYDPL ANNPGWKKNGAGLMVNSRFGFGLLNAKALVDLADPSTWSSVPEKKECVVKDNDFEPRALK ANGEVIIEIPTRACEGQENAIKSLEHVQFEATIEYSRRGDLHVTLTSAAGTSTVLLAERE RDTSPNGFKNWDFMSVHTWGENPIGTWTLRIADMSGRIQNEGRIVTWKLILHGTSSQPEH MKQPRVYTSYNTVQNDRRGVEKVVDSGEEQPTQEGLDENAQASQSPSGSGVGGRRDELAE GAPSEAMLRLLQSAFSKNSPSKQSPKKPPSAKPNIPYENFYEALERLNKPSQLKDSEDSL YNDYVDGFYNTKPYKHRDDRLLQALVDLLREEN
Predicted Disorder Regions 186-201, 276-281, 355-373, 597-692, 714-721
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Glycosylation is also required for proper activation
Additional Comments  loss-of-function mutations in PCSK1 exhibit a variable and pleiotropic syndrome consisting of some or all of the following: obesity, malabsorptive diarrhea, hypogonadotropic hypogonadism, altered thyroid and adrenal function, and impaired regulation of plasma glucose levels in association with elevated circulating proinsulin-to-insulin ratio.
Bibliography Stijnen P, Ramos-Molina B, O'Rahilly S, Creemers JW. PCSK1 Mutations and Human Endocrinopathies: From Obesity to Gastrointestinal Disorders. Endocr Rev. 2016 Aug;37(4):347-71. doi: 10.1210/er.2015-1117. Epub 2016 May 17. PMID: 27187081.