SCIN

SCIN
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	3FG6, 5A1K, 5A1M
Identifikatori
Aliasi	SCIN
Vanjski ID-jevi	OMIM: 613416 MGI: 1306794 HomoloGene: 36296 GeneCards: SCIN
Lokacija gena (čovjek)
Hrom.	Hromosom 7 (čovjek)
Kraj	12,660,182 bp
Lokacija gena (miš)
Hrom.	Hromosom 12 (miš)
Kraj	40,184,227 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• calcium ion binding; • phosphatidylserine binding; • actin filament binding; • 1-phosphatidylinositol binding; • actin binding; • phosphatidylinositol-4,5-bisphosphate binding; • vezivanje iona metala;
Ćelijska komponenta	• citoplazma; • cell cortex; • brush border; • Egzosom; • citoskelet; • podosome; • međućelijske veze; • projekcija ćelije; • ćelijska membrana; • GO:0009327 makromolekulani kompleks;
Biološki proces	• sequestering of actin monomers; • regulation of chondrocyte differentiation; • actin nucleation; • actin filament severing; • positive regulation of actin nucleation; • positive regulation of secretion; • actin filament capping; • positive regulation of apoptotic process; • positive regulation of megakaryocyte differentiation; • negative regulation of cell population proliferation; • calcium-ion regulated exocytosis;
	Izvori:Amigo / QuickGO
Ortolozi
	85477
	20259
	ENSG00000006747
	ENSMUSG00000002565
	Q9Y6U3
	Q60604
	NM_001112706; NM_033128
	NM_001146196; NM_009132
	NP_001106177; NP_149119
	NP_001139668; NP_033158
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Scinderin (poznat i kao adseverin) jest protein koji je kod ljudi kodiran genom SCIN.^[5]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 715 aminokiselina, а molekulska težina 80.489 Da.^[6]

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
MARELYHEEF	ARAGKQAGLQ	VWRIEKLELV	PVPQSAHGDF	YVGDAYLVLH
TAKTSRGFTY	HLHFWLGKEC	SQDESTAAAI	FTVQMDDYLG	GKPVQNRELQ
GYESNDFVSY	FKGGLKYKAG	GVASGLNHVL	TNDLTAKRLL	HVKGRRVVRA
TEVPLSWDSF	NKGDCFIIDL	GTEIYQWCGS	SCNKYERLKA	NQVATGIRYN
ERKGRSELIV	VEEGSEPSEL	IKVLGEKPEL	PDGGDDDDII	ADISNRKMAK
LYMVSDASGS	MRVTVVAEEN	PFSMAMLLSE	ECFILDHGAA	KQIFVWKGKD
ANPQERKAAM	KTAEEFLQQM	NYSKNTQIQV	LPEGGETPIF	KQFFKDWRDK
DQSDGFGKVY	VTEKVAQIKQ	IPFDASKLHS	SPQMAAQHNM	VDDGSGKVEI
WRVENNGRIQ	VDQNSYGEFY	GGDCYIILYT	YPRGQIIYTW	QGANATRDEL
TTSAFLTVQL	DRSLGGQAVQ	IRVSQGKEPV	HLLSLFKDKP	LIIYKNGTSK
KGGQAPAPPT	RLFQVRRNLA	SITRIVEVDV	DANSLNSNDV	FVLKLPQNSG
YIWVGKGASQ	EEEKGAEYVA	SVLKCKTLRI	QEGEEPEEFW	NSLGGKKDYQ
TSPLLETQAE	DHPPRLYGCS	NKTGRFVIEE	IPGEFTQDDL	AEDDVMLLDA
WEQIFIWIGK	DANEVEKKES	LKSAKMYLET	DPSGRDKRTP	IVIIKQGHEP
PTFTGWFLGW	DSSKW

Funkcija

Scinderin je aktin-razdvajajući protein natporodice gelsolina .^[7] Otkriven je u laboratoriji dr. Trifara na Univerzitetu u Ottawi, Kanada. Sekretinska tkiva su bogata scinderinom. U tim tkivima scinderin, protein ovisan o kalciju, regulira kortikalne aktinske mreže. Normalno sekretorne vezikule isključene su sa mjesta oslobađanja na plazmamembrani, zbog prisustva korine aktinske mreže. Tokom stimulacije ćelija, kalcijevi kanali se otvaraju, dopuštajući kalcijevim ionima da uđu u sekretornu ćeliju. Povećanje unutarćelijskog kalcija aktivira scinderin sa posljedičnim prekidanjem aktinske niti i lokalnom disocijacijom mreža aktinskih niti. To omogućuje kretanje sekretornih vezikula da oslobode mjesta na plazmamembrani.

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000006747 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000002565 - 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: SCIN scinderin".
^ "UniProt, Q9Y6U3" (jezik: engleski). Pristupljeno 28. 9. 2021.
^ Ghoshdastider, U; Popp, D; Burtnick, L. D.; Robinson, R. C. (2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton. 70 (11): 775–95. doi:10.1002/cm.21149. PMID 24155256. S2CID 205643538.

Dopunska literatura

Rodríguez Del Castillo A; Vitale ML; Trifaró JM (1992). "Ca2+ and pH determine the interaction of chromaffin cell scinderin with phosphatidylserine and phosphatidylinositol 4,5,-biphosphate and its cellular distribution during nicotinic-receptor stimulation and protein kinase C activation". J. Cell Biol. 119 (4): 797–810. doi:10.1083/jcb.119.4.797. PMC 2289683. PMID 1331119.
Rodríguez Del Castillo A; Vitale ML; Tchakarov L; Trifaró JM (1992). "Human platelets contain scinderin, a Ca(2+)-dependent actin filament-severing protein". Thromb. Haemost. 67 (2): 248–51. doi:10.1055/s-0038-1648420. PMID 1621245.
Lueck A; Brown D; Kwiatkowski DJ (1999). "The actin-binding proteins adseverin and gelsolin are both highly expressed but differentially localized in kidney and intestine". J. Cell Sci. 111. ( Pt 24): 3633–43. PMID 9819354.
Zunino R, Li Q, Rosé SD, et al. (2001). "Expression of scinderin in megakaryoblastic leukemia cells induces differentiation, maturation, and apoptosis with release of plateletlike particles and inhibits proliferation and tumorigenesis". Blood. 98 (7): 2210–9. doi:10.1182/blood.V98.7.2210. PMID 11568009.
Nagase T; Kikuno R; Ohara O (2002). "Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins". DNA Res. 8 (4): 179–87. doi:10.1093/dnares/8.4.179. PMID 11572484.
Lejen T; Pene TD; Rosé SD; Trifaró JM (2002). "The role of different Scinderin domains in the control of F-actin cytoskeleton during exocytosis". Ann. N. Y. Acad. Sci. 971 (1): 248–50. Bibcode:2002NYASA.971..248L. doi:10.1111/j.1749-6632.2002.tb04469.x. PMID 12438125. S2CID 19994226.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. Bibcode:2003Natur.424..157H. doi:10.1038/nature01782. PMID 12853948.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
Ehre C, Rossi AH, Abdullah LH, et al. (2005). "Barrier role of actin filaments in regulated mucin secretion from airway goblet cells". Am. J. Physiol., Cell Physiol. 288 (1): C46–56. doi:10.1152/ajpcell.00397.2004. PMID 15342343.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000006747 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000002565 - 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: SCIN scinderin".

[UniProt-6] "UniProt, Q9Y6U3" (jezik: engleski). Pristupljeno 28. 9. 2021.

[7] Ghoshdastider, U; Popp, D; Burtnick, L. D.; Robinson, R. C. (2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton. 70 (11): 775–95. doi:10.1002/cm.21149. PMID 24155256. S2CID 205643538.

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