COL5A1

COL5A1
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1A89, 1A9A
Identifikatori
Aliasi	COL5A1
Vanjski ID-jevi	OMIM: 120215 MGI: 88457 HomoloGene: 55434 GeneCards: COL5A1
Lokacija gena (čovjek)
Hrom.	Hromosom 9 (čovjek)
Kraj	134,844,843 bp
Lokacija gena (miš)
Hrom.	Hromosom 2 (miš)
Kraj	27,929,526 bp
Obrazac RNK ekspresije
	; ; ; ;
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• extracellular matrix structural constituent; • vezivanje iona metala; • integrin binding; • platelet-derived growth factor binding; • proteoglycan binding; • heparin binding; • GO:0001948, GO:0016582 vezivanje za proteine; • extracellular matrix structural constituent conferring tensile strength;
Ćelijska komponenta	• collagen; • endoplasmic reticulum lumen; • collagen type V trimer; • basement membrane; • Egzosom; • GO:0005578 Vanćelijski matriks; • Vanćelijsko; • extracellular region; • collagen-containing extracellular matrix;
Biološki proces	• eye morphogenesis; • negative regulation of endodermal cell differentiation; • tendon development; • wound healing, spreading of epidermal cells; • integrin biosynthetic process; • heart morphogenesis; • regulation of cellular component organization; • extracellular matrix organization; • Ćelijska adhezija; • blood vessel development; • collagen biosynthetic process; • collagen catabolic process; • Ćelijska migracija; • skin development; • collagen fibril organization; • supramolecular fiber organization;
	Izvori:Amigo / QuickGO
Ortolozi
	1289
	12831
	ENSG00000130635
	ENSMUSG00000026837
	P20908
	O88207
	NM_000093; NM_001278074
	NM_015734
	NP_000084; NP_001265003
	NP_056549
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Kolagenski lanac alfa-1(V) jest protein koji je kod ljudi koditan genom COL5A1.^[5]^[6]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 1.838 aminokiselina, а molekulska težina 183.560 Da.^[7]

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
MDVHTRWKAR	SALRPGAPLL	PPLLLLLLWA	PPPSRAAQPA	DLLKVLDFHN
LPDGITKTTG	FCATRRSSKG	PDVAYRVTKD	AQLSAPTKQL	YPASAFPEDF
SILTTVKAKK	GSQAFLVSIY	NEQGIQQIGL	ELGRSPVFLY	EDHTGKPGPE
DYPLFRGINL	SDGKWHRIAL	SVHKKNVTLI	LDCKKKTTKF	LDRSDHPMID
INGIIVFGTR	ILDEEVFEGD	IQQLLFVSDH	RAAYDYCEHY	SPDCDTAVPD
TPQSQDPNPD	EYYTEGDGEG	ETYYYEYPYY	EDPEDLGKEP	TPSKKPVEAA
KETTEVPEEL	TPTPTEAAPM	PETSEGAGKE	EDVGIGDYDY	VPSEDYYTPS
PYDDLTYGEG	EENPDQPTDP	GAGAEIPTST	ADTSNSSNPA	PPPGEGADDL
EGEFTEETIR	NLDENYYDPY	YDPTSSPSEI	GPGMPANQDT	IYEGIGGPRG
EKGQKGEPAI	IEPGMLIEGP	PGPEGPAGLP	GPPGTMGPTG	QVGDPGERGP
PGRPGLPGAD	GLPGPPGTML	MLPFRFGGGG	DAGSKGPMVS	AQESQAQAIL
QQARLALRGP	AGPMGLTGRP	GPVGPPGSGG	LKGEPGDVGP	QGPRGVQGPP
GPAGKPGRRG	RAGSDGARGM	PGQTGPKGDR	GFDGLAGLPG	EKGHRGDPGP
SGPPGPPGDD	GERGDDGEVG	PRGLPGEPGP	RGLLGPKGPP	GPPGPPGVTG
MDGQPGPKGN	VGPQGEPGPP	GQQGNPGAQG	LPGPQGAIGP	PGEKGPLGKP
GLPGMPGADG	PPGHPGKEGP	PGEKGGQGPP	GPQGPIGYPG	PRGVKGADGI
RGLKGTKGEK	GEDGFPGFKG	DMGIKGDRGE	IGPPGPRGED	GPEGPKGRGG
PNGDPGPLGP	PGEKGKLGVP	GLPGYPGRQG	PKGSIGFPGF	PGANGEKGGR
GTPGKPGPRG	QRGPTGPRGE	RGPRGITGKP	GPKGNSGGDG	PAGPPGERGP
NGPQGPTGFP	GPKGPPGPPG	KDGLPGHPGQ	RGETGFQGKT	GPPGPPGVVG
PQGPTGETGP	MGERGHPGPP	GPPGEQGLPG	LAGKEGTKGD	PGPAGLPGKD
GPPGLRGFPG	DRGLPGPVGA	LGLKGNEGPP	GPPGPAGSPG	ERGPAGAAGP
IGIPGRPGPQ	GPPGPAGEKG	APGEKGPQGP	AGRDGLQGPV	GLPGPAGPVG
PPGEDGDKGE	IGEPGQKGSK	GDKGEQGPPG	PTGPQGPIGQ	PGPSGADGEP
GPRGQQGLFG	QKGDEGPRGF	PGPPGPVGLQ	GLPGPPGEKG	ETGDVGQMGP
PGPPGPRGPS	GAPGADGPQG	PPGGIGNPGA	VGEKGEPGEA	GEPGLPGEGG
PPGPKGERGE	KGESGPSGAA	GPPGPKGPPG	DDGPKGSPGP	VGFPGDPGPP
GEPGPAGQDG	PPGDKGDDGE	PGQTGSPGPT	GEPGPSGPPG	KRGPPGPAGP
EGRQGEKGAK	GEAGLEGPPG	KTGPIGPQGA	PGKPGPDGLR	GIPGPVGEQG
LPGSPGPDGP	PGPMGPPGLP	GLKGDSGPKG	EKGHPGLIGL	IGPPGEQGEK
GDRGLPGPQG	SSGPKGEQGI	TGPSGPIGPP	GPPGLPGPPG	PKGAKGSSGP
TGPKGEAGHP	GPPGPPGPPG	EVIQPLPIQA	SRTRRNIDAS	QLLDDGNGEN
YVDYADGMEE	IFGSLNSLKL	EIEQMKRPLG	TQQNPARTCK	DLQLCHPDFP
DGEYWVDPNQ	GCSRDSFKVY	CNFTAGGSTC	VFPDKKSEGA	RITSWPKENP
GSWFSEFKRG	KLLSYVDAEG	NPVGVVQMTF	LRLLSASAHQ	NVTYHCYQSV
AWQDAATGSY	DKALRFLGSN	DEEMSYDNNP	YIRALVDGCA	TKKGYQKTVL
EIDTPKVEQV	PIVDIMFNDF	GEASQKFGFE	VGPACFMG

Funkcija

This gene encodes an alpha chain for one of the low abundance fibrillar collagens. Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen. This gene product is closely related to type XI collagen and it is possible that the collagen chains of types V and XI constitute a single collagen type with tissue-specific chain combinations. Mutations in this gene are associated with Ehlers-Danlos syndrome, types I and II.^[6]

Također pogledajte

Kolagen

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000130635 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026837 - 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.
^ Greenspan DS, Byers MG, Eddy RL, Cheng W, Jani-Sait S, Shows TB (maj 1992). "Human collagen gene COL5A1 maps to the q34.2----q34.3 region of chromosome 9, near the locus for nail-patella syndrome". Genomics. 12 (4): 836–7. doi:10.1016/0888-7543(92)90320-R. PMID 1572660.
^ ^a ^b "Entrez Gene: COL5A1 collagen, type V, alpha 1".
^ "UniProt, P20908". Pristupljeno 7. 9. 2021.

Dopunska literatura

Mann K (1992). "Isolation of the alpha 3-chain of human type V collagen and characterization by partial sequencing". Biol. Chem. Hoppe-Seyler. 373 (2): 69–75. doi:10.1515/bchm3.1992.373.1.69. PMID 1571108.
Greenspan DS, Cheng W, Hoffman GG (1992). "The pro-alpha 1(V) collagen chain. Complete primary structure, distribution of expression, and comparison with the pro-alpha 1(XI) collagen chain". J. Biol. Chem. 266 (36): 24727–33. doi:10.1016/S0021-9258(18)54290-3. PMID 1722213.
Takahara K, Sato Y, Okazawa K, et al. (1991). "Complete primary structure of human collagen alpha 1 (V) chain". J. Biol. Chem. 266 (20): 13124–9. doi:10.1016/S0021-9258(18)98813-7. PMID 2071595.
Yaoi Y, Hashimoto K, Koitabashi H, et al. (1990). "Primary structure of the heparin-binding site of type V collagen". Biochim. Biophys. Acta. 1035 (2): 139–45. doi:10.1016/0304-4165(90)90108-9. PMID 2203476.
Seyer JM, Kang AH (1989). "Covalent structure of collagen: amino acid sequence of three cyanogen bromide-derived peptides from human alpha 1(V) collagen chain". Arch. Biochem. Biophys. 271 (1): 120–9. doi:10.1016/0003-9861(89)90262-2. PMID 2496661.
Niyibizi C, Fietzek PP, van der Rest M (1984). "Human placenta type V collagens. Evidence for the existence of an alpha 1(V) alpha 2(V) alpha 3(V) collagen molecule". J. Biol. Chem. 259 (22): 14170–4. doi:10.1016/S0021-9258(18)89872-6. PMID 6501291.
Mumby SM, Raugi GJ, Bornstein P (1984). "Interactions of thrombospondin with extracellular matrix proteins: selective binding to type V collagen". J. Cell Biol. 98 (2): 646–52. doi:10.1083/jcb.98.2.646. PMC 2113082. PMID 6693501.
Rhodes RK, Miller EJ (1982). "Evidence for the existence of an alpha 1(V) alpha 2(V) alpha 3(V) collagen molecule in human placental tissue". Coll. Relat. Res. 1 (4): 337–43. doi:10.1016/s0174-173x(81)80010-6. PMID 7346227.
Lee S, Greenspan DS (1995). "Transcriptional promoter of the human alpha 1(V) collagen gene (COL5A1)". Biochem. J. 310 (1): 15–22. doi:10.1042/bj3100015. PMC 1135848. PMID 7646438.
Moradi-Améli M, Rousseau JC, Kleman JP, et al. (1994). "Diversity in the processing events at the N-terminus of type-V collagen". Eur. J. Biochem. 221 (3): 987–95. doi:10.1111/j.1432-1033.1994.tb18815.x. PMID 8181482.
Takahara K, Hoffman GG, Greenspan DS (1996). "Complete structural organization of the human alpha 1 (V) collagen gene (COL5A1): divergence from the conserved organization of other characterized fibrillar collagen genes". Genomics. 29 (3): 588–97. doi:10.1006/geno.1995.9961. PMID 8575750.
De Paepe A, Nuytinck L, Hausser I, et al. (1997). "Mutations in the COL5A1 gene are causal in the Ehlers-Danlos syndromes I and II". Am. J. Hum. Genet. 60 (3): 547–54. PMC 1712501. PMID 9042913.
Tillet E, Ruggiero F, Nishiyama A, Stallcup WB (1997). "The membrane-spanning proteoglycan NG2 binds to collagens V and VI through the central nonglobular domain of its core protein". J. Biol. Chem. 272 (16): 10769–76. doi:10.1074/jbc.272.16.10769. PMID 9099729.
Sasaki T, Brakebusch C, Engel J, Timpl R (1998). "Mac-2 binding protein is a cell-adhesive protein of the extracellular matrix which self-assembles into ring-like structures and binds beta1 integrins, collagens and fibronectin". EMBO J. 17 (6): 1606–13. doi:10.1093/emboj/17.6.1606. PMC 1170508. PMID 9501082.
Wu YL, Sumiyoshi H, Khaleduzzaman M, et al. (1998). "cDNA sequence and expression of the mouse alpha1(V) collagen gene (Col5a1)". Biochim. Biophys. Acta. 1397 (3): 275–84. doi:10.1016/S0167-4781(98)00016-5. PMID 9582436.
Burrows NP, Nicholls AC, Richards AJ, et al. (1998). "A point mutation in an intronic branch site results in aberrant splicing of COL5A1 and in Ehlers-Danlos syndrome type II in two British families". Am. J. Hum. Genet. 63 (2): 390–8. doi:10.1086/301948. PMC 1377290. PMID 9683580.
Aho S, Uitto J (1999). "Two-hybrid analysis reveals multiple direct interactions for thrombospondin 1". Matrix Biol. 17 (6): 401–12. doi:10.1016/S0945-053X(98)90100-7. PMID 9840442.
Giunta C, Steinmann B (2000). "Compound heterozygosity for a disease-causing G1489E [correction of G1489D] and disease-modifying G530S substitution in COL5A1 of a patient with the classical type of Ehlers-Danlos syndrome: an explanation of intrafamilial variability?". Am. J. Med. Genet. 90 (1): 72–9. doi:10.1002/(SICI)1096-8628(20000103)90:1<72::AID-AJMG13>3.0.CO;2-C. PMID 10602121.
Imamura Y, Scott IC, Greenspan DS (2000). "The pro-alpha3(V) collagen chain. Complete primary structure, expression domains in adult and developing tissues, and comparison to the structures and expression domains of the other types V and XI procollagen chains". J. Biol. Chem. 275 (12): 8749–59. doi:10.1074/jbc.275.12.8749. PMID 10722718.

Vanjski linkovi

Ehlers-Danlos Syndrome, Classic Type. Includes: Ehlers-Danlos Syndrome Type I, Ehlers-Danlos Syndrome Type II

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000130635 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000026837 - 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.

[pmid1572660-5] Greenspan DS, Byers MG, Eddy RL, Cheng W, Jani-Sait S, Shows TB (maj 1992). "Human collagen gene COL5A1 maps to the q34.2----q34.3 region of chromosome 9, near the locus for nail-patella syndrome". Genomics. 12 (4): 836–7. doi:10.1016/0888-7543(92)90320-R. PMID 1572660.

[entrez-6] "Entrez Gene: COL5A1 collagen, type V, alpha 1".

[UniProt-7] "UniProt, P20908". Pristupljeno 7. 9. 2021.

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