Primary Information |
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| BoMiProt ID | Bomi7437 |
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| Protein Name | Neuroendocrine convertase 1(NEC 1)/Prohormone convertase 1/Prohormone convertase 1(PC1) |
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| Organism | Bos taurus |
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| Uniprot ID | Q9GLR1 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_776837.1 |
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| Aminoacid Length | 753 |
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| Molecular Weight | 83807 |
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| FASTA Sequence |
Download |
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| Gene Name | PCSK1 |
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| Gene ID | 281967 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| 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. |
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| 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. |
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| PTMs | glycosylation on Asn |
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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
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| Predicted Disorder Regions | 186-201, 276-281, 355-373, 597-692, 714-721 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Glycosylation is also required for proper activation |
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| 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. |
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| 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. |
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