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) Bend 7p21.3 Početak 12,570,577 bp Kraj 12,660,182 bp
Lokacija gena (miš) Hrom. Hromosom 12 (miš) Bend 12|12 B1 Početak 40,109,768 bp 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
Vrste	Čovjek	Miš
Entrez	85477	20259
Ensembl	ENSG00000006747	ENSMUSG00000002565
UniProt	Q9Y6U3	Q60604
RefSeq (mRNK)	NM_001112706 NM_033128	NM_001146196 NM_009132
RefSeq (bjelančevina)	NP_001106177 NP_149119	NP_001139668 NP_033158
Lokacija (UCSC)	Chr 7: 12.57 – 12.66 Mb	Chr 12: 40.11 – 40.18 Mb
PubMed pretraga
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

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

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 715 aminokiselina, а molekulska težina 80.489 Da.

• 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 . 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.

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.