SERPINB10
| SERPINB10 | |||||||||||||||||||||||||
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| Identifikatori | |||||||||||||||||||||||||
| Aliasi | SERPINB10 | ||||||||||||||||||||||||
| Vanjski ID-jevi | OMIM: 602058 MGI: 2138648 HomoloGene: 68430 GeneCards: SERPINB10 | ||||||||||||||||||||||||
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| Ortolozi | |||||||||||||||||||||||||
| Vrste | Čovjek | Miš | |||||||||||||||||||||||
| Entrez | |||||||||||||||||||||||||
| Ensembl | |||||||||||||||||||||||||
| UniProt | |||||||||||||||||||||||||
| RefSeq (mRNK) | |||||||||||||||||||||||||
| RefSeq (bjelančevina) | |||||||||||||||||||||||||
| Lokacija (UCSC) | Chr 18: 63.9 – 63.94 Mb | Chr 1: 107.46 – 107.48 Mb | |||||||||||||||||||||||
| PubMed pretraga | [3] | [4] | |||||||||||||||||||||||
| Wikipodaci | |||||||||||||||||||||||||
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Član 10 kladusa B inhibitora serpin-peptidaze (ovalbumin) je protein koji je kod ljudi kodiran genom SERPINB10.[5]
Dužina polipeptidnog lanca je 397 aminokiselina, sa molekulksom težinom od 45.403.[6].
Aminokiselinska sekvenca
- Simboli
C: Cistein
D: Asparaginska kiselina
E: Glutaminska kiselina
F: Fenilalanin
G: Glicin
H: Histidin
I: Izoleucin
K: Lizin
L: Leucin
M: Metionin
N: Asparagin
P: Prolin
Q: Glutamin
R: Arginin
S: Serin
T: Treonin
V: Valin
W: Triptofan
Y: Tirozin
| 10 | 20 | 30 | 40 | 50 | ||||
|---|---|---|---|---|---|---|---|---|
| MDSLATSINQ | FALELSKKLA | ESAQGKNIFF | SSWSISTSLT | IVYLGAKGTT | ||||
| AAQMAQVLQF | NRDQGVKCDP | ESEKKRKMEF | NLSNSEEIHS | DFQTLISEIL | ||||
| KPNDDYLLKT | ANAIYGEKTY | AFHNKYLEDM | KTYFGAEPQP | VNFVEASDQI | ||||
| RKDINSWVER | QTEGKIQNLL | PDDSVDSTTR | MILVNALYFK | GIWEHQFLVQ | ||||
| NTTEKPFRIN | ETTSKPVQMM | FMKKKLHIFH | IEKPKAVGLQ | LYYKSRDLSL | ||||
| LILLPEDING | LEQLEKAITY | EKLNEWTSAD | MMELYEVQLH | LPKFKLEDSY | ||||
| DLKSTLSSMG | MSDAFSQSKA | DFSGMSSARN | LFLSNVFHKA | FVEINEQGTE | ||||
| AAAGSGSEID | IRIRVPSIEF | NANHPFLFFI | RHNKTNTILF | YGRLCSP |
Funkcija
Superporodica inhibitora serinske proteinaze visoke molekulske težine (serpin) regulira raznolik niz unutarćelijskih i vanćelijskih procesa, kao što su aktivacija komplementa, fibrinoliza, koagulacija, ćelijska diferencijacija, suzbijanje tumora, apoptoza i migracija ćelija. Serpin odlikuje dobro konzerviranu tercijarna strukturu, koja se sastoji od tri beta-lista i osam ili devet alfa-heliks.[7] Kritični dio molekule, reaktivna središnja petlja, povezuje beta listove A i C. Inhibitor proteaze-10 (PI10; SERPINB10) član je potporodice ov-serpina, koju, u odnosu na arhetipski serpin PI1 (MIM 107400), karakterizira visok stupanj homologije s kokošijim ovalbuminom, nedostatak produžetaka N– i C-terminala, odsustvo signalnog peptida i serinnski umjesto asparaginskih ostatka na pretposljednjem položaju.[8]
Reference
- ^ a b c GRCh38: Ensembl release 89: ENSG00000242550 - Ensembl, maj 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000092572 - Ensembl, maj 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Entrez Gene: Serpin peptidase inhibitor, clade B (ovalbumin), member 10".
- ^ "UniProt, P48595". Pristupljeno 12. 9. 2017.
- ^ Huber R, Carrell RW (novembar 1989). "Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins". Biochemistry. 28 (23): 8951–66. doi:10.1021/bi00449a001. PMID 2690952.
- ^ * Bartuski AJ, Kamachi Y, Schick C, Overhauser J, Silverman GA (august 1997). "Cytoplasmic antiproteinase 2 (PI8) and bomapin (PI10) map to the serpin cluster at 18q21.3". Genomics. 43 (3): 321–8. doi:10.1006/geno.1997.4827. PMID 9268635.
Dopunska literatura
- Chuang TL, Schleef RR (april 1999). "Identification of a nuclear targeting domain in the insertion between helices C and D in protease inhibitor-10". The Journal of Biological Chemistry. 274 (16): 11194–8. doi:10.1074/jbc.274.16.11194. PMID 10196205.
- Lindskog C, Korsgren O, Pontén F, Eriksson JW, Johansson L, Danielsson A (maj 2012). "Novel pancreatic beta cell-specific proteins: antibody-based proteomics for identification of new biomarker candidates". Journal of Proteomics. 75 (9): 2611–20. doi:10.1016/j.jprot.2012.03.008. PMID 22465717.
- Schleef RR, Chuang TL (august 2000). "Protease inhibitor 10 inhibits tumor necrosis factor alpha -induced cell death. Evidence for the formation of intracellular high M(r) protease inhibitor 10-containing complexes". The Journal of Biological Chemistry. 275 (34): 26385–9. doi:10.1074/jbc.C000389200. PMID 10871600.
- Przygodzka P, Ramstedt B, Tengel T, Larsson G, Wilczynska M (april 2010). "Bomapin is a redox-sensitive nuclear serpin that affects responsiveness of myeloid progenitor cells to growth environment". BMC Cell Biology. 11: 30. doi:10.1186/1471-2121-11-30. PMC 2874763. PMID 20433722.
- Shioji G, Ezura Y, Nakajima T, Ohgaki K, Fujiwara H, Kubota Y, Ichikawa T, Inoue K, Shuin T, Habuchi T, Ogawa O, Nishimura T, Emi M (2005). "Nucleotide variations in genes encoding plasminogen activator inhibitor-2 and serine proteinase inhibitor B10 associated with prostate cancer". Journal of Human Genetics. 50 (10): 507–15. doi:10.1007/s10038-005-0285-1. PMID 16172807.
- Riewald M, Schleef RR (novembar 1995). "Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow". The Journal of Biological Chemistry. 270 (45): 26754–7. doi:10.1074/jbc.270.45.26754. PMID 7592909.
Vanjski linkovi
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