SERPINB10

SERPINB10
Identifikatori
Aliasi	SERPINB10
Vanjski ID-jevi	OMIM: 602058 MGI: 2138648 HomoloGene: 68430 GeneCards: SERPINB10
Lokacija gena (čovjek)
Hrom.	Hromosom 18 (čovjek)
Kraj	63,936,111 bp
Lokacija gena (miš)
Hrom.	Hromosom 1 (miš)
Kraj	107,477,001 bp
Ontologija gena
Molekularna funkcija	• peptidase inhibitor activity; • serine-type endopeptidase inhibitor activity;
Ćelijska komponenta	• citoplazma; • Vanćelijsko; • ćelijska membrana; • secretory granule membrane; • ficolin-1-rich granule membrane; • jedro;
Biološki proces	• negative regulation of peptidase activity; • negative regulation of endopeptidase activity; • neutrophil degranulation; • negative regulation of apoptotic process;
	Izvori:Amigo / QuickGO
Ortolozi
	5273
	241197
	ENSG00000242550
	ENSMUSG00000092572
	P48595
	Q8K1K6
	NM_005024
	NM_001160307; NM_198028
	NP_005015
	NP_001153779; NP_932145
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

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

Šablon:Serpini

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000242550 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000092572 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: Serpin peptidase inhibitor, clade B (ovalbumin), member 10".

[UniProt-6] "UniProt, P48595". Pristupljeno 12. 9. 2017.

[7] 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.

[8] * 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.

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