COL7A1

Alfa-1 lanac kolagena VII jest protein koji je kod ljudi kodiran genom COL7A1 sa hromosoma 3.^[5]

COL7A1
Identifikatori
Aliasi	COL7A1
Vanjski ID-jevi	OMIM: 120120 MGI: 88462 HomoloGene: 73 GeneCards: COL7A1
Lokacija gena (čovjek) Hrom. Hromosom 3 (čovjek)[1] Bend 3p21.31 Početak 48,564,073 bp[1] Kraj 48,595,329 bp[1]
Lokacija gena (miš) Hrom. Hromosom 9 (miš)[2] Bend 9 F2|9 59.63 cM Početak 108,782,654 bp[2] Kraj 108,813,943 bp[2]
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • peptidase inhibitor activity • GO:0001948, GO:0016582 vezivanje za proteine • serine-type endopeptidase inhibitor activity • vezivanje identičnih proteina • extracellular matrix structural constituent conferring tensile strength Ćelijska komponenta • collagen • endoplasmic reticulum lumen • collagen type VII trimer • GO:0005578 Vanćelijski matriks • extracellular region • basement membrane • COPII-coated ER to Golgi transport vesicle • endoplasmic reticulum-Golgi intermediate compartment membrane • Golđijeva membrana • Vanćelijsko • collagen-containing extracellular matrix Biološki proces • negative regulation of peptidase activity • endodermal cell differentiation • extracellular matrix organization • endoplasmic reticulum to Golgi vesicle-mediated transport • COPII vesicle coating • Ćelijska adhezija • epidermis development • collagen catabolic process • negative regulation of endopeptidase activity • growth plate cartilage chondrocyte morphogenesis Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	1294	12836
Ensembl	ENSG00000114270	ENSMUSG00000025650
UniProt	Q02388	Q63870
RefSeq (mRNK)	NM_000094	NM_007738
RefSeq (bjelančevina)	NP_000085	NP_031764
Lokacija (UCSC)	Chr 3: 48.56 – 48.6 Mb	Chr 9: 108.78 – 108.81 Mb
PubMed pretraga	[3]	[4]
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 2.944 aminokiselina, а molekulska težina Da. 295 220^[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
MTLRLLVAAL		CAGILAEAPR		VRAQHRERVT		CTRLYAADIV		FLLDGSSSIG
RSNFREVRSF		LEGLVLPFSG		AASAQGVRFA		TVQYSDDPRT		EFGLDALGSG
GDVIRAIREL		SYKGGNTRTG		AAILHVADHV		FLPQLARPGV		PKVCILITDG
KSQDLVDTAA		QRLKGQGVKL		FAVGIKNADP		EELKRVASQP		TSDFFFFVND
FSILRTLLPL		VSRRVCTTAG		GVPVTRPPDD		STSAPRDLVL		SEPSSQSLRV
QWTAASGPVT		GYKVQYTPLT		GLGQPLPSER		QEVNVPAGET		SVRLRGLRPL
TEYQVTVIAL		YANSIGEAVS		GTARTTALEG		PELTIQNTTA		HSLLVAWRSV
PGATGYRVTW		RVLSGGPTQQ		QELGPGQGSV		LLRDLEPGTD		YEVTVSTLFG
RSVGPATSLM		ARTDASVEQT		LRPVILGPTS		ILLSWNLVPE		ARGYRLEWRR
ETGLEPPQKV		VLPSDVTRYQ		LDGLQPGTEY		RLTLYTLLEG		HEVATPATVV
PTGPELPVSP		VTDLQATELP		GQRVRVSWSP		VPGATQYRII		VRSTQGVERT
LVLPGSQTAF		DLDDVQAGLS		YTVRVSARVG		PREGSASVLT		VRREPETPLA
VPGLRVVVSD		ATRVRVAWGP		VPGASGFRIS		WSTGSGPESS		QTLPPDSTAT
DITGLQPGTT		YQVAVSVLRG		REEGPAAVIV		ARTDPLGPVR		TVHVTQASSS
SVTITWTRVP		GATGYRVSWH		SAHGPEKSQL		VSGEATVAEL		DGLEPDTEYT
VHVRAHVAGV		DGPPASVVVR		TAPEPVGRVS		RLQILNASSD		VLRITWVGVT
GATAYRLAWG		RSEGGPMRHQ		ILPGNTDSAE		IRGLEGGVSY		SVRVTALVGD
REGTPVSIVV		TTPPEAPPAL		GTLHVVQRGE		HSLRLRWEPV		PRAQGFLLHW
QPEGGQEQSR		VLGPELSSYH		LDGLEPATQY		RVRLSVLGPA		GEGPSAEVTA
RTESPRVPSI		ELRVVDTSID		SVTLAWTPVS		RASSYILSWR		PLRGPGQEVP
GSPQTLPGIS		SSQRVTGLEP		GVSYIFSLTP		VLDGVRGPEA		SVTQTPVCPR
GLADVVFLPH		ATQDNAHRAE		ATRRVLERLV		LALGPLGPQA		VQVGLLSYSH
RPSPLFPLNG		SHDLGIILQR		IRDMPYMDPS		GNNLGTAVVT		AHRYMLAPDA
PGRRQHVPGV		MVLLVDEPLR		GDIFSPIREA		QASGLNVVML		GMAGADPEQL
RRLAPGMDSV		QTFFAVDDGP		SLDQAVSGLA		TALCQASFTT		QPRPEPCPVY
CPKGQKGEPG		EMGLRGQVGP		PGDPGLPGRT		GAPGPQGPPG		SATAKGERGF
PGADGRPGSP		GRAGNPGTPG		APGLKGSPGL		PGPRGDPGER		GPRGPKGEPG
APGQVIGGEG		PGLPGRKGDP		GPSGPPGPRG		PLGDPGPRGP		PGLPGTAMKG
DKGDRGERGP		PGPGEGGIAP		GEPGLPGLPG		SPGPQGPVGP		PGKKGEKGDS
EDGAPGLPGQ		PGSPGEQGPR		GPPGAIGPKG		DRGFPGPLGE		AGEKGERGPP
GPAGSRGLPG		VAGRPGAKGP		EGPPGPTGRQ		GEKGEPGRPG		DPAVVGPAVA
GPKGEKGDVG		PAGPRGATGV		QGERGPPGLV		LPGDPGPKGD		PGDRGPIGLT
GRAGPPGDSG		PPGEKGDPGR		PGPPGPVGPR		GRDGEVGEKG		DEGPPGDPGL
PGKAGERGLR		GAPGVRGPVG		EKGDQGDPGE		DGRNGSPGSS		GPKGDRGEPG
PPGPPGRLVD		TGPGAREKGE		PGDRGQEGPR		GPKGDPGLPG		APGERGIEGF
RGPPGPQGDP		GVRGPAGEKG		DRGPPGLDGR		SGLDGKPGAA		GPSGPNGAAG
KAGDPGRDGL		PGLRGEQGLP		GPSGPPGLPG		KPGEDGKPGL		NGKNGEPGDP
GEDGRKGEKG		DSGASGREGR		DGPKGERGAP		GILGPQGPPG		LPGPVGPPGQ
GFPGVPGGTG		PKGDRGETGS		KGEQGLPGER		GLRGEPGSVP		NVDRLLETAG
IKASALREIV		ETWDESSGSF		LPVPERRRGP		KGDSGEQGPP		GKEGPIGFPG
ERGLKGDRGD		PGPQGPPGLA		LGERGPPGPS		GLAGEPGKPG		IPGLPGRAGG
VGEAGRPGER		GERGEKGERG		EQGRDGPPGL		PGTPGPPGPP		GPKVSVDEPG
PGLSGEQGPP		GLKGAKGEPG		SNGDQGPKGD		RGVPGIKGDR		GEPGPRGQDG
NPGLPGERGM		AGPEGKPGLQ		GPRGPPGPVG		GHGDPGPPGA		PGLAGPAGPQ
GPSGLKGEPG		ETGPPGRGLT		GPTGAVGLPG		PPGPSGLVGP		QGSPGLPGQV
GETGKPGAPG		RDGASGKDGD		RGSPGVPGSP		GLPGPVGPKG		EPGPTGAPGQ
AVVGLPGAKG		EKGAPGGLAG		DLVGEPGAKG		DRGLPGPRGE		KGEAGRAGEP
GDPGEDGQKG		APGPKGFKGD		PGVGVPGSPG		PPGPPGVKGD		LGLPGLPGAP
GVVGFPGQTG		PRGEMGQPGP		SGERGLAGPP		GREGIPGPLG		PPGPPGSVGP
PGASGLKGDK		GDPGVGLPGP		RGERGEPGIR		GEDGRPGQEG		PRGLTGPPGS
RGERGEKGDV		GSAGLKGDKG		DSAVILGPPG		PRGAKGDMGE		RGPRGLDGDK
GPRGDNGDPG		DKGSKGEPGD		KGSAGLPGLR		GLLGPQGQPG		AAGIPGDPGS
PGKDGVPGIR		GEKGDVGFMG		PRGLKGERGV		KGACGLDGEK		GDKGEAGPPG
RPGLAGHKGE		MGEPGVPGQS		GAPGKEGLIG		PKGDRGFDGQ		PGPKGDQGEK
GERGTPGIGG		FPGPSGNDGS		AGPPGPPGSV		GPRGPEGLQG		QKGERGPPGE
RVVGAPGVPG		APGERGEQGR		PGPAGPRGEK		GEAALTEDDI		RGFVRQEMSQ
HCACQGQFIA		SGSRPLPSYA		ADTAGSQLHA		VPVLRVSHAE		EEERVPPEDD
EYSEYSEYSV		EEYQDPEAPW		DSDDPCSLPL		DEGSCTAYTL		RWYHRAVTGS
TEACHPFVYG		GCGGNANRFG		TREACERRCP		PRVVQSQGTG		TAQD

Funkcija

Ovaj gen kodira alfa lanac kolagena tipa VII. Kolagensko vlakno tipa VII, sastavljeno od tri identična alfa-kolagenska lanca, ograničeno je na baznu zonu ispod slojevitog pločastog epitela. Funkcionira kao vlakno za sidrenje između vanjskog epitela i strome ispod. Mutacije u ovom genu su povezane sa svim oblicima distrofijska epidermolysis bullosa.^[7] U odsustvu mutacija, međutim, autoimunski odgovor protiv kolagena tipa VII može dovesti do stečenog oblika ove bolesti koji se naziva epidermolysis bullosa acquisita.^[8]

Kolagen tipa VII također nalazi se u retini; njegova funkcija u ovom organu nije poznata.^[9]

COL7A1 nalazi se na kratkom kraku hromosoma 3, u regiji 3p21.31. Gen je veličine otprilike 31.000 baznih parova i izvanredan je po ekstremnoj fragmentaciji kodirajuće sekvence na 118 egzona.^[10][11] COL7A1 se transkribira iu iRNK od 9.287 baznih parova.^[12] U koži, kolagene proteine tipa VII sintetiziraju keratinociti i dermni fibroblasti.^[13]

Simbol za ortologni gen kućnog miša je Col7a1.

Klinički značaj

Nasljedna bolest, epidermolysis bullosa dystrophica, uzrokovana je dominantnim ili recesivnim mutacijama u COL7A1.^[14]

Epidermolysis bullosa acquisita uključuje autoimunsku reakciju na ovaj oblik kolagena.^[15]

Interakcije

Pokazalo se da kolagen tipa VII alfa 1 ima interakcije sa lamininom 5^[16] i fibronektinom.^[17][18]

Također pogledajte

• Kolagen

Reference

1. GRCh38: Ensembl release 89: ENSG00000114270 - Ensembl, maj 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000025650 - 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.
5. Parente MG, Chung LC, Ryynänen J, Woodley DT, Wynn KC, Bauer EA, Mattei MG, Chu ML, Uitto J (august 1991). "Human type VII collagen: cDNA cloning and chromosomal mapping of the gene". Proceedings of the National Academy of Sciences of the United States of America. 88 (16): 6931–5. Bibcode:1991PNAS...88.6931P. doi:10.1073/pnas.88.16.6931. PMC 52207. PMID 1871109.
6. "UniProt, Q02388" (jezik: engleski). Pristupljeno 3. 11. 2021.
7. Bardhan A, Bruckner-Tuderman L, Chapple IL, Fine JD, Harper N, Has C, et al. (septembar 2020). "Epidermolysis bullosa". Nature Reviews. Disease Primers. 6 (1): 78. doi:10.1038/s41572-020-0210-0. PMID 32973163. S2CID 221861310.
8. "COL7A1 collagen, type VII, alpha 1 (epidermolysis bullosa, dystrophic, dominant and recessive)". NCBI Entrez Gene database.
9. Ponsioen TL, van Luyn MJ, van der Worp RJ, van Meurs JC, Hooymans JM, Los LI (septembar 2008). "Collagen distribution in the human vitreoretinal interface". Investigative Ophthalmology & Visual Science. 49 (9): 4089–95. doi:10.1167/iovs.07-1456. PMID 18450587.
10. Christiano AM, Hoffman GG, Chung-Honet LC, Lee S, Cheng W, Uitto J, Greenspan DS (maj 1994). "Structural organization of the human type VII collagen gene (COL7A1), composed of more exons than any previously characterized gene". Genomics. 21 (1): 169–79. doi:10.1006/geno.1994.1239. PMID 8088784.
11. "COL7A1 genomic sequence". NCBI Entrez Nucleotide Database. 17. 5. 2004.
12. "COL7A1 mRNA sequence". NCBI Entrez Nucleotide Database. 15. 9. 1995.
13. OMIM: COL7A1 -120120
14. Dang N, Murrell DF (juli 2008). "Mutation analysis and characterization of COL7A1 mutations in dystrophic epidermolysis bullosa". Experimental Dermatology. 17 (7): 553–68. doi:10.1111/j.1600-0625.2008.00723.x. PMID 18558993. S2CID 32600295.
15. Helen Chapel; Mansel Haeney; Siraj Misbah (2006). Essentials of clinical immunology. Wiley-Blackwell. str. 207–. ISBN 978-1-4051-2761-5. Pristupljeno 25. 6. 2010.
16. Rousselle P, Keene DR, Ruggiero F, Champliaud MF, Rest M, Burgeson RE (august 1997). "Laminin 5 binds the NC-1 domain of type VII collagen". The Journal of Cell Biology. 138 (3): 719–28. doi:10.1083/jcb.138.3.719. PMC 2141627. PMID 9245798.
17. Lapiere JC, Chen JD, Iwasaki T, Hu L, Uitto J, Woodley DT (novembar 1994). "Type VII collagen specifically binds fibronectin via a unique subdomain within the collagenous triple helix". The Journal of Investigative Dermatology. 103 (5): 637–41. doi:10.1111/1523-1747.ep12398270. PMID 7963647.
18. Chen M, Marinkovich MP, Veis A, Cai X, Rao CN, O'Toole EA, Woodley DT (juni 1997). "Interactions of the amino-terminal noncollagenous (NC1) domain of type VII collagen with extracellular matrix components. A potential role in epidermal-dermal adherence in human skin". The Journal of Biological Chemistry. 272 (23): 14516–22. doi:10.1074/jbc.272.23.14516. PMID 9169408.

Dopunska literatura

• Mecklenbeck S, Hammami-Hauasli N, Höpfner B, Schumann H, Kramer A, Küster W, Bruckner-Tuderman L (mart 1999). "Clustering of COL7A1 mutations in exon 73: implications for mutation analysis in dystrophic epidermolysis bullosa". The Journal of Investigative Dermatology. 112 (3): 398–400. doi:10.1046/j.1523-1747.1999.00518.x. PMID 10084325.
• Dang N, Klingberg S, Marr P, Murrell DF (juni 2007). "Review of collagen VII sequence variants found in Australasian patients with dystrophic epidermolysis bullosa reveals nine novel COL7A1 variants". Journal of Dermatological Science. 46 (3): 169–78. doi:10.1016/j.jdermsci.2007.02.006. PMID 17425959.
• Christiano AM, Rosenbaum LM, Chung-Honet LC, Parente MG, Woodley DT, Pan TC, Zhang RZ, Chu ML, Burgeson RE, Uitto J (oktobar 1992). "The large non-collagenous domain (NC-1) of type VII collagen is amino-terminal and chimeric. Homology to cartilage matrix protein, the type III domains of fibronectin and the A domains of von Willebrand factor". Human Molecular Genetics. 1 (7): 475–81. doi:10.1093/hmg/1.7.475. PMID 1307247.
• Gammon WR, Abernethy ML, Padilla KM, Prisayanh PS, Cook ME, Wright J, Briggaman RA, Hunt SW (decembar 1992). "Noncollagenous (NC1) domain of collagen VII resembles multidomain adhesion proteins involved in tissue-specific organization of extracellular matrix". The Journal of Investigative Dermatology. 99 (6): 691–6. doi:10.1111/1523-1747.ep12614080. PMID 1469284.
• Tanaka T, Takahashi K, Furukawa F, Imamura S (mart 1992). "Molecular cloning and characterization of type VII collagen cDNA". Biochemical and Biophysical Research Communications. 183 (3): 958–63. doi:10.1016/S0006-291X(05)80283-9. PMID 1567409.
• Seltzer JL, Eisen AZ, Bauer EA, Morris NP, Glanville RW, Burgeson RE (mart 1989). "Cleavage of type VII collagen by interstitial collagenase and type IV collagenase (gelatinase) derived from human skin". The Journal of Biological Chemistry. 264 (7): 3822–6. doi:10.1016/S0021-9258(19)84924-4. PMID 2537292.
• Fine JD, Johnson L, Wright T (maj 1989). "Epidermolysis bullosa simplex superficialis. A new variant of epidermolysis bullosa characterized by subcorneal skin cleavage mimicking peeling skin syndrome". Archives of Dermatology. 125 (5): 633–8. doi:10.1001/archderm.125.5.633. PMID 2653224.
• Bart BJ, Gorlin RJ, Anderson VE, Lynch FW (mart 1966). "Congenital localized absence of skin and associated abnormalities resembling epidermolysis bullosa. A new syndrome". Archives of Dermatology. 93 (3): 296–304. doi:10.1001/archderm.93.3.296. PMID 5910871.
• Tanaka T, Furukawa F, Imamura S (maj 1994). "Epitope mapping for epidermolysis bullosa acquisita autoantibody by molecularly cloned cDNA for type VII collagen". The Journal of Investigative Dermatology. 102 (5): 706–9. doi:10.1111/1523-1747.ep12374333. PMID 7513737.
• Christiano AM, Morricone A, Paradisi M, Angelo C, Mazzanti C, Cavalieri R, Uitto J (mart 1995). "A glycine-to-arginine substitution in the triple-helical domain of type VII collagen in a family with dominant dystrophic epidermolysis bullosa". The Journal of Investigative Dermatology. 104 (3): 438–40. doi:10.1111/1523-1747.ep12666033. PMID 7861014.
• Christiano AM, Suga Y, Greenspan DS, Ogawa H, Uitto J (mart 1995). "Premature termination codons on both alleles of the type VII collagen gene (COL7A1) in three brothers with recessive dystrophic epidermolysis bullosa". The Journal of Clinical Investigation. 95 (3): 1328–34. doi:10.1172/JCI117783. PMC 441472. PMID 7883979.
• Lapiere JC, Chen JD, Iwasaki T, Hu L, Uitto J, Woodley DT (novembar 1994). "Type VII collagen specifically binds fibronectin via a unique subdomain within the collagenous triple helix". The Journal of Investigative Dermatology. 103 (5): 637–41. doi:10.1111/1523-1747.ep12398270. PMID 7963647.
• Christiano AM, Greenspan DS, Lee S, Uitto J (august 1994). "Cloning of human type VII collagen. Complete primary sequence of the alpha 1(VII) chain and identification of intragenic polymorphisms". The Journal of Biological Chemistry. 269 (32): 20256–62. doi:10.1016/S0021-9258(17)31984-1. PMID 8051117.
• Christiano AM, Ryynänen M, Uitto J (april 1994). "Dominant dystrophic epidermolysis bullosa: identification of a Gly-->Ser substitution in the triple-helical domain of type VII collagen". Proceedings of the National Academy of Sciences of the United States of America. 91 (9): 3549–53. doi:10.1073/pnas.91.9.3549. PMC 43617. PMID 8170945.
• Greenspan DS, Byers MG, Eddy RL, Hoffman GG, Shows TB (1993). "Localization of the human collagen gene COL7A1 to 3p21.3 by fluorescence in situ hybridization". Cytogenetics and Cell Genetics. 62 (1): 35–6. doi:10.1159/000133440. PMID 8422754.
• Greenspan DS (mart 1993). "The carboxyl-terminal half of type VII collagen, including the non-collagenous NC-2 domain and intron/exon organization of the corresponding region of the COL7A1 gene". Human Molecular Genetics. 2 (3): 273–8. doi:10.1093/hmg/2.3.273. PMID 8499916.
• Christiano AM, Greenspan DS, Hoffman GG, Zhang X, Tamai Y, Lin AN, Dietz HC, Hovnanian A, Uitto J (maj 1993). "A missense mutation in type VII collagen in two affected siblings with recessive dystrophic epidermolysis bullosa". Nature Genetics. 4 (1): 62–6. doi:10.1038/ng0593-62. PMID 8513326. S2CID 9099319.
• Christiano AM, Lee JY, Chen WJ, LaForgia S, Uitto J (septembar 1995). "Pretibial epidermolysis bullosa: genetic linkage to COL7A1 and identification of a glycine-to-cysteine substitution in the triple-helical domain of type VII collagen". Human Molecular Genetics. 4 (9): 1579–83. doi:10.1093/hmg/4.9.1579. PMID 8541842.

Vanjski linkovi

• GeneReviews/NCBI/NIH/UW entry on Dystrophic Epidermolysis Bullosa