Q02388 (CO7A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(VII) chain

Alternative name(s):
Long-chain collagen
Short name=LC collagen

Gene names

Name:

COL7A1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2944 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen.
Subunit structure	Homotrimer. Interacts with MIA3/TANGO1; facilitating its loading into transport carriers and subsequent secretion. Ref.9
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane.
Post-translational modification	Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Involvement in disease	Epidermolysis bullosa acquisita (EBA) is an autoimmune acquired blistering skin disease resulting from autoantibodies to type VII collagen. Epidermolysis bullosa dystrophica, autosomal dominant (DDEB) [MIM:131750]: A group of autosomal dominant blistering skin diseases characterized by tissue separation which occurs below the dermal-epidermal basement membrane at the level of the anchoring fibrils. Various clinical types with different severity are recognized, ranging from severe mutilating forms to mild forms with limited and localized scarring, and less frequent extracutaneous manifestations. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.23 Ref.24 Ref.25 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.37 Ref.38 Ref.45 Epidermolysis bullosa dystrophica, autosomal recessive (RDEB) [MIM:226600]: A group of autosomal recessive blistering skin diseases characterized by tissue separation which occurs below the dermal-epidermal basement membrane at the level of the anchoring fibrils. Various clinical types with different severity are recognized, ranging from severe mutilating forms to mild forms with limited and localized scarring, and less frequent extracutaneous manifestations. Mild forms include epidermolysis bullosa mitis and epidermolysis bullosa localisata. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.20 Ref.22 Ref.23 Ref.25 Ref.26 Ref.32 Ref.39 Ref.40 Ref.45 Epidermolysis bullosa dystrophica, Pasini type (P-DEB) [MIM:131750]: A severe, dominantly inherited form of dystrophic epidermolysis bullosa characterized by albopapuloid Pasini papule, dorsal extremity blistering, milia formation and red atrophic scarring after recurrent blisters. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.33 Epidermolysis bullosa dystrophica, Hallopeau-Siemens type (HS-DEB) [MIM:226600]: The most severe recessive form of dystrophic epidermolysis bullosa. It manifests with mutilating scarring, joint contractures, corneal erosions, esophagus structures, and propensity to formation of cutaneous squamous cell carcinomas leading to premature demise of the affected individuals. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.18 Ref.21 Ref.25 Ref.32 Transient bullous dermolysis of the newborn (TBDN) [MIM:131705]: TBDN is a neonatal form of dystrophic epidermolysis bullosa characterized by sub-epidermal blisters, reduced or abnormal anchoring fibrils at the dermo-epidermal junction, and electron-dense inclusions in keratinocytes. TBDN heals spontaneously or strongly improves within the first months and years of life. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.28 Epidermolysis bullosa dystrophica, pretibial type (PR-DEB) [MIM:131850]: A form of dystrophic epidermolysis bullosa characterized by pretibial blisters that develop into prurigo-like hyperkeratotic lesions. It predominantly affects the pretibial areas, sparing the knees and other parts of the skin. Other clinical features include nail dystrophy, albopapuloid skin lesions, and hypertrophic scars without pretibial predominance. The phenotype shows considerable interindividual variability. Inheritance is autosomal dominant. Note: The disease is caused by mutations affecting the gene represented in this entry. Epidermolysis bullosa dystrophica, Bart type (B-DEB) [MIM:132000]: An autosomal dominant form of dystrophic epidermolysis bullosa characterized by congenital localized absence of skin, skin fragility and deformity of nails. Note: The disease is caused by mutations affecting the gene represented in this entry. Epidermolysis bullosa pruriginosa (EBP) [MIM:604129]: A distinct clinical subtype of epidermolysis bullosa dystrophica. It is characterized by skin fragility, blistering, scar formation, intense pruritus and excoriated prurigo nodules. Onset is in early childhood, but in some cases is delayed until the second or third decade of life. Inheritance can be autosomal dominant or recessive. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.34 Ref.38 Nail disorder, non-syndromic congenital, 8 (NDNC8) [MIM:607523]: A nail disorder characterized by isolated toenail dystrophy. The nail changes are most severe in the great toes and consist of the nail plate being buried in the nail bed with a deformed and narrow free edge. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.41 Epidermolysis bullosa dystrophica, with subcorneal cleavage (EBDSC) [MIM:131750]: A bullous skin disorder with variable sized clefts just beneath the level of the stratum corneum. Clinical features include blisters, milia, atrophic scarring, nail dystrophy, and oral and conjunctival involvement, as seen in dystrophic epidermolysis bullosa. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.42
Sequence similarities	Contains 1 BPTI/Kunitz inhibitor domain. Contains 9 fibronectin type-III domains. Contains 2 VWFA domains.
Sequence caution	The sequence BAA02853.1 differs from that shown. Reason: Frameshift at positions 275, 282, 476, 494, 523, 541 and 543.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Epidermolysis bullosa
Domain	Collagen Repeat Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW epidermis development Traceable author statement Ref.14. Source: ProtInc extracellular matrix organization Traceable author statement. Source: Reactome
Cellular_component	basement membrane Traceable author statement Ref.10. Source: ProtInc collagen type VII Traceable author statement Ref.10. Source: ProtInc endoplasmic reticulum lumen Traceable author statement. Source: Reactome
Molecular_function	serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MIA3	Q5JRA6	2	EBI-724237,EBI-2291868

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q02388-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q02388-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1869-1900: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Chain	17 – 2944	2928	Collagen alpha-1(VII) chain		PRO_0000005761
Regions
	Domain	38 – 211	174	VWFA 1
	Domain	231 – 325	95	Fibronectin type-III 1
	Domain	331 – 413	83	Fibronectin type-III 2
	Domain	414 – 503	90	Fibronectin type-III 3
	Domain	507 – 593	87	Fibronectin type-III 4
	Domain	598 – 683	86	Fibronectin type-III 5
	Domain	685 – 771	87	Fibronectin type-III 6
	Domain	775 – 862	88	Fibronectin type-III 7
	Domain	867 – 952	86	Fibronectin type-III 8
	Domain	955 – 1046	92	Fibronectin type-III 9
	Domain	1054 – 1229	176	VWFA 2
	Domain	2872 – 2944	73	BPTI/Kunitz inhibitor
	Region	17 – 1253	1237	Nonhelical region (NC1)
	Region	1254 – 2784	1531	Triple-helical region
	Region	1254 – 1477	224	Interrupted collagenous region
	Region	2785 – 2944	160	Nonhelical region (NC2)
	Motif	1170 – 1172	3	Cell attachment site Potential
	Motif	1334 – 1336	3	Cell attachment site Potential
	Motif	2008 – 2010	3	Cell attachment site Potential
	Motif	2553 – 2555	3	Cell attachment site Potential
Sites
	Site	2886 – 2887	2	Reactive bond By similarity
Amino acid modifications
	Modified residue	2167	1	4-hydroxyproline
	Modified residue	2176	1	4-hydroxyproline
	Modified residue	2185	1	4-hydroxyproline
	Modified residue	2188	1	4-hydroxyproline
	Modified residue	2625	1	5-hydroxylysine; alternate
	Modified residue	2631	1	5-hydroxylysine; alternate
	Modified residue	2664	1	4-hydroxyproline
	Modified residue	2667	1	4-hydroxyproline
	Modified residue	2673	1	4-hydroxyproline
	Glycosylation	337	1	N-linked (GlcNAc...) Potential
	Glycosylation	786	1	N-linked (GlcNAc...) Potential
	Glycosylation	1109	1	N-linked (GlcNAc...) Potential
	Glycosylation	2625	1	O-linked (Gal...); alternate
	Glycosylation	2631	1	O-linked (Gal...); alternate
	Disulfide bond	2634		Interchain Potential
	Disulfide bond	2802		Interchain Potential
	Disulfide bond	2804		Interchain Potential
	Disulfide bond	2876 ↔ 2929		By similarity
	Disulfide bond	2885 ↔ 2912		By similarity
	Disulfide bond	2904 ↔ 2925		By similarity
Natural variations
	Alternative sequence	1869 – 1900	32	Missing in isoform 2.		VSP_024026
	Natural variant	119	1	T → P in a breast cancer sample; somatic mutation. Ref.43		VAR_035740
	Natural variant	142	1	K → R in RDEB.		VAR_001809
	Natural variant	547	1	V → F. Corresponds to variant rs2229823 [ dbSNP | Ensembl ].		VAR_048765
	Natural variant	595	1	P → L in RDEB. Corresponds to variant rs2228561 [ dbSNP | Ensembl ].		VAR_001810
	Natural variant	1120	1	R → K. Corresponds to variant rs2228563 [ dbSNP | Ensembl ].		VAR_048766
	Natural variant	1277	1	P → L in RDEB. Corresponds to variant rs35761247 [ dbSNP | Ensembl ].		VAR_001811
	Natural variant	1347	1	G → R in RDEB; localized type; mild. Ref.26		VAR_011160
	Natural variant	1364	1	P → T in a breast cancer sample; somatic mutation. Ref.43		VAR_035741
	Natural variant	1366	1	R → W in a breast cancer sample; somatic mutation. Ref.43		VAR_035742
	Natural variant	1519	1	G → D in TBDN; compound heterozygous with E-2251; clinically silent when heterozygous with a normal allele. Ref.24 Ref.28		VAR_011161
	Natural variant	1522	1	G → E in DDEB.		VAR_011162
	Natural variant	1557	1	G → R in DDEB.		VAR_001812
	Natural variant	1595	1	G → R in NDNC8. Ref.41		VAR_015519
	Natural variant	1604	1	G → R in RDEB.		VAR_011163
	Natural variant	1652	1	G → R in RDEB; mitis type. Ref.22		VAR_011164
	Natural variant	1703	1	G → E in RDEB.		VAR_011165
	Natural variant	1772	1	R → W in RDEB.		VAR_011166
	Natural variant	1776	1	G → R in DDEB.		VAR_011167
	Natural variant	1782	1	G → R in RDEB; mitis type. Ref.19		VAR_001813
	Natural variant	1791	1	G → E in EBP. Ref.34		VAR_011168
	Natural variant	1812	1	G → R in RDEB. Ref.39		VAR_011169
	Natural variant	1815	1	G → R in NDNC8. Ref.41		VAR_015520
	Natural variant	1845	1	G → R in RDEB. Ref.45		VAR_064994
	Natural variant	1981	1	K → R in RDEB; mild form. Ref.45		VAR_064995
	Natural variant	1982	1	G → W in HS-DEB. Ref.21		VAR_001814
	Natural variant	2003	1	G → R in DDEB. Ref.45		VAR_001815
	Natural variant	2006	1	G → A in DDEB.		VAR_011170
	Natural variant	2006	1	G → D in DDEB; interferes with collagen VII folding and secretion. Ref.24 Ref.32		VAR_011171
	Natural variant	2008	1	R → C in HS-DEB; also in a milder localized type. Ref.25 Ref.32		VAR_011172
	Natural variant	2008	1	R → G in HS-DEB. Ref.21 Ref.32		VAR_001816
	Natural variant	2009	1	G → R in RDEB. Ref.23 Ref.32		VAR_011173
	Natural variant	2015	1	G → E in DDEB; interferes with collagen VII folding and secretion. Ref.24 Ref.32		VAR_011174
	Natural variant	2025	1	G → A in RDEB; mitis type. Ref.21		VAR_001817
	Natural variant	2028	1	G → A in DDEB. Ref.38		VAR_011175
	Natural variant	2028	1	G → R in DDEB and EBP. Ref.37 Ref.38		VAR_011176
	Natural variant	2031	1	G → S in RDEB; severe phenotype. Ref.40		VAR_011177
	Natural variant	2034	1	G → R in DDEB and EBDSC; interferes with collagen VII folding and secretion. Ref.12 Ref.24 Ref.32 Ref.42		VAR_001818
	Natural variant	2034	1	G → W in DDEB. Ref.27 Ref.32		VAR_011178
	Natural variant	2037	1	G → E in P-DEB. Ref.33		VAR_011179
	Natural variant	2040	1	G → D in DDEB. Ref.45		VAR_011180
	Natural variant	2040	1	G → S in P-DEB. Ref.14		VAR_001819
	Natural variant	2040	1	G → V in DDEB. Ref.27		VAR_011181
	Natural variant	2043	1	G → R in DDEB. Ref.16 Ref.23 Ref.27 Ref.32 Ref.45		VAR_001820
	Natural variant	2043	1	G → W in DDEB; localized type. Ref.32		VAR_011182
	Natural variant	2046	1	G → V in DDEB.		VAR_011183
	Natural variant	2049	1	G → E in HS-DEB. Ref.21 Ref.45		VAR_001821
	Natural variant	2055	1	G → E in DDEB.		VAR_001822
	Natural variant	2063	1	R → W in HS-DEB; also in a mild form. Ref.21 Ref.29 Ref.45		VAR_001823
	Natural variant	2064	1	G → R in DDEB. Ref.27 Ref.45		VAR_011184
	Natural variant	2069	1	R → C in RDEB. Ref.45		VAR_064996
	Natural variant	2070	1	G → R in DDEB. Ref.45		VAR_064997
	Natural variant	2073	1	G → D in RDEB; mitis type. Ref.20		VAR_001825
	Natural variant	2076	1	G → D in DDEB; also in recessive forms. Ref.45		VAR_001826
	Natural variant	2079	1	G → E in DDEB. Ref.29		VAR_001827
	Natural variant	2079	1	G → R in DDEB; associated with squamous cell carcinoma. Ref.31		VAR_011185
	Natural variant	2132	1	G → D in RDEB.		VAR_011186
	Natural variant	2192	1	G → S in RDEB.		VAR_011187
	Natural variant	2207	1	G → R in DDEB. Ref.25		VAR_011188
	Natural variant	2221	1	G → A in a patient with recessive dystrophic epidermolysis bullosa. Ref.44		VAR_064998
	Natural variant	2242	1	G → R in EBP. Ref.34		VAR_001828
	Natural variant	2251	1	G → E in TBDN; compound heterozygous with D-1519; leads to isolated toenail dystrophy when heterozygous with a normal allele. Ref.28		VAR_011189
	Natural variant	2263	1	G → V in RDEB.		VAR_011190
	Natural variant	2287	1	G → R in a compound heterozygote affected by moderately severe dystrophic epidermolysis bullosa; in combination with R-2316; leads to isolated toenail dystrophy when heterozygous with a normal allele. Ref.35		VAR_011191
	Natural variant	2296	1	G → E in RDEB. Ref.45		VAR_064999
	Natural variant	2316	1	G → R in a compound heterozygote affected by moderately severe dystrophic epidermolysis bullosa; in combination with R-2287. Ref.35		VAR_011192
	Natural variant	2348	1	G → R in DDEB/RDEB; mild form. Ref.30		VAR_011193
	Natural variant	2351	1	G → R in a patient with dystrophic epidermolysis bullosa; mitis type. Corresponds to variant rs1800013 [ dbSNP | Ensembl ].		VAR_001829
	Natural variant	2366	1	G → S in RDEB; mitis type. Ref.29		VAR_011194
	Natural variant	2369	1	G → S in EBP. Ref.34		VAR_011195
	Natural variant	2429	1	P → L. Corresponds to variant rs2229822 [ dbSNP | Ensembl ].		VAR_033786
	Natural variant	2557	1	G → R in RDEB. Ref.45		VAR_065000
	Natural variant	2569	1	G → R in RDEB; severe and mitis type.		VAR_001830
	Natural variant	2575	1	G → R in HS-DEB; also in a mild form. Ref.18 Ref.21		VAR_001831
	Natural variant	2622	1	R → W in RDEB. Ref.45		VAR_065001
	Natural variant	2623	1	G → C in PR-DEB; dominant. Ref.15		VAR_001832
	Natural variant	2653	1	G → R in RDEB; mitis type.		VAR_001833
	Natural variant	2671	1	G → V in RDEB.		VAR_001834
	Natural variant	2674	1	G → D in RDEB.		VAR_011196
	Natural variant	2674	1	G → R in RDEB; mitis type.		VAR_001835
	Natural variant	2713	1	G → D in DDEB. Ref.27		VAR_011197
	Natural variant	2713	1	G → R in EBP. Ref.34		VAR_011198
	Natural variant	2740	1	G → A in RDEB.		VAR_011199
	Natural variant	2749	1	G → R in HS-DEB; also in a mild form.		VAR_001836
	Natural variant	2775	1	G → S in RDEB; mitis type. Ref.25		VAR_011200
	Natural variant	2791	1	R → W in DDEB.		VAR_011201
	Natural variant	2798	1	M → K in HS-DEB; also in a mild form; the anchoring fibrils may be absent. Ref.13		VAR_001837
Experimental info
	Sequence conflict	195 – 197	3	FFF → EFR in BAA02853. Ref.4
	Sequence conflict	369 – 371	3	QQQ → EFR in AAA36357. Ref.5
	Sequence conflict	369 – 371	3	QQQ → EFR in AAB24637. Ref.5
	Sequence conflict	518 – 519	2	EL → DV in AAA36357. Ref.5
	Sequence conflict	518 – 519	2	EL → DV in AAB24637. Ref.5
	Sequence conflict	529	1	S → C in BAA02853. Ref.4
	Sequence conflict	541	1	V → W in AAA36357. Ref.5
	Sequence conflict	541	1	V → W in AAB24637. Ref.5
	Sequence conflict	851	1	R → H in BAA02853. Ref.4
	Sequence conflict	893	1	A → E in AAA58965. Ref.1
	Sequence conflict	893	1	A → E in BAA02853. Ref.4
	Sequence conflict	893	1	A → E in AAA96439. Ref.6
	Sequence conflict	1122	1	R → L in BAA02853. Ref.4
	Sequence conflict	1463 – 1464	2	SP → LR AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 96D8BF6D0FD387DB	FASTA	2,944	295,220
	10 20 30 40 50 60 MTLRLLVAAL CAGILAEAPR VRAQHRERVT CTRLYAADIV FLLDGSSSIG RSNFREVRSF 70 80 90 100 110 120 LEGLVLPFSG AASAQGVRFA TVQYSDDPRT EFGLDALGSG GDVIRAIREL SYKGGNTRTG 130 140 150 160 170 180 AAILHVADHV FLPQLARPGV PKVCILITDG KSQDLVDTAA QRLKGQGVKL FAVGIKNADP 190 200 210 220 230 240 EELKRVASQP TSDFFFFVND FSILRTLLPL VSRRVCTTAG GVPVTRPPDD STSAPRDLVL 250 260 270 280 290 300 SEPSSQSLRV QWTAASGPVT GYKVQYTPLT GLGQPLPSER QEVNVPAGET SVRLRGLRPL 310 320 330 340 350 360 TEYQVTVIAL YANSIGEAVS GTARTTALEG PELTIQNTTA HSLLVAWRSV PGATGYRVTW 370 380 390 400 410 420 RVLSGGPTQQ QELGPGQGSV LLRDLEPGTD YEVTVSTLFG RSVGPATSLM ARTDASVEQT 430 440 450 460 470 480 LRPVILGPTS ILLSWNLVPE ARGYRLEWRR ETGLEPPQKV VLPSDVTRYQ LDGLQPGTEY 490 500 510 520 530 540 RLTLYTLLEG HEVATPATVV PTGPELPVSP VTDLQATELP GQRVRVSWSP VPGATQYRII 550 560 570 580 590 600 VRSTQGVERT LVLPGSQTAF DLDDVQAGLS YTVRVSARVG PREGSASVLT VRREPETPLA 610 620 630 640 650 660 VPGLRVVVSD ATRVRVAWGP VPGASGFRIS WSTGSGPESS QTLPPDSTAT DITGLQPGTT 670 680 690 700 710 720 YQVAVSVLRG REEGPAAVIV ARTDPLGPVR TVHVTQASSS SVTITWTRVP GATGYRVSWH 730 740 750 760 770 780 SAHGPEKSQL VSGEATVAEL DGLEPDTEYT VHVRAHVAGV DGPPASVVVR TAPEPVGRVS 790 800 810 820 830 840 RLQILNASSD VLRITWVGVT GATAYRLAWG RSEGGPMRHQ ILPGNTDSAE IRGLEGGVSY 850 860 870 880 890 900 SVRVTALVGD REGTPVSIVV TTPPEAPPAL GTLHVVQRGE HSLRLRWEPV PRAQGFLLHW 910 920 930 940 950 960 QPEGGQEQSR VLGPELSSYH LDGLEPATQY RVRLSVLGPA GEGPSAEVTA RTESPRVPSI 970 980 990 1000 1010 1020 ELRVVDTSID SVTLAWTPVS RASSYILSWR PLRGPGQEVP GSPQTLPGIS SSQRVTGLEP 1030 1040 1050 1060 1070 1080 GVSYIFSLTP VLDGVRGPEA SVTQTPVCPR GLADVVFLPH ATQDNAHRAE ATRRVLERLV 1090 1100 1110 1120 1130 1140 LALGPLGPQA VQVGLLSYSH RPSPLFPLNG SHDLGIILQR IRDMPYMDPS GNNLGTAVVT 1150 1160 1170 1180 1190 1200 AHRYMLAPDA PGRRQHVPGV MVLLVDEPLR GDIFSPIREA QASGLNVVML GMAGADPEQL 1210 1220 1230 1240 1250 1260 RRLAPGMDSV QTFFAVDDGP SLDQAVSGLA TALCQASFTT QPRPEPCPVY CPKGQKGEPG 1270 1280 1290 1300 1310 1320 EMGLRGQVGP PGDPGLPGRT GAPGPQGPPG SATAKGERGF PGADGRPGSP GRAGNPGTPG 1330 1340 1350 1360 1370 1380 APGLKGSPGL PGPRGDPGER GPRGPKGEPG APGQVIGGEG PGLPGRKGDP GPSGPPGPRG 1390 1400 1410 1420 1430 1440 PLGDPGPRGP PGLPGTAMKG DKGDRGERGP PGPGEGGIAP GEPGLPGLPG SPGPQGPVGP 1450 1460 1470 1480 1490 1500 PGKKGEKGDS EDGAPGLPGQ PGSPGEQGPR GPPGAIGPKG DRGFPGPLGE AGEKGERGPP 1510 1520 1530 1540 1550 1560 GPAGSRGLPG VAGRPGAKGP EGPPGPTGRQ GEKGEPGRPG DPAVVGPAVA GPKGEKGDVG 1570 1580 1590 1600 1610 1620 PAGPRGATGV QGERGPPGLV LPGDPGPKGD PGDRGPIGLT GRAGPPGDSG PPGEKGDPGR 1630 1640 1650 1660 1670 1680 PGPPGPVGPR GRDGEVGEKG DEGPPGDPGL PGKAGERGLR GAPGVRGPVG EKGDQGDPGE 1690 1700 1710 1720 1730 1740 DGRNGSPGSS GPKGDRGEPG PPGPPGRLVD TGPGAREKGE PGDRGQEGPR GPKGDPGLPG 1750 1760 1770 1780 1790 1800 APGERGIEGF RGPPGPQGDP GVRGPAGEKG DRGPPGLDGR SGLDGKPGAA GPSGPNGAAG 1810 1820 1830 1840 1850 1860 KAGDPGRDGL PGLRGEQGLP GPSGPPGLPG KPGEDGKPGL NGKNGEPGDP GEDGRKGEKG 1870 1880 1890 1900 1910 1920 DSGASGREGR DGPKGERGAP GILGPQGPPG LPGPVGPPGQ GFPGVPGGTG PKGDRGETGS 1930 1940 1950 1960 1970 1980 KGEQGLPGER GLRGEPGSVP NVDRLLETAG IKASALREIV ETWDESSGSF LPVPERRRGP 1990 2000 2010 2020 2030 2040 KGDSGEQGPP GKEGPIGFPG ERGLKGDRGD PGPQGPPGLA LGERGPPGPS GLAGEPGKPG 2050 2060 2070 2080 2090 2100 IPGLPGRAGG VGEAGRPGER GERGEKGERG EQGRDGPPGL PGTPGPPGPP GPKVSVDEPG 2110 2120 2130 2140 2150 2160 PGLSGEQGPP GLKGAKGEPG SNGDQGPKGD RGVPGIKGDR GEPGPRGQDG NPGLPGERGM 2170 2180 2190 2200 2210 2220 AGPEGKPGLQ GPRGPPGPVG GHGDPGPPGA PGLAGPAGPQ GPSGLKGEPG ETGPPGRGLT 2230 2240 2250 2260 2270 2280 GPTGAVGLPG PPGPSGLVGP QGSPGLPGQV GETGKPGAPG RDGASGKDGD RGSPGVPGSP 2290 2300 2310 2320 2330 2340 GLPGPVGPKG EPGPTGAPGQ AVVGLPGAKG EKGAPGGLAG DLVGEPGAKG DRGLPGPRGE 2350 2360 2370 2380 2390 2400 KGEAGRAGEP GDPGEDGQKG APGPKGFKGD PGVGVPGSPG PPGPPGVKGD LGLPGLPGAP 2410 2420 2430 2440 2450 2460 GVVGFPGQTG PRGEMGQPGP SGERGLAGPP GREGIPGPLG PPGPPGSVGP PGASGLKGDK 2470 2480 2490 2500 2510 2520 GDPGVGLPGP RGERGEPGIR GEDGRPGQEG PRGLTGPPGS RGERGEKGDV GSAGLKGDKG 2530 2540 2550 2560 2570 2580 DSAVILGPPG PRGAKGDMGE RGPRGLDGDK GPRGDNGDPG DKGSKGEPGD KGSAGLPGLR 2590 2600 2610 2620 2630 2640 GLLGPQGQPG AAGIPGDPGS PGKDGVPGIR GEKGDVGFMG PRGLKGERGV KGACGLDGEK 2650 2660 2670 2680 2690 2700 GDKGEAGPPG RPGLAGHKGE MGEPGVPGQS GAPGKEGLIG PKGDRGFDGQ PGPKGDQGEK 2710 2720 2730 2740 2750 2760 GERGTPGIGG FPGPSGNDGS AGPPGPPGSV GPRGPEGLQG QKGERGPPGE RVVGAPGVPG 2770 2780 2790 2800 2810 2820 APGERGEQGR PGPAGPRGEK GEAALTEDDI RGFVRQEMSQ HCACQGQFIA SGSRPLPSYA 2830 2840 2850 2860 2870 2880 ADTAGSQLHA VPVLRVSHAE EEERVPPEDD EYSEYSEYSV EEYQDPEAPW DSDDPCSLPL 2890 2900 2910 2920 2930 2940 DEGSCTAYTL RWYHRAVTGS TEACHPFVYG GCGGNANRFG TREACERRCP PRVVQSQGTG TAQD
	Isoform 2 [UniParc]. Checksum: C206B8957E4333A2	FASTA	2,912	292,267
	10 20 30 40 50 60 MTLRLLVAAL CAGILAEAPR VRAQHRERVT CTRLYAADIV FLLDGSSSIG RSNFREVRSF 70 80 90 100 110 120 LEGLVLPFSG AASAQGVRFA TVQYSDDPRT EFGLDALGSG GDVIRAIREL SYKGGNTRTG 130 140 150 160 170 180 AAILHVADHV FLPQLARPGV PKVCILITDG KSQDLVDTAA QRLKGQGVKL FAVGIKNADP 190 200 210 220 230 240 EELKRVASQP TSDFFFFVND FSILRTLLPL VSRRVCTTAG GVPVTRPPDD STSAPRDLVL 250 260 270 280 290 300 SEPSSQSLRV QWTAASGPVT GYKVQYTPLT GLGQPLPSER QEVNVPAGET SVRLRGLRPL 310 320 330 340 350 360 TEYQVTVIAL YANSIGEAVS GTARTTALEG PELTIQNTTA HSLLVAWRSV PGATGYRVTW 370 380 390 400 410 420 RVLSGGPTQQ QELGPGQGSV LLRDLEPGTD YEVTVSTLFG RSVGPATSLM ARTDASVEQT 430 440 450 460 470 480 LRPVILGPTS ILLSWNLVPE ARGYRLEWRR ETGLEPPQKV VLPSDVTRYQ LDGLQPGTEY 490 500 510 520 530 540 RLTLYTLLEG HEVATPATVV PTGPELPVSP VTDLQATELP GQRVRVSWSP VPGATQYRII 550 560 570 580 590 600 VRSTQGVERT LVLPGSQTAF DLDDVQAGLS YTVRVSARVG PREGSASVLT VRREPETPLA 610 620 630 640 650 660 VPGLRVVVSD ATRVRVAWGP VPGASGFRIS WSTGSGPESS QTLPPDSTAT DITGLQPGTT 670 680 690 700 710 720 YQVAVSVLRG REEGPAAVIV ARTDPLGPVR TVHVTQASSS SVTITWTRVP GATGYRVSWH 730 740 750 760 770 780 SAHGPEKSQL VSGEATVAEL DGLEPDTEYT VHVRAHVAGV DGPPASVVVR TAPEPVGRVS 790 800 810 820 830 840 RLQILNASSD VLRITWVGVT GATAYRLAWG RSEGGPMRHQ ILPGNTDSAE IRGLEGGVSY 850 860 870 880 890 900 SVRVTALVGD REGTPVSIVV TTPPEAPPAL GTLHVVQRGE HSLRLRWEPV PRAQGFLLHW 910 920 930 940 950 960 QPEGGQEQSR VLGPELSSYH LDGLEPATQY RVRLSVLGPA GEGPSAEVTA RTESPRVPSI 970 980 990 1000 1010 1020 ELRVVDTSID SVTLAWTPVS RASSYILSWR PLRGPGQEVP GSPQTLPGIS SSQRVTGLEP 1030 1040 1050 1060 1070 1080 GVSYIFSLTP VLDGVRGPEA SVTQTPVCPR GLADVVFLPH ATQDNAHRAE ATRRVLERLV 1090 1100 1110 1120 1130 1140 LALGPLGPQA VQVGLLSYSH RPSPLFPLNG SHDLGIILQR IRDMPYMDPS GNNLGTAVVT 1150 1160 1170 1180 1190 1200 AHRYMLAPDA PGRRQHVPGV MVLLVDEPLR GDIFSPIREA QASGLNVVML GMAGADPEQL 1210 1220 1230 1240 1250 1260 RRLAPGMDSV QTFFAVDDGP SLDQAVSGLA TALCQASFTT QPRPEPCPVY CPKGQKGEPG 1270 1280 1290 1300 1310 1320 EMGLRGQVGP PGDPGLPGRT GAPGPQGPPG SATAKGERGF PGADGRPGSP GRAGNPGTPG 1330 1340 1350 1360 1370 1380 APGLKGSPGL PGPRGDPGER GPRGPKGEPG APGQVIGGEG PGLPGRKGDP GPSGPPGPRG 1390 1400 1410 1420 1430 1440 PLGDPGPRGP PGLPGTAMKG DKGDRGERGP PGPGEGGIAP GEPGLPGLPG SPGPQGPVGP 1450 1460 1470 1480 1490 1500 PGKKGEKGDS EDGAPGLPGQ PGSPGEQGPR GPPGAIGPKG DRGFPGPLGE AGEKGERGPP 1510 1520 1530 1540 1550 1560 GPAGSRGLPG VAGRPGAKGP EGPPGPTGRQ GEKGEPGRPG DPAVVGPAVA GPKGEKGDVG 1570 1580 1590 1600 1610 1620 PAGPRGATGV QGERGPPGLV LPGDPGPKGD PGDRGPIGLT GRAGPPGDSG PPGEKGDPGR 1630 1640 1650 1660 1670 1680 PGPPGPVGPR GRDGEVGEKG DEGPPGDPGL PGKAGERGLR GAPGVRGPVG EKGDQGDPGE 1690 1700 1710 1720 1730 1740 DGRNGSPGSS GPKGDRGEPG PPGPPGRLVD TGPGAREKGE PGDRGQEGPR GPKGDPGLPG 1750 1760 1770 1780 1790 1800 APGERGIEGF RGPPGPQGDP GVRGPAGEKG DRGPPGLDGR SGLDGKPGAA GPSGPNGAAG 1810 1820 1830 1840 1850 1860 KAGDPGRDGL PGLRGEQGLP GPSGPPGLPG KPGEDGKPGL NGKNGEPGDP GEDGRKGEKG 1870 1880 1890 1900 1910 1920 DSGASGREGF PGVPGGTGPK GDRGETGSKG EQGLPGERGL RGEPGSVPNV DRLLETAGIK 1930 1940 1950 1960 1970 1980 ASALREIVET WDESSGSFLP VPERRRGPKG DSGEQGPPGK EGPIGFPGER GLKGDRGDPG 1990 2000 2010 2020 2030 2040 PQGPPGLALG ERGPPGPSGL AGEPGKPGIP GLPGRAGGVG EAGRPGERGE RGEKGERGEQ 2050 2060 2070 2080 2090 2100 GRDGPPGLPG TPGPPGPPGP KVSVDEPGPG LSGEQGPPGL KGAKGEPGSN GDQGPKGDRG 2110 2120 2130 2140 2150 2160 VPGIKGDRGE PGPRGQDGNP GLPGERGMAG PEGKPGLQGP RGPPGPVGGH GDPGPPGAPG 2170 2180 2190 2200 2210 2220 LAGPAGPQGP SGLKGEPGET GPPGRGLTGP TGAVGLPGPP GPSGLVGPQG SPGLPGQVGE 2230 2240 2250 2260 2270 2280 TGKPGAPGRD GASGKDGDRG SPGVPGSPGL PGPVGPKGEP GPTGAPGQAV VGLPGAKGEK 2290 2300 2310 2320 2330 2340 GAPGGLAGDL VGEPGAKGDR GLPGPRGEKG EAGRAGEPGD PGEDGQKGAP GPKGFKGDPG 2350 2360 2370 2380 2390 2400 VGVPGSPGPP GPPGVKGDLG LPGLPGAPGV VGFPGQTGPR GEMGQPGPSG ERGLAGPPGR 2410 2420 2430 2440 2450 2460 EGIPGPLGPP GPPGSVGPPG ASGLKGDKGD PGVGLPGPRG ERGEPGIRGE DGRPGQEGPR 2470 2480 2490 2500 2510 2520 GLTGPPGSRG ERGEKGDVGS AGLKGDKGDS AVILGPPGPR GAKGDMGERG PRGLDGDKGP 2530 2540 2550 2560 2570 2580 RGDNGDPGDK GSKGEPGDKG SAGLPGLRGL LGPQGQPGAA GIPGDPGSPG KDGVPGIRGE 2590 2600 2610 2620 2630 2640 KGDVGFMGPR GLKGERGVKG ACGLDGEKGD KGEAGPPGRP GLAGHKGEMG EPGVPGQSGA 2650 2660 2670 2680 2690 2700 PGKEGLIGPK GDRGFDGQPG PKGDQGEKGE RGTPGIGGFP GPSGNDGSAG PPGPPGSVGP 2710 2720 2730 2740 2750 2760 RGPEGLQGQK GERGPPGERV VGAPGVPGAP GERGEQGRPG PAGPRGEKGE AALTEDDIRG 2770 2780 2790 2800 2810 2820 FVRQEMSQHC ACQGQFIASG SRPLPSYAAD TAGSQLHAVP VLRVSHAEEE ERVPPEDDEY 2830 2840 2850 2860 2870 2880 SEYSEYSVEE YQDPEAPWDS DDPCSLPLDE GSCTAYTLRW YHRAVTGSTE ACHPFVYGGC 2890 2900 2910 GGNANRFGTR EACERRCPPR VVQSQGTGTA QD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural organization of the human type VII collagen gene (COL7A1), composed of more exons than any previously characterized gene." Christiano A.M., Hoffman G.G., Chung-Honet L.C., Lee S., Cheng W., Uitto J., Greenspan D.S. Genomics 21:169-179(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2). Tissue: Placenta.
[2]	"Cloning of human type VII collagen. Complete primary sequence of the alpha 1(VII) chain and identification of intragenic polymorphisms." Christiano A.M., Greenspan D.S., Lee S., Uitto J. J. Biol. Chem. 269:20256-20262(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"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." Christiano A.M., Rosenbaum L.M., Chung-Honet L.C., Parente M.G., Woodley D.T., Pan T.C., Zhang R.Z., Chu M.-L., Burgeson R.E., Uitto J. Hum. Mol. Genet. 1:475-481(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 128-1493, PARTIAL PROTEIN SEQUENCE.
[4]	"Molecular cloning and characterization of type VII collagen cDNA." Tanaka T., Takahashi K., Furukawa F., Imamura S. Biochem. Biophys. Res. Commun. 183:958-963(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 195-1275. Tissue: Keratinocyte.
[5]	"Noncollagenous (NC1) domain of collagen VII resembles multidomain adhesion proteins involved in tissue-specific organization of extracellular matrix." Gammon W.R., Abernethy M.L., Padilla K.M., Prisayanh P.S., Cook M.E., Wright J., Briggaman R.A., Hunt S.W. III J. Invest. Dermatol. 99:691-696(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 369-1255.
[6]	"Human type VII collagen: cDNA cloning and chromosomal mapping of the gene." Parente M.G., Chung L.C., Ryynaenen J., Woodley D.T., Wynn K.W., Bauer E.A., Mattei M.-G., Chu M.-L., Uitto J. Proc. Natl. Acad. Sci. U.S.A. 88:6931-6935(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 815-1439.
[7]	"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." Greenspan D.S. Hum. Mol. Genet. 2:273-278(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2395-2944.
[8]	"Cleavage of type VII collagen by interstitial collagenase and type IV collagenase (gelatinase) derived from human skin." Seltzer J.L., Eisen A.Z., Bauer E.A., Morris N.P., Glanville R.W., Burgeson R.E. J. Biol. Chem. 264:3822-3826(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[9]	"TANGO1 facilitates cargo loading at endoplasmic reticulum exit sites." Saito K., Chen M., Bard F., Chen S., Zhou H., Woodley D., Polischuk R., Schekman R., Malhotra V. Cell 136:891-902(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MIA3.
[10]	"Molecular basis of dystrophic epidermolysis bullosa: mutations in the type VII collagen gene (COL7A1)." Jaervikallio A., Pulkkinen L., Uitto J. Hum. Mutat. 10:338-347(1997) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Epidermolysis bullosa simplex superficialis. A new variant of epidermolysis bullosa characterized by subcorneal skin cleavage mimicking peeling skin syndrome." Fine J.-D., Johnson L., Wright T. Arch. Dermatol. 125:633-638(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT EBDSC ARG-2034.
[13]	"A missense mutation in type VII collagen in two affected siblings with recessive dystrophic epidermolysis bullosa." Christiano A.M., Greenspan D.S., Hoffman G.G., Zhang X., Tamai Y., Lin A.N., Dietz H.C., Hovnanian A., Uitto J. Nat. Genet. 4:62-66(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HS-DEB LYS-2798.
[14]	"Dominant dystrophic epidermolysis bullosa: identification of a Gly-->Ser substitution in the triple-helical domain of type VII collagen." Christiano A.M., Ryynaenen M., Uitto J. Proc. Natl. Acad. Sci. U.S.A. 91:3549-3553(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT P-DEB SER-2040.
[15]	"Pretibial epidermolysis bullosa: genetic linkage to COL7A1 and identification of a glycine-to-cysteine substitution in the triple-helical domain of type VII collagen." Christiano A.M., Lee J.Y.-Y., Chen W.J., Laforgia S., Uitto J. Hum. Mol. Genet. 4:1579-1583(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PR-DEB CYS-2623.
[16]	"A glycine-to-arginine substitution in the triple-helical domain of type VII collagen in a family with dominant dystrophic epidermolysis bullosa." Christiano A.M., Morricone A., Paradisi M., Angelo C., Mazzanti C., Cavalieri R., Uitto J. J. Invest. Dermatol. 104:438-440(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDEB ARG-2043.
[17]	"Glycine substitutions in the triple-helical region of type VII collagen result in a spectrum of dystrophic epidermolysis bullosa phenotypes and patterns of inheritance." Christiano A.M., McGrath J.A., Tan K.C., Uitto J. Am. J. Hum. Genet. 58:671-681(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DEB.
[18]	"Molecular basis of recessive dystrophic epidermolysis bullosa: genotype/phenotype correlation in a case of moderate clinical severity." Shimizu H., McGrath J.A., Christiano A.M., Nishikawa T., Uitto J. J. Invest. Dermatol. 106:119-124(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HS-DEB ARG-2575.
[19]	"Influence of the second COL7A1 mutation in determining the phenotypic severity of recessive dystrophic epidermolysis bullosa." Christiano A.M., McGrath J.A., Uitto J. J. Invest. Dermatol. 106:766-770(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RDEB ARG-1782.
[20]	"Clinicopathological correlations of compound heterozygous COL7A1 mutations in recessive dystrophic epidermolysis bullosa." Dunnill M.G.S., McGrath J.A., Richards A.J., Christiano A.M., Uitto J., Pope F.M., Eady R.A.J. J. Invest. Dermatol. 107:171-177(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RDEB ASP-2073.
[21]	"Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechanisms underlying defective anchoring fibril formation." Hovnanian A., Rochat A., Bodemer C., Petit E., Rivers C.A., Prost C., Fraitag S., Christiano A.M., Uitto J., Lathrop M., Barrandon Y., de Prost Y. Am. J. Hum. Genet. 61:599-610(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS HS-DEB TRP-1982; GLY-2008; ALA-2025; GLU-2049; TRP-2063 AND ARG-2575.
[22]	"Identification of a glycine substitution and a splice site mutation in the type VII collagen gene in a proband with mitis recessive dystrophic epidermolysis bullosa." Cserhalmi-Friedman P.B., Karpati S., Horvath A., Christiano A.M. Arch. Dermatol. Res. 289:640-645(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RDEB ARG-1652.
[23]	"Modulation of disease severity of dystrophic epidermolysis bullosa by a splice site mutation in combination with a missense mutation in the COL7A1 gene." Winberg J.-O., Hammami-Hauasli N., Nilssen O., Anton-Lamprecht I., Naylor S.L., Kerbacher K., Zimmermann M., Krajci P., Gedde-Dahl T. Jr., Bruckner-Tuderman L. Hum. Mol. Genet. 6:1125-1135(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RDEB ARG-2009, VARIANT DDEB ARG-2043.
[24]	"Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering." Hammami-Hauasli N., Schumann H., Raghunath M., Kilgus O., Luethi U., Luger T., Bruckner-Tuderman L. J. Biol. Chem. 273:19228-19234(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DDEB ASP-1519; ASP-2006; GLU-2015 AND ARG-2034.
[25]	"Novel COL7A1 mutations in dystrophic forms of epidermolysis bullosa." Kon A., Pulkkinen L., Ishida-Yamamoto A., Hashimoto I., Uitto J. J. Invest. Dermatol. 111:534-537(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HS-DEB CYS-2008, VARIANT DDEB ARG-2207, VARIANT RDEB SER-2775.
[26]	"Compound heterozygosity for a recessive glycine substitution and a splice site mutation in the COL7A1 gene causes an unusually mild form of localized recessive dystrophic epidermolysis bullosa." Terracina M., Posteraro P., Schubert M., Sonego G., Atzori F., Zambruno G., Bruckner-Tuderman L., Castiglia D. J. Invest. Dermatol. 111:744-750(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RDEB ARG-1347.
[27]	"Novel and de novo glycine substitution mutations in the type VII collagen gene (COL7A1) in dystrophic epidermolysis bullosa: implications for genetic counseling." Rouan F., Pulkkinen L., Jonkman M.F., Bauer J.W., Cserhalmi-Friedman P.B., Christiano A.M., Uitto J. J. Invest. Dermatol. 111:1210-1213(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DDEB TRP-2034; VAL-2040; ARG-2043; ARG-2064 AND ASP-2713.
[28]	"Transient bullous dermolysis of the newborn associated with compound heterozygosity for recessive and dominant COL7A1 mutations." Hammami-Hauasli N., Raghunath M., Kuester W., Bruckner-Tuderman L. J. Invest. Dermatol. 111:1214-1219(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TBDN ASP-1519 AND GLU-2251.
[29]	"Diagnostic dilemma of 'sporadic' cases of dystrophic epidermolysis bullosa: a new dominant or mitis recessive mutation?" Hashimoto I., Kon A., Tamai K., Uitto J. Exp. Dermatol. 8:140-142(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DDEB/RDEB TRP-2063 AND SER-2366, VARIANT DDEB GLU-2079.
[30]	"Identification of a de novo glycine substitution in the type VII collagen gene in a proband with mild dystrophic epidermolysis bullosa." Cserhalmi-Friedman P.B., Grossman J., Karpati S., Ahmad W., Horvath A., Christiano A.M. Exp. Dermatol. 8:143-145(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDEB/RDEB ARG-2348.
[31]	"Squamous cell carcinoma in a family with dominant dystrophic epidermolysis bullosa: a molecular genetic study." Christiano A.M., Crollick J., Pincus S., Uitto J. Exp. Dermatol. 8:146-152(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDEB ARG-2079.
[32]	"Clustering of COL7A1 mutations in exon 73: implications for mutation analysis in dystrophic epidermolysis bullosa." Mecklenbeck S., Hammami-Hauasli N., Hoepfner B., Schumann H., Kramer A., Kuester W., Bruckner-Tuderman L. J. Invest. Dermatol. 112:398-400(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DDEB ASP-2006; GLU-2015; ARG-2034; TRP-2034; ARG-2043 AND TRP-2043, VARIANTS HS-DEB CYS-2008 AND GLY-2008, VARIANT RDEB ARG-2009.
[33]	"Dominant dystrophic epidermolysis bullosa (Pasini) caused by a novel glycine substitution mutation in the type VII collagen gene (COL7A1)." Jonkman M.F., Moreno G., Rouan F., Oranje A.P., Pulkkinen L., Uitto J. J. Invest. Dermatol. 112:815-817(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT P-DEB GLU-2037.
[34]	"Allelic heterogeneity of dominant and recessive COL7A1 mutations underlying epidermolysis bullosa pruriginosa." Mellerio J.E., Ashton G.H.S., Mohammedi R., Lyon C.C., Kirby B., Harman K.E., Salas-Alanis J.C., Atherton D.J., Harrison P.V., Griffiths W.A.D., Black M.M., Eady R.A.J., McGrath J.A. J. Invest. Dermatol. 112:984-987(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS EBP GLU-1791; ARG-2242; SER-2369 AND ARG-2713.
[35]	"Compound heterozygosity for silent and dominant glycine substitution mutations in COL7A1 leads to a marked transient intracytoplasmic retention of procollagen VII and a moderately severe dystrophic epidermolysis bullosa phenotype." Shimizu H., Hammami-Hauasli N., Hatta N., Nishikawa T., Bruckner-Tuderman L. J. Invest. Dermatol. 113:419-421(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARG-2287 AND ARG-2316.
[36]	"Comparative mutation detection screening of the type VII collagen gene (COL7A1) using the protein truncation test, fluorescent chemical cleavage of mismatch, and conformation sensitive gel electrophoresis." Whittock N.V., Ashton G.H.S., Mohammedi R., Mellerio J.E., Mathew C.G., Abbs S.J., Eady R.A.J., McGrath J.A. J. Invest. Dermatol. 113:673-686(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DEB.
[37]	"A de novo glycine substitution mutation in the collagenous domain of COL7A1 in dominant dystrophic epidermolysis bullosa." Lee J.Y.-Y., Li C., Chao S.-C., Pulkkinen L., Uitto J. Arch. Dermatol. Res. 292:159-163(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDEB ARG-2028.
[38]	"Glycine substitution mutations by different amino acids in the same codon of COL7A1 lead to heterogeneous clinical phenotypes of dominant dystrophic epidermolysis bullosa." Murata T., Masunaga T., Shimizu H., Takizawa Y., Ishiko A., Hatta N., Nishikawa T. Arch. Dermatol. Res. 292:477-481(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT DDEB ALA-2028, VARIANT EBP ARG-2028.
[39]	"Combination of novel premature termination codon and glycine substitution mutations in COL7A1 leads to moderately severe recessive dystrophic epidermolysis bullosa." Masunaga T., Shimizu H., Takizawa Y., Uitto J., Nishikawa T. J. Invest. Dermatol. 114:204-205(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RDEB ARG-1812.
[40]	"Generalized dystrophic epidermolysis bullosa: identification of a novel, homozygous glycine substitution, G2031S, in exon 73 of COL7A1 in monozygous triplets." Nordal E.J., Mecklenbeck S., Hausser I., Skranes J., Bruckner-Tuderman L., Gedde-Dahl T. Jr. Br. J. Dermatol. 144:151-157(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RDEB SER-2031.
[41]	"Toenail dystrophy with COL7A1 glycine substitution mutations segregates as an autosomal dominant trait in 2 families with dystrophic epidermolysis bullosa." Sato-Matsumura K.C., Yasukawa K., Tomita Y., Shimizu H. Arch. Dermatol. 138:269-271(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS NDNC8 ARG-1595 AND ARG-1815.
[42]	"EB simplex superficialis resulting from a mutation in the type VII collagen gene." Martinez-Mir A., Liu J., Gordon D., Weiner M.S., Ahmad W., Fine J.D., Ott J., Gilliam T.C., Christiano A.M. J. Invest. Dermatol. 118:547-549(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT EBDSC ARG-2034.
[43]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-119; THR-1364 AND TRP-1366.
[44]	"Novel human pathological mutations. Gene symbol: COL7A1. Disease: Epidermolysis bullosa dystrophica." Garcia M., Escamez M.J., Cuadrado-Corrales N., Sanchez-Jimeno C., Illera N., Lopez-Martinez M.A., Trujillo-Tiebas M.J., Ayuso C., Del Rio M. Hum. Genet. 127:116-117(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-2221.
[45]	"Analysis of the COL7A1 gene in Czech patients with dystrophic epidermolysis bullosa reveals novel and recurrent mutations." Jerabkova B., Kopeckova L., Buckova H., Vesely K., Valickova J., Fajkusova L. J. Dermatol. Sci. 59:136-140(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RDEB ARG-1845; ARG-1981; GLU-2049; TRP-2063; CYS-2069; GLU-2296; ARG-2557 AND TRP-2622, VARIANTS DDEB ARG-2003; ASP-2040; ARG-2043; ARG-2064; ARG-2070 AND ASP-2076.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	L23982 Genomic DNA. Translation: AAA58965.1. L02870 mRNA. Translation: AAA75438.1. D13694 mRNA. Translation: BAA02853.1. Frameshift. M96984 mRNA. Translation: AAA36357.2. S51236 mRNA. Translation: AAB24637.1. M65158 mRNA. Translation: AAA96439.1. L06862 mRNA. Translation: AAA89196.1.
IPI	IPI00025418. IPI00795118.
PIR	A54849.
RefSeq	NP_000085.1. NM_000094.3.
UniGene	Hs.476218.
3D structure databases
ProteinModelPortal	Q02388.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q02388. 6 interactions.
MINT	MINT-1390694.
STRING	9606.ENSP00000332371.
Protein family/group databases
MEROPS	I02.967.
PTM databases
PhosphoSite	Q02388.
Polymorphism databases
DMDM	1345650.
Proteomic databases
PaxDb	Q02388.
PRIDE	Q02388.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000328333; ENSP00000332371; ENSG00000114270. ENST00000454817; ENSP00000412569; ENSG00000114270.
GeneID	1294.
KEGG	hsa:1294.
UCSC	uc003ctz.2. human.
Organism-specific databases
CTD	1294.
GeneCards	GC03M048576.
HGNC	HGNC:2214. COL7A1.
HPA	CAB016357.
MIM	120120. gene. 131705. phenotype. 131750. phenotype. 131850. phenotype. 132000. phenotype. 226600. phenotype. 604129. phenotype. 607523. phenotype.
neXtProt	NX_Q02388.
Orphanet	158673. Acral dystrophic epidermolysis bullosa. 79407. Autosomal dominant dystrophic epidermolysis bullosa, Cockayne-Touraine type. 216989. Autosomal dominant dystrophic epidermolysis bullosa, Pasini type. 79408. Autosomal recessive dystrophic epidermolysis bullosa, Hallopeau-Siemens type. 89842. Autosomal recessive dystrophic epidermolysis bullosa, non-Hallopeau-Siemens type. 89841. Centripetal dystrophic epidermolysis bullosa. 79409. Dystrophic epidermolysis bullosa inversa. 89839. Epidermolysis bullosa simplex superficialis. 158676. Epidermolysis bullosa, dystrophic, nails only. 79410. Pretibial dystrophic epidermolysis bullosa. 89843. Pruriginous dystrophic epidermolysis bullosa. 79411. Transient bullous dermolysis of the newborn.
PharmGKB	PA26730.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000111866.
HOVERGEN	HBG051053.
InParanoid	Q02388.
KO	K16628.
OMA	RRVCTTA.
OrthoDB	EOG4J117P.
PhylomeDB	Q02388.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	Q02388.
Bgee	Q02388.
CleanEx	HS_COL7A1.
Genevestigator	Q02388.
GermOnline	ENSG00000114270. Homo sapiens.
Family and domain databases
Gene3D	2.60.40.10. 9 hits. 4.10.410.10. 1 hit.
InterPro	IPR008160. Collagen. IPR003961. Fibronectin_type3. IPR013783. Ig-like_fold. IPR002223. Prot_inh_Kunz-m. IPR020901. Prtase_inh_Kunz-CS. IPR002035. VWF_A. [Graphical view]
Pfam	PF01391. Collagen. 18 hits. PF00041. fn3. 9 hits. PF00014. Kunitz_BPTI. 1 hit. PF00092. VWA. 2 hits. [Graphical view]
PRINTS	PR00759. BASICPTASE.
SMART	SM00060. FN3. 9 hits. SM00327. VWA. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 9 hits. SSF57362. Prot_inh_Kunz-m. 1 hit.
PROSITE	PS00280. BPTI_KUNITZ_1. 1 hit. PS50279. BPTI_KUNITZ_2. 1 hit. PS50853. FN3. 9 hits. PS50234. VWFA. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	COL7A1. human.
GenomeRNAi	1294.
NextBio	5251.
SOURCE	Search...

Entry information

Entry name

CO7A1_HUMAN

Accession

Primary (citable) accession number: Q02388
Secondary accession number(s): Q14054, Q16507

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 158 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.