Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q63870 (CO7A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(VII) chain
Alternative name(s):
Long-chain collagen
Short name=LC collagen
Gene names
Name:Col7a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2944 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.4 UniProtKB Q02388

Subunit structure

Homotrimer. Interacts with MIA3/TANGO1; facilitating its loading into transport carriers and subsequent secretion By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane By similarity.

Induction

Transcription of COL7A1 is stimulated by TGFB1 in keratinocytes and this is possibly dependent on a putative interaction between SMADS and AP1. Ref.5

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.

Disruption phenotype

Mice do not express type VII collagen in their skin; they are born with extensive cutaneous blistering and die during the first two weeks of life, possibly because of complications arising from blistering; this mouse mutant resembles the autosomal recessive inherited form of the dystrophic epidermolysis bullosa (DEB) in humans. Heterozygotes by comparison display a normal phenotype. Ref.4

Sequence similarities

Contains 1 BPTI/Kunitz inhibitor domain.

Contains 9 fibronectin type-III domains.

Contains 2 VWFA domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-8313134,EBI-8313134

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 29442920Collagen alpha-1(VII) chain
PRO_0000282951

Regions

Domain39 – 212174VWFA 1
Domain235 – 33096Fibronectin type-III 1
Domain331 – 41787Fibronectin type-III 2
Domain418 – 50891Fibronectin type-III 3
Domain511 – 59888Fibronectin type-III 4
Domain601 – 68888Fibronectin type-III 5
Domain689 – 77688Fibronectin type-III 6
Domain779 – 86789Fibronectin type-III 7
Domain870 – 95788Fibronectin type-III 8
Domain959 – 105395Fibronectin type-III 9
Domain1055 – 1230176VWFA 2
Domain2879 – 293153BPTI/Kunitz inhibitor
Region18 – 12541237Nonhelical region (NC1)
Region1255 – 27751521Triple-helical region
Region1255 – 1475221Interrupted collagenous region
Region2776 – 2944169Nonhelical region (NC2)
Motif1171 – 11733Cell attachment site Potential
Motif2002 – 20043Cell attachment site Potential
Motif2063 – 20653Cell attachment site Potential
Motif2601 – 26033Cell attachment site Potential
Motif2631 – 26333Cell attachment site Potential

Sites

Site2889 – 28902Reactive bond By similarity

Amino acid modifications

Modified residue215814-hydroxyproline By similarity
Modified residue216714-hydroxyproline By similarity
Modified residue217614-hydroxyproline By similarity
Modified residue217914-hydroxyproline By similarity
Modified residue261615-hydroxylysine By similarity
Modified residue262215-hydroxylysine By similarity
Modified residue265514-hydroxyproline By similarity
Modified residue265814-hydroxyproline By similarity
Modified residue266414-hydroxyproline By similarity
Glycosylation3381N-linked (GlcNAc...) Potential
Glycosylation7871N-linked (GlcNAc...) Potential
Glycosylation11101N-linked (GlcNAc...) Potential
Disulfide bond2625Interchain By similarity
Disulfide bond2793Interchain By similarity
Disulfide bond2795Interchain By similarity
Disulfide bond2879 ↔ 2931 By similarity
Disulfide bond2888 ↔ 2914 By similarity
Disulfide bond2906 ↔ 2927 By similarity

Experimental info

Sequence conflict6591S → G in AAB66593. Ref.1
Sequence conflict19271R → A in AAB66593. Ref.1
Sequence conflict19271R → A in AAB27492. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q63870 [UniParc].

Last modified April 3, 2007. Version 3.
Checksum: 13D01CA7ED36C958

FASTA2,944295,232
        10         20         30         40         50         60 
MRLRLLVAAL CAAEILMGAP EVWAQPRDRV TCTRLYAADI VFLLDGSSSI GRSNFREVRG 

        70         80         90        100        110        120 
FLEGLVLPFS GAASAQGVRF ATVQYSDDPQ TEFGLDTLGS GSDTIRAIRE LSYKGGNTRT 

       130        140        150        160        170        180 
GAALHHVSDR VFLPRLTRPG VPKVCILITD GKSQDLVDTA AQKLKGQGVK LFAVGIKNAD 

       190        200        210        220        230        240 
PEELKRVASQ PTSDFFFFVN DFSILRTLLP LISRRVCTTA GGVPVTLPSD DTPSGPRDLV 

       250        260        270        280        290        300 
LSEPSSQSLR VQWTAASGPV TGYKVQYTPL TGLGQPLPSE RQEVNIPAGE TSTRLQGLRP 

       310        320        330        340        350        360 
LTDYQVTVVA LYANSIGEAV SGTARTTAKE GLELSLQNIT SHSLLVAWRR VPGANGYRVT 

       370        380        390        400        410        420 
WRDLSGGPTQ QQDLSPGQGS VFLDHLEPGT DYEVTVSALF GHSVGPAASL TARTASSVEQ 

       430        440        450        460        470        480 
TLHPIILSPT SILLSWNLVP EARGYRLEWR RESGLETPQK VELPPDVTRH QLDGLQPGTE 

       490        500        510        520        530        540 
YRLTLYTLLE GREVATPATV VPTGLEQLVS PVMNLQAIEL PGQRVRVSWN PVPGATEYRF 

       550        560        570        580        590        600 
TVRTTQGVER TLLLPGSQTT FDLDDVRAGL SYTVRVSARV GAQEGDASIL TIHRDPEAPL 

       610        620        630        640        650        660 
VVPGLRVVAS DATRIRVAWG LVPGASGFRI SWRTGSGPES SRTLTPDSTV TDILGLQPST 

       670        680        690        700        710        720 
SYQVAVSALR GREEGPPVVI VARTDPLGPV RRVHLTQAGS SSVSITWTGV PGATGYRVSW 

       730        740        750        760        770        780 
HSGHGPEKSL LVSGDATVAE IDGLEPDTEY IVRVRTHVAG VDGAPASVVV RTAPEPVGSV 

       790        800        810        820        830        840 
SKLQILNASS DVLRVTWVGV PGATSYKLAW GRSEGGPMKH RILPGNKESA EIRDLEGGVS 

       850        860        870        880        890        900 
YSVRVTALVG DREGAPVSIV ITTPPATPAL LETLQVVQSG EHSLRLRWEP VPGAPGFRLH 

       910        920        930        940        950        960 
WQPEGGQEQS LTLGPESNSY NLVGLEPATK YQVWLTVLGQ TGEGPPRKVT AYTEPSHIPS 

       970        980        990       1000       1010       1020 
TELRVVDTSI DSVTLTWTPV SGASSYILSW RPLRGTGQEV PRAPQTLPGT SSSHRVTGLE 

      1030       1040       1050       1060       1070       1080 
PGISYVFSLT PIQSGVRGSE ISVTQTPACS HGPVDVVFLL HATRDNAHNA EAVRRVLERL 

      1090       1100       1110       1120       1130       1140 
VSALGPLGPQ AAQVGLLTYS HRPSPLFPLN SSHDLGIILR KIRDIPYVDP SGNNLGTAVT 

      1150       1160       1170       1180       1190       1200 
TAHRYLLASN APGRRQQVPG VMVLLVDEPL RGDILSPIRE AQTSGLKVMA LSLVGADPEQ 

      1210       1220       1230       1240       1250       1260 
LRRLAPGTDP IQNFFAVDNG PGLDRAVSDL AVALCQAAVT IEPQTGPCAV HCPKGQKGEP 

      1270       1280       1290       1300       1310       1320 
GVTGLQGQAG PPGPPGLPGR TGAPGPQGPP GSTQAKGERG FPGPEGPPGS PGLPGVPGSP 

      1330       1340       1350       1360       1370       1380 
GIKGSTGRPG PRGEQGERGP QGPKGEPGEP GQITGGGGPG FPGKKGDPGP SGPPGSRGPV 

      1390       1400       1410       1420       1430       1440 
GDPGPRGPPG LPGISVKGDK GDRGERGPPG PGIGASEQGD PGLPGLPGSP GPQGPAGRPG 

      1450       1460       1470       1480       1490       1500 
EKGEKGDCED GGPGLPGQPG PPGEPGLRGA PGMTGPKGDR GLTGTPGEPG VKGERGHPGP 

      1510       1520       1530       1540       1550       1560 
VGPQGLPGAA GHPGVEGPEG PPGPTGRRGE KGEPGRPGDP AVGPGGAGAK GEKGEAGLPG 

      1570       1580       1590       1600       1610       1620 
PRGASGSKGE QGAPGLALPG DPGPKGDPGD RGPIGLTGRA GPTGDSGPPG EKGEPGRPGS 

      1630       1640       1650       1660       1670       1680 
PGPVGPRGRD GEAGEKGDEG IPGEPGLPGK AGERGLRGAP GPRGPVGEKG DQGDPGEDGR 

      1690       1700       1710       1720       1730       1740 
NGSPGSSGPK GDRGEPGPPG PPGRLVDAGI ESRDKGEPGQ EGPRGPKGDP GPPGVSGERG 

      1750       1760       1770       1780       1790       1800 
IDGLRGPPGP QGDPGVRGPA GDKGDRGPPG LDGRSGLDGK PGAPGPPGLH GASGKAGDPG 

      1810       1820       1830       1840       1850       1860 
RDGLPGLRGE HGPPGPPGPP GVPGKAGDDG KPGLNGKNGD PGDPGEDGRK GEKGDSGAPG 

      1870       1880       1890       1900       1910       1920 
REGPDGPKGE RGAPGNPGLQ GPPGLPGQVG PPGQGFPGVP GITGPKGDRG ETGSKGEQGL 

      1930       1940       1950       1960       1970       1980 
PGERGLRGEP GSLPNAERLL ETAGIKVSAL REIVDTWDES SGSFLPVPER RPGPKGDPGD 

      1990       2000       2010       2020       2030       2040 
RGPPGKEGLI GFPGERGLKG ERGDPGPQGP PGLALGERGP PGPPGLAGEP GKPGIPGLPG 

      2050       2060       2070       2080       2090       2100 
RAGGSGEAGR PGERGERGEK GERGDQGRDG LPGLPGPPGP PGPKVAIEEP GPGLAREQGP 

      2110       2120       2130       2140       2150       2160 
PGLKGAKGEP GSDGDPGPKG DRGVPGIKGD VGEPGKRGHD GNPGLPGERG VAGPEGKPGL 

      2170       2180       2190       2200       2210       2220 
QGPRGTPGPV GSHGDPGPPG APGLAGPAGP QGPSGLKGEP GETGPPGRGL PGPVGAVGLP 

      2230       2240       2250       2260       2270       2280 
GPPGPSGLVG PQGSPGLPGQ VGETGKPGPP GRDGSSGKDG DRGSPGVPGS PGLPGPVGPK 

      2290       2300       2310       2320       2330       2340 
GEPGPVGAPG QVVVGPPGAK GEKGAPGDLA GALLGEPGAK GDRGLPGPRG EKGEAGRAGG 

      2350       2360       2370       2380       2390       2400 
PGDPGEDGQK GAPGLKGLKG EPGIGVQGPP GPSGPPGMKG DLGPPGAPGA PGVVGFPGQT 

      2410       2420       2430       2440       2450       2460 
GPRGETGQPG PVGERGLAGP PGREGAPGPL GPPGPPGSAG APGASGLKGD KGDPGAGLPG 

      2470       2480       2490       2500       2510       2520 
PRGERGEPGV RGEDGHPGQE GPRGLVGPPG SRGEQGEKGA AGAAGLKGDK GDSAVIEGPP 

      2530       2540       2550       2560       2570       2580 
GPRGAKGDMG ERGPRGIDGD KGPRGESGNP GDKGSKGEPG DKGSAGSIGV RGLTGPKGEP 

      2590       2600       2610       2620       2630       2640 
GAAGIPGEPG APGKDGIPGF RGDKGDIGFM GPRGLKGEKG IKGTCGRDGE RGDKGEAGFP 

      2650       2660       2670       2680       2690       2700 
GRPGLAGKKG DMGEPGLPGQ SGAPGKEGLI GPKGDRGFDG QSGPKGDQGE KGERGPPGVG 

      2710       2720       2730       2740       2750       2760 
GFPGPRGNDG SSGPPGPPGG VGPKGPEGLQ GQKGERGPPG ESVVGAPGAP GTPGERGEQG 

      2770       2780       2790       2800       2810       2820 
RPGPAGPRGE KGEAALTEDD IRDFVRQEMS QHCACQGQFI ASGSRPLPGY AADTAGSQLH 

      2830       2840       2850       2860       2870       2880 
HVPVLRVSHV EEEGQVPPED DDDFSEYSVY SVEDYQEPEV PWDGEAEIKG WDQRGSDLCS 

      2890       2900       2910       2920       2930       2940 
LPLDEGSCTA YTLRWYHRAV PGGTACHPFV YGGCGGNANR FGTREACERR CPPQGVHSQK 


TGAA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of mouse type VII collagen reveals evolutionary conservation of functional protein domains and genomic organization."
Kivirikko S., Li K., Christiano A.M., Uitto J.
J. Invest. Dermatol. 106:1300-1306(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"cDNA cloning and chromosomal mapping of the mouse type VII collagen gene (Col7a1): evidence for rapid evolutionary divergence of the gene."
Li K., Christiano A.M., Copeland N.G., Gilbert D.J., Chu M.-L., Jenkins N.A., Uitto J.
Genomics 16:733-739(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1139-2058.
[4]"Targeted inactivation of the type VII collagen gene (Col7a1) in mice results in severe blistering phenotype: a model for recessive dystrophic epidermolysis bullosa."
Heinonen S., Mannikko M., Klement J.F., Whitaker-Menezes D., Murphy G.F., Uitto J.
J. Cell Sci. 112:3641-3648(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[5]"Transcriptional control of the mouse Col7a1 gene in keratinocytes: basal and transforming growth factor-beta regulated expression."
Naso M., Uitto J., Klement J.F.
J. Invest. Dermatol. 121:1469-1478(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U32107 mRNA. Translation: AAB66593.1.
AC174646 Genomic DNA. No translation available.
S63654 mRNA. Translation: AAB27492.1.
PIRA45748.
RefSeqNP_031764.2. NM_007738.3.
XP_006511998.1. XM_006511935.1.
UniGeneMm.6200.

3D structure databases

ProteinModelPortalQ63870.
SMRQ63870. Positions 39-216, 231-1058.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ63870. 1 interaction.
MINTMINT-4109970.

Protein family/group databases

MEROPSI02.967.

PTM databases

PhosphoSiteQ63870.

Proteomic databases

PaxDbQ63870.
PRIDEQ63870.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026740; ENSMUSP00000026740; ENSMUSG00000025650.
ENSMUST00000112070; ENSMUSP00000107701; ENSMUSG00000025650.
GeneID12836.
KEGGmmu:12836.
UCSCuc009rrh.1. mouse.

Organism-specific databases

CTD1294.
MGIMGI:88462. Col7a1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00720000108691.
HOGENOMHOG000111866.
HOVERGENHBG051053.
InParanoidQ63870.
KOK16628.
OMAWHSGHGP.
OrthoDBEOG7CG6Z4.
TreeFamTF351645.

Gene expression databases

BgeeQ63870.
CleanExMM_COL7A1.
GenevestigatorQ63870.

Family and domain databases

Gene3D2.60.40.10. 9 hits.
3.40.50.410. 2 hits.
4.10.410.10. 1 hit.
InterProIPR008160. Collagen.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
IPR002035. VWF_A.
[Graphical view]
PfamPF01391. Collagen. 22 hits.
PF00041. fn3. 9 hits.
PF00014. Kunitz_BPTI. 1 hit.
PF00092. VWA. 2 hits.
[Graphical view]
PRINTSPR00759. BASICPTASE.
SMARTSM00060. FN3. 9 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 5 hits.
SSF57362. SSF57362. 1 hit.
PROSITEPS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
PS50853. FN3. 9 hits.
PS50234. VWFA. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio282356.
PROQ63870.
SOURCESearch...

Entry information

Entry nameCO7A1_MOUSE
AccessionPrimary (citable) accession number: Q63870
Secondary accession number(s): Q78EC6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: March 19, 2014
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot