Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Collagen alpha-1(IV) chain

Gene

Cg25C

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Collagen type IV is specific for basement membranes.

GO - Molecular functioni

GO - Biological processi

  • cardiac muscle cell development Source: FlyBase
  • dorsal closure Source: FlyBase
  • intestinal epithelial structure maintenance Source: FlyBase
  • oviduct morphogenesis Source: FlyBase
  • post-embryonic digestive tract morphogenesis Source: FlyBase
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-DME-1442490. Collagen degradation.
R-DME-1650814. Collagen biosynthesis and modifying enzymes.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(IV) chain
Gene namesi
Name:Cg25C
Synonyms:DCg1
ORF Names:CG4145
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000299. Cg25C.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: FlyBase
  • collagen type IV trimer Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 1779Collagen alpha-1(IV) chainPRO_0000005755
Signal peptidei1 – 2323Add
BLAST
Propeptidei24 – ?N-terminal propeptide (7S domain)PRO_0000005754

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...)Curated
Disulfide bondi1570 ↔ 1659Or C-1570 with C-1656PROSITE-ProRule annotation
Disulfide bondi1603 ↔ 1656Or C-1603 with C-1659PROSITE-ProRule annotation
Disulfide bondi1615 ↔ 1621PROSITE-ProRule annotation
Disulfide bondi1678 ↔ 1774Or C-1678 with C-1771PROSITE-ProRule annotation
Disulfide bondi1712 ↔ 1771Or C-1712 with C-1774PROSITE-ProRule annotation
Disulfide bondi1724 ↔ 1731PROSITE-ProRule annotation

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiP08120.
PRIDEiP08120.

Expressioni

Gene expression databases

BgeeiFBgn0000299.
ExpressionAtlasiP08120. differential.
GenevisibleiP08120. DM.

Interactioni

Subunit structurei

Trimers of two alpha 1(IV) and one alpha 2(IV) chain. Type IV collagen forms a mesh-like network linked through intermolecular interactions between 7S domains and between NC1 domains.

Protein-protein interaction databases

BioGridi59908. 9 interactions.
DIPiDIP-59819N.
IntActiP08120. 8 interactions.
MINTiMINT-1738460.
STRINGi7227.FBpp0078641.

Structurei

3D structure databases

ProteinModelPortaliP08120.
SMRiP08120. Positions 1557-1777.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1555 – 1778224Collagen IV NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni? – 1545Triple-helical region

Domaini

Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.

Sequence similaritiesi

Belongs to the type IV collagen family.PROSITE-ProRule annotation
Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
InParanoidiP08120.
KOiK06237.
OMAiIKMPAKG.
OrthoDBiEOG091G0613.
PhylomeDBiP08120.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 15 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08120-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPFWKRLLY AAVIAGALVG ADAQFWKTAG TAGSIQDSVK HYNRNEPKFP
60 70 80 90 100
IDDSYDIVDS AGVARGDLPP KNCTAGYAGC VPKCIAEKGN RGLPGPLGPT
110 120 130 140 150
GLKGEMGFPG MEGPSGDKGQ KGDPGPYGQR GDKGERGSPG LHGQAGVPGV
160 170 180 190 200
QGPAGNPGAP GINGKDGCDG QDGIPGLEGL SGMPGPRGYA GQLGSKGEKG
210 220 230 240 250
EPAKENGDYA KGEKGEPGWR GTAGLAGPQG FPGEKGERGD SGPYGAKGPR
260 270 280 290 300
GEHGLKGEKG ASCYGPMKPG APGIKGEKGE PASSFPVKPT HTVMGPRGDM
310 320 330 340 350
GQKGEPGLVG RKGEPGPEGD TGLDGQKGEK GLPGGPGDRG RQGNFGPPGS
360 370 380 390 400
TGQKGDRGEP GLNGLPGNPG QKGEPGRAGA TGKPGLLGPP GPPGGGRGTP
410 420 430 440 450
GPPGPKGPRG YVGAPGPQGL NGVDGLPGPQ GYNGQKGGAG LPGRPGNEGP
460 470 480 490 500
PGKKGEKGTA GLNGPKGSIG PIGHPGPPGP EGQKGDAGLP GYGIQGSKGD
510 520 530 540 550
AGIPGYPGLK GSKGERGFKG NAGAPGDSKL GRPGTPGAAG APGQKGDAGR
560 570 580 590 600
PGTPGQKGDM GIKGDVGGKC SSCRAGPKGD KGTSGLPGIP GKDGARGPPG
610 620 630 640 650
ERGYPGERGH DGINGQTGPP GEKGEDGRTG LPGATGEPGK PALCDLSLIE
660 670 680 690 700
PLKGDKGYPG APGAKGVQGF KGAEGLPGIP GPKGEFGFKG EKGLSGAPGN
710 720 730 740 750
DGTPGRAGRD GYPGIPGQSI KGEPGFHGRD GAKGDKGSFG RSGEKGEPGS
760 770 780 790 800
CALDEIKMPA KGNKGEPGQT GMPGPPGEDG SPGERGYTGL KGNTGPQGPP
810 820 830 840 850
GVEGPRGLNG PRGEKGNQGA VGVPGNPGKD GLRGIPGRNG QPGPRGEPGI
860 870 880 890 900
SRPGPMGPPG LNGLQGEKGD RGPTGPIGFP GADGSVGYPG DRGDAGLPGV
910 920 930 940 950
SGRPGIVGEK GDVGPIGPAG VAGPPGVPGI DGVRGRDGAK GEPGSPGLVG
960 970 980 990 1000
MPGNKGDRGA PGNDGPKGFA GVTGAPGKRG PAGIPGVSGA KGDKGATGLT
1010 1020 1030 1040 1050
GNDGPVGGRG PPGAPGLMGI KGDQGLAGAP GQQGLDGMPG EKGNQGFPGL
1060 1070 1080 1090 1100
DGPPGLPGDA SEKGQKGEPG PSGLRGDTGP AGTPGWPGEK GLPGLAVHGR
1110 1120 1130 1140 1150
AGPPGEKGDQ GRSGIDGRDG INGEKGEQGL QGVWGQPGEK GSVGAPGIPG
1160 1170 1180 1190 1200
APGMDGLPGA AGAPGAVGYP GDRGDKGEPG LSGLPGLKGE TGPVGLQGFT
1210 1220 1230 1240 1250
GAPGPKGERG IRGQPGLPAT VPDIRGDKGS QGERGYTGEK GEQGERGLTG
1260 1270 1280 1290 1300
PAGVAGAKGD RGLQGPPGAS GLNGIPGAKG DIGPRGEIGY PGVTIKGEKG
1310 1320 1330 1340 1350
LPGRPGRNGR QGLIGAPGLI GERGLPGLAG EPGLVGLPGP IGPAGSKGER
1360 1370 1380 1390 1400
GLAGSPGQPG QDGFPGAPGL KGDTGPQGFK GERGLNGFEG QKGDKGDRGL
1410 1420 1430 1440 1450
QGPSGLPGLV GQKGDTGYPG LNGNDGPVGA PGERGFTGPK GRDGRDGTPG
1460 1470 1480 1490 1500
LPGQKGEPGM LPPPGPKGEP GQPGRNGPKG EPGRPGERGL IGIQGERGEK
1510 1520 1530 1540 1550
GERGLIGETG NVGRPGPKGD RGEPGERGYE GAIGLIGQKG EPGAPAPAAL
1560 1570 1580 1590 1600
DYLTGILITR HSQSETVPAC SAGHTELWTG YSLLYVDGND YAHNQDLGSP
1610 1620 1630 1640 1650
GSCVPRFSTL PVLSCGQNNV CNYASRNDKT FWLTTNAAIP MMPVENIEIR
1660 1670 1680 1690 1700
QYISRCVVCE APANVIAVHS QTIEVPDCPN GWEGLWIGYS FLMHTAVGNG
1710 1720 1730 1740 1750
GGGQALQSPG SCLEDFRATP FIECNGAKGT CHFYETMTSF WMYNLESSQP
1760 1770
FERPQQQTIK AGERQSHVSR CQVCMKNSS
Length:1,779
Mass (Da):174,300
Last modified:December 4, 2007 - v3
Checksum:i6770F18AE40A313E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti383 – 3831K → E in AAA28404 (PubMed:3142875).Curated
Sequence conflicti383 – 3831K → E in AAA28423 (PubMed:3142875).Curated
Sequence conflicti383 – 3831K → E in AAB59184 (Ref. 2) Curated
Sequence conflicti437 – 4371G → D in AAA28404 (PubMed:3142875).Curated
Sequence conflicti437 – 4371G → D in AAA28423 (PubMed:3142875).Curated
Sequence conflicti437 – 4371G → D in AAB59184 (Ref. 2) Curated
Sequence conflicti948 – 9481L → S in CAA23486 (PubMed:6210912).Curated
Sequence conflicti997 – 9971T → S in AAA28404 (PubMed:3142875).Curated
Sequence conflicti997 – 9971T → S in AAA28423 (PubMed:3142875).Curated
Sequence conflicti997 – 9971T → S in AAB59184 (Ref. 2) Curated
Sequence conflicti1329 – 13335AGEPG → PESR in AAA28404 (PubMed:3142875).Curated
Sequence conflicti1329 – 13335AGEPG → PESR in AAA28423 (PubMed:3142875).Curated
Sequence conflicti1329 – 13335AGEPG → PESR in AAB59184 (Ref. 2) Curated
Sequence conflicti1358 – 13581Q → K in AAA28422 (PubMed:3109906).Curated
Sequence conflicti1361 – 13611Q → K in AAA28422 (PubMed:3109906).Curated
Sequence conflicti1374 – 13741T → I in AAA28422 (PubMed:3109906).Curated
Sequence conflicti1424 – 14241N → T in AAA28422 (PubMed:3109906).Curated
Sequence conflicti1497 – 14971R → L in AAA28404 (PubMed:3142875).Curated
Sequence conflicti1497 – 14971R → L in AAA28423 (PubMed:3142875).Curated
Sequence conflicti1497 – 14971R → L in AAB59184 (Ref. 2) Curated
Sequence conflicti1508 – 15125ETGNV → RAGQR in AAA28422 (PubMed:3109906).Curated
Sequence conflicti1530 – 15301E → K in AAA28422 (PubMed:3109906).Curated
Sequence conflicti1600 – 16023Missing in AAA28404 (PubMed:3142875).Curated
Sequence conflicti1600 – 16023Missing in AAA28423 (PubMed:3142875).Curated
Sequence conflicti1600 – 16023Missing in AAB59184 (Ref. 2) Curated
Sequence conflicti1600 – 16023Missing in AAA28422 (PubMed:3109906).Curated
Sequence conflicti1737 – 17371M → I in AAA28422 (PubMed:3109906).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02727 mRNA. Translation: AAA28423.1.
M23704 mRNA. Translation: AAA28404.1.
M96575 Genomic DNA. Translation: AAB59184.1.
AE014134 Genomic DNA. Translation: AAF52204.1.
AE014134 Genomic DNA. Translation: AAN10519.1.
AE014134 Genomic DNA. Translation: AAN10520.1.
V00200 Genomic DNA. Translation: CAA23486.2.
M28334 mRNA. Translation: AAA28422.1.
PIRiA31893.
RefSeqiNP_723044.1. NM_164615.2.
NP_723045.1. NM_164616.2.
NP_723046.1. NM_164617.2.
UniGeneiDm.5178.

Genome annotation databases

EnsemblMetazoaiFBtr0079001; FBpp0078640; FBgn0000299.
FBtr0079002; FBpp0078641; FBgn0000299.
FBtr0079003; FBpp0078642; FBgn0000299.
GeneIDi33727.
KEGGidme:Dmel_CG4145.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02727 mRNA. Translation: AAA28423.1.
M23704 mRNA. Translation: AAA28404.1.
M96575 Genomic DNA. Translation: AAB59184.1.
AE014134 Genomic DNA. Translation: AAF52204.1.
AE014134 Genomic DNA. Translation: AAN10519.1.
AE014134 Genomic DNA. Translation: AAN10520.1.
V00200 Genomic DNA. Translation: CAA23486.2.
M28334 mRNA. Translation: AAA28422.1.
PIRiA31893.
RefSeqiNP_723044.1. NM_164615.2.
NP_723045.1. NM_164616.2.
NP_723046.1. NM_164617.2.
UniGeneiDm.5178.

3D structure databases

ProteinModelPortaliP08120.
SMRiP08120. Positions 1557-1777.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59908. 9 interactions.
DIPiDIP-59819N.
IntActiP08120. 8 interactions.
MINTiMINT-1738460.
STRINGi7227.FBpp0078641.

Proteomic databases

PaxDbiP08120.
PRIDEiP08120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079001; FBpp0078640; FBgn0000299.
FBtr0079002; FBpp0078641; FBgn0000299.
FBtr0079003; FBpp0078642; FBgn0000299.
GeneIDi33727.
KEGGidme:Dmel_CG4145.

Organism-specific databases

CTDi33727.
FlyBaseiFBgn0000299. Cg25C.

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
InParanoidiP08120.
KOiK06237.
OMAiIKMPAKG.
OrthoDBiEOG091G0613.
PhylomeDBiP08120.

Enzyme and pathway databases

ReactomeiR-DME-1442490. Collagen degradation.
R-DME-1650814. Collagen biosynthesis and modifying enzymes.

Miscellaneous databases

ChiTaRSiCg25C. fly.
GenomeRNAii33727.
PROiP08120.

Gene expression databases

BgeeiFBgn0000299.
ExpressionAtlasiP08120. differential.
GenevisibleiP08120. DM.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 15 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO4A1_DROME
AccessioniPrimary (citable) accession number: P08120
Secondary accession number(s): A4V070, Q9VMV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: December 4, 2007
Last modified: September 7, 2016
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.