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Protein

Collagen alpha-2(IV) chain

Gene

Col4a2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.1 Publication
Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity. It inhibits proliferation and migration of endothelial cells, reduces mitochondrial membrane potential, and induces apoptosis. Specifically induces Fas-dependent apoptosis and activates procaspase-8 and -9 activity. Ligand for alphavbeta3 and alphavbeta5 integrins (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processAngiogenesis

Enzyme and pathway databases

ReactomeiR-MMU-1442490 Collagen degradation
R-MMU-1474244 Extracellular matrix organization
R-MMU-1650814 Collagen biosynthesis and modifying enzymes
R-MMU-186797 Signaling by PDGF
R-MMU-2022090 Assembly of collagen fibrils and other multimeric structures
R-MMU-216083 Integrin cell surface interactions
R-MMU-2214320 Anchoring fibril formation
R-MMU-2243919 Crosslinking of collagen fibrils
R-MMU-3000157 Laminin interactions
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-419037 NCAM1 interactions
R-MMU-8948216 Collagen chain trimerization

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(IV) chain
Cleaved into the following chain:
Gene namesi
Name:Col4a2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:88455 Col4a2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Add BLAST25
PropeptideiPRO_000000582626 – 183N-terminal propeptide (7S domain)Add BLAST158
ChainiPRO_0000005827184 – 1707Collagen alpha-2(IV) chainAdd BLAST1524
ChainiPRO_00003904871481 – 1707CanstatinAdd BLAST227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi138N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1270N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1499 ↔ 1588PROSITE-ProRule annotation
Disulfide bondi1532 ↔ 1585PROSITE-ProRule annotation
Disulfide bondi1544 ↔ 1550PROSITE-ProRule annotation
Disulfide bondi1607 ↔ 1703PROSITE-ProRule annotation
Disulfide bondi1641 ↔ 1700PROSITE-ProRule annotation
Disulfide bondi1653 ↔ 1660PROSITE-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.
Proteolytic processing produces the C-terminal NC1 peptide, canstatin.By similarity
The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiP08122
PaxDbiP08122
PRIDEiP08122

PTM databases

iPTMnetiP08122
PhosphoSitePlusiP08122
SwissPalmiP08122

Expressioni

Gene expression databases

BgeeiENSMUSG00000031503 Expressed in 300 organ(s), highest expression level in epithelium of lens
CleanExiMM_COL4A2
ExpressionAtlasiP08122 baseline and differential
GenevisibleiP08122 MM

Interactioni

Subunit structurei

There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.

Protein-protein interaction databases

BioGridi198817, 1 interactor
ComplexPortaliCPX-2959 Collagen type IV trimer variant 1
STRINGi10090.ENSMUSP00000033899

Structurei

3D structure databases

ProteinModelPortaliP08122
SMRiP08122
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1484 – 1707Collagen IV NC1PROSITE-ProRule annotationAdd BLAST224

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni184 – 1479Triple-helical regionAdd BLAST1296

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

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00900000140804
HOVERGENiHBG004933
InParanoidiP08122
KOiK06237
OMAiNPGTKGW
OrthoDBiEOG091G0613
PhylomeDBiP08122
TreeFamiTF344135

Family and domain databases

Gene3Di2.170.240.10, 1 hit
InterProiView protein in InterPro
IPR008160 Collagen
IPR001442 Collagen_IV_NC
IPR036954 Collagen_IV_NC_sf
IPR016187 CTDL_fold
PfamiView protein in Pfam
PF01413 C4, 2 hits
PF01391 Collagen, 16 hits
SMARTiView protein in SMART
SM00111 C4, 2 hits
SUPFAMiSSF56436 SSF56436, 2 hits
PROSITEiView protein in PROSITE
PS51403 NC1_IV, 1 hit

Sequencei

Sequence statusi: Complete.

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

P08122-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDRVRFKASG PPLRGWLLLA TVTVGLLAQS VLGGVKKLDV PCGGRDCSGG
60 70 80 90 100
CQCYPEKGAR GQPGAVGPQG YNGPPGLQGF PGLQGRKGDK GERGVPGPTG
110 120 130 140 150
PKGDVGARGV SGFPGADGIP GHPGQGGPRG RPGYDGCNGT RGDAGPQGPS
160 170 180 190 200
GSGGFPGLPG PQGPKGQKGE PYALSKEDRD KYRGEPGEPG LVGYQGPPGR
210 220 230 240 250
PGPIGQMGPM GAPGRPGPPG PPGPKGQPGN RGLGFYGQKG EKGDIGQPGP
260 270 280 290 300
NGIPSDITLV GPTTSTIHPD LYKGEKGDEG EQGIPGVISK GEEGIMGFPG
310 320 330 340 350
IRGFPGLDGE KGVVGQKGSR GLDGFQGPSG PRGPKGERGE QGPPGPSVYS
360 370 380 390 400
PHPSLAKGAR GDPGFQGAHG EPGSRGEPGE PGTAGPPGPS VGDEDSMRGL
410 420 430 440 450
PGEMGPKGFS GEPGSPARYL GPPGADGRPG PQGVPGPAGP PGPDGFLFGL
460 470 480 490 500
KGSEGRVGYP GPSGFPGTRG QKGWKGEAGD CQCGQVIGGL PGLPGPKGFP
510 520 530 540 550
GVNGELGKKG DQGDPGLHGI PGFPGFKGAP GVAGAPGPKG IKGDSRTITT
560 570 580 590 600
KGERGQPGIP GVHGMKGDDG VPGRDGLDGF PGLPGPPGDG IKGPPGDAGL
610 620 630 640 650
PGVPGTKGFP GDIGPPGQGL PGPKGERGFP GDAGLPGPPG FPGPPGPPGT
660 670 680 690 700
PGQRDCDTGV KRPIGGGQQV VVQPGCIEGP TGSPGQPGPP GPTGAKGVRG
710 720 730 740 750
MPGFPGASGE QGLKGFPGDP GREGFPGPPG FMGPRGSKGT TGLPGPDGPP
760 770 780 790 800
GPIGLPGPAG PPGDRGIPGE VLGAQPGTRG DAGLPGQPGL KGLPGETGAP
810 820 830 840 850
GFRGSQGMPG MPGLKGQPGF PGPSGQPGQS GPPGQHGFPG TPGREGPLGQ
860 870 880 890 900
PGSPGLGGLP GDRGEPGDPG VPGPVGMKGL SGDRGDAGMS GERGHPGSPG
910 920 930 940 950
FKGMAGMPGI PGQKGDRGSP GMDGFQGMLG LKGRQGFPGT KGEAGFFGVP
960 970 980 990 1000
GLKGLPGEPG VKGNRGDRGP PGPPPLILPG MKDIKGEKGD EGPMGLKGYL
1010 1020 1030 1040 1050
GLKGIQGMPG VPGVSGFPGL PGRPGFIKGV KGDIGVPGTP GLPGFPGVSG
1060 1070 1080 1090 1100
PPGITGFPGF TGSRGEKGTP GVAGVFGETG PTGDFGDIGD TVDLPGSPGL
1110 1120 1130 1140 1150
KGERGITGIP GLKGFFGEKG AAGDIGFPGI TGMAGAQGSP GLKGQTGFPG
1160 1170 1180 1190 1200
LTGLQGPQGE PGRIGIPGDK GDFGWPGVPG LPGFPGIRGI SGLHGLPGTK
1210 1220 1230 1240 1250
GFPGSPGVDA HGDPGFPGPT GDRGDRGEAN TLPGPVGVPG QKGERGTPGE
1260 1270 1280 1290 1300
RGPAGSPGLQ GFPGISPPSN ISGSPGDVGA PGIFGLQGYQ GPPGPPGPNA
1310 1320 1330 1340 1350
LPGIKGDEGS SGAAGFPGQK GWVGDPGPQG QPGVLGLPGE KGPKGEQGFM
1360 1370 1380 1390 1400
GNTGPSGAVG DRGPKGPKGD QGFPGAPGSM GSPGIPGIPQ KIAVQPGTLG
1410 1420 1430 1440 1450
PQGRRGLPGA LGEIGPQGPP GDPGFRGAPG KAGPQGRGGV SAVPGFRGDQ
1460 1470 1480 1490 1500
GPMGHQGPVG QEGEPGRPGS PGLPGMPGRS VSIGYLLVKH SQTDQEPMCP
1510 1520 1530 1540 1550
VGMNKLWSGY SLLYFEGQEK AHNQDLGLAG SCLARFSTMP FLYCNPGDVC
1560 1570 1580 1590 1600
YYASRNDKSY WLSTTAPLPM MPVAEEEIKP YISRCSVCEA PAVAIAVHSQ
1610 1620 1630 1640 1650
DTSIPHCPAG WRSLWIGYSF LMHTAAGDEG GGQSLVSPGS CLEDFRATPF
1660 1670 1680 1690 1700
IECNGGRGTC HYFANKYSFW LTTIPEQNFQ STPSADTLKA GLIRTHISRC

QVCMKNL
Length:1,707
Mass (Da):167,325
Last modified:February 20, 2007 - v4
Checksum:i67CB3E3CB2A5B1F6
GO

Sequence cautioni

The sequence AAH80789 differs from that shown. Contaminating sequence. Potential poly-A sequence starting in position 277.Curated
The sequence AAI07686 differs from that shown. Contaminating sequence. Potential poly-A sequence starting in position 277.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti275E → K in AAH80789 (PubMed:15489334).Curated1
Sequence conflicti626E → R in AAA50293 (PubMed:2703491).Curated1
Sequence conflicti837G → A in AAA50293 (PubMed:2703491).Curated1
Sequence conflicti1051P → R in CAA27998 (PubMed:3758345).Curated1
Sequence conflicti1097S → G in CAA26655 (PubMed:3839908).Curated1
Sequence conflicti1171G → S in CAA27998 (PubMed:3758345).Curated1
Sequence conflicti1179P → R in CAA27998 (PubMed:3758345).Curated1
Sequence conflicti1241Q → E in CAA27998 (PubMed:3758345).Curated1
Sequence conflicti1328P → A in CAA27998 (PubMed:3758345).Curated1
Sequence conflicti1573V → L in CAA28308 (PubMed:3780963).Curated1
Sequence conflicti1583S → I in AAR89902 (PubMed:15592653).Curated1
Sequence conflicti1583S → I in AAQ83370 (PubMed:15592653).Curated1
Sequence conflicti1623H → Y in AAA50293 (PubMed:2703491).Curated1
Sequence conflicti1623H → Y in AAA37341 (PubMed:3597383).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04695 mRNA Translation: AAA50293.1
AK053858 mRNA Translation: BAC35559.1
AK075619 mRNA Translation: BAC35863.1
AK164096 mRNA Translation: BAE37626.1
BC013560 mRNA Translation: AAH13560.2
BC080789 mRNA Translation: AAH80789.1 Sequence problems.
BC107685 mRNA Translation: AAI07686.1 Sequence problems.
M23334, M23333 Genomic DNA Translation: AAA51626.1
J04448 Genomic DNA Translation: AAA37438.1
X02896 mRNA Translation: CAA26655.1
X02897 Genomic DNA Translation: CAB51614.1
X02898 Genomic DNA Translation: CAA26657.1
X02899 Genomic DNA Translation: CAA26658.1
X04410 mRNA Translation: CAA27998.1
X04647 mRNA Translation: CAA28308.1
M15833 mRNA Translation: AAA37341.1
AY375463 mRNA Translation: AAQ83370.1
AY502946 mRNA Translation: AAR89901.1
AY502947 mRNA Translation: AAR89902.1
CCDSiCCDS40220.1
PIRiA33526
RefSeqiNP_034062.3, NM_009932.4
UniGeneiMm.181021

Genome annotation databases

EnsembliENSMUST00000033899; ENSMUSP00000033899; ENSMUSG00000031503
GeneIDi12827
KEGGimmu:12827
UCSCiuc009kvc.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04695 mRNA Translation: AAA50293.1
AK053858 mRNA Translation: BAC35559.1
AK075619 mRNA Translation: BAC35863.1
AK164096 mRNA Translation: BAE37626.1
BC013560 mRNA Translation: AAH13560.2
BC080789 mRNA Translation: AAH80789.1 Sequence problems.
BC107685 mRNA Translation: AAI07686.1 Sequence problems.
M23334, M23333 Genomic DNA Translation: AAA51626.1
J04448 Genomic DNA Translation: AAA37438.1
X02896 mRNA Translation: CAA26655.1
X02897 Genomic DNA Translation: CAB51614.1
X02898 Genomic DNA Translation: CAA26657.1
X02899 Genomic DNA Translation: CAA26658.1
X04410 mRNA Translation: CAA27998.1
X04647 mRNA Translation: CAA28308.1
M15833 mRNA Translation: AAA37341.1
AY375463 mRNA Translation: AAQ83370.1
AY502946 mRNA Translation: AAR89901.1
AY502947 mRNA Translation: AAR89902.1
CCDSiCCDS40220.1
PIRiA33526
RefSeqiNP_034062.3, NM_009932.4
UniGeneiMm.181021

3D structure databases

ProteinModelPortaliP08122
SMRiP08122
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198817, 1 interactor
ComplexPortaliCPX-2959 Collagen type IV trimer variant 1
STRINGi10090.ENSMUSP00000033899

PTM databases

iPTMnetiP08122
PhosphoSitePlusiP08122
SwissPalmiP08122

Proteomic databases

MaxQBiP08122
PaxDbiP08122
PRIDEiP08122

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033899; ENSMUSP00000033899; ENSMUSG00000031503
GeneIDi12827
KEGGimmu:12827
UCSCiuc009kvc.2 mouse

Organism-specific databases

CTDi1284
MGIiMGI:88455 Col4a2

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG410XNMM LUCA
GeneTreeiENSGT00900000140804
HOVERGENiHBG004933
InParanoidiP08122
KOiK06237
OMAiNPGTKGW
OrthoDBiEOG091G0613
PhylomeDBiP08122
TreeFamiTF344135

Enzyme and pathway databases

ReactomeiR-MMU-1442490 Collagen degradation
R-MMU-1474244 Extracellular matrix organization
R-MMU-1650814 Collagen biosynthesis and modifying enzymes
R-MMU-186797 Signaling by PDGF
R-MMU-2022090 Assembly of collagen fibrils and other multimeric structures
R-MMU-216083 Integrin cell surface interactions
R-MMU-2214320 Anchoring fibril formation
R-MMU-2243919 Crosslinking of collagen fibrils
R-MMU-3000157 Laminin interactions
R-MMU-3000171 Non-integrin membrane-ECM interactions
R-MMU-419037 NCAM1 interactions
R-MMU-8948216 Collagen chain trimerization

Miscellaneous databases

ChiTaRSiCol4a2 mouse
PROiPR:P08122
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031503 Expressed in 300 organ(s), highest expression level in epithelium of lens
CleanExiMM_COL4A2
ExpressionAtlasiP08122 baseline and differential
GenevisibleiP08122 MM

Family and domain databases

Gene3Di2.170.240.10, 1 hit
InterProiView protein in InterPro
IPR008160 Collagen
IPR001442 Collagen_IV_NC
IPR036954 Collagen_IV_NC_sf
IPR016187 CTDL_fold
PfamiView protein in Pfam
PF01413 C4, 2 hits
PF01391 Collagen, 16 hits
SMARTiView protein in SMART
SM00111 C4, 2 hits
SUPFAMiSSF56436 SSF56436, 2 hits
PROSITEiView protein in PROSITE
PS51403 NC1_IV, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCO4A2_MOUSE
AccessioniPrimary (citable) accession number: P08122
Secondary accession number(s): Q3B7C2
, Q3TPV9, Q61375, Q66JS5, Q6RCT6, Q6RCT7, Q6U9X1, Q8BPI9, Q8BPK3, Q91VI3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 20, 2007
Last modified: November 7, 2018
This is version 186 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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