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Q9QZS0 (CO4A3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-3(IV) chain

Cleaved into the following chain:

  1. Tumstatin
Gene names
Name:Col4a3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1669 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.7 Ref.9 UniProtKB Q01955

Tumstatin, a cleavage fragment corresponding to the collagen alpha 3(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity; these two anti-tumor properties may be regulated via RGD-independent ITGB3-mediated mechanisms. Ref.3 Ref.7 Ref.9 UniProtKB Q01955

Subunit structure

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. The alpha 3(IV) chain forms a triple helical protomer with alpha 4(IV) and alpha 5(IV); this triple helical structure dimerizes through NC1-NC1 domain interactions such that the alpha 3(IV), alpha 4(IV) and alpha 5(IV) chains of one protomer connect with the alpha 5(IV), alpha 4(IV) and alpha 3(IV) chains of the opposite promoter, respectively. Interacts with COL4A3BP and ITGB3 By similarity. Associates with LAMB2 at the neuromuscular junction and in GBM. Ref.3 Ref.8 UniProtKB Q01955

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL). Ref.3

Tissue specificity

Highly expressed in kidney and lung. Detected at lower levels in heart, muscle and skin. Ref.3

Domain

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 By similarity. UniProtKB Q01955

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 By similarity. UniProtKB Q01955

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 By similarity. UniProtKB Q01955

The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues By similarity.

Phosphorylated by the Goodpasture antigen-binding protein/COL4A3BP By similarity. UniProtKB Q01955

Disruption phenotype

Mice exhibit normal pregnancy and wound healing, but consistent with the human hereditary disorder Alport syndrome they develop a progressive glomerulonephritis with microhematuria and proteinuria. Ref.6

Sequence similarities

Belongs to the type IV collagen family.

Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 16691641Collagen alpha-3(IV) chain
PRO_0000279698
Chain1424 – 1669246Tumstatin Ref.3
PRO_0000279699

Regions

Domain1444 – 1668225Collagen IV NC1
Region29 – 42147S domain By similarity UniProtKB Q01955
Region43 – 14361394Triple-helical region UniProtKB Q01955
Region1425 – 144319Epitope recognized by Goodpasture antibodies By similarity UniProtKB Q01955
Region1478 – 155679Required for the anti-angiogenic activity of tumstatin By similarity UniProtKB Q01955
Region1609 – 162719Required for the anti-tumor cell activity of tumstatin By similarity UniProtKB Q01955
Motif830 – 8323Cell attachment site Potential
Motif994 – 9963Cell attachment site Potential
Motif1152 – 11543Cell attachment site Potential
Motif1304 – 13063Cell attachment site Potential

Sites

Site1424 – 14252Cleavage; by collagenase By similarity UniProtKB Q01955

Amino acid modifications

Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Disulfide bond1459 ↔ 1550Or C-1459 with C-1547 By similarity UniProtKB Q01955
Disulfide bond1492 ↔ 1547Or C-1492 with C-1550 By similarity UniProtKB Q01955
Disulfide bond1504 ↔ 1510 By similarity UniProtKB Q01955
Disulfide bond1569 ↔ 1664Or C-1569 with C-1661 By similarity UniProtKB Q01955
Disulfide bond1603 ↔ 1661Or C-1603 with C-1664 By similarity UniProtKB Q01955
Disulfide bond1615 ↔ 1621 By similarity UniProtKB Q01955
Cross-link1412Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1532S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1650) By similarity
Cross-link1650S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1532) By similarity

Experimental info

Sequence conflict10411L → R in AAD50449. Ref.1
Sequence conflict15941G → R in CAA57689. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9QZS0 [UniParc].

Last modified March 6, 2007. Version 2.
Checksum: 2E976B2F2E66D28E

FASTA1,669161,726
        10         20         30         40         50         60 
MHSKTAPRFL VFLLLTLLLL LAASPVASKG CVCKGKGQCL CAGTKGEKGE KGVPGSPGFP 

        70         80         90        100        110        120 
GQKGFPGPEG LPGPQGPKGS PGLPGLTGPK GIRGITGLPG FAGPPGLPGL PGHPGPRGLA 

       130        140        150        160        170        180 
GLPGCNGSKG EQGFPGFPGT PGYAGLPGPD GLKGQKGEPA QGEDRGFNGK GDPGPPGVPG 

       190        200        210        220        230        240 
FQGFPGLPGF PGPAGPPGPP GFFGLPGAMG PRGPKGHMGD SVIGQKGERG MKGLTGPPGP 

       250        260        270        280        290        300 
PGTVIFTLTQ PYNKSDFKGE KGDEGERGEP GPPGPSGPPG DSYGSEKGAP GEPGPRGKPG 

       310        320        330        340        350        360 
KDGAPGFPGT EGAKGNRGFP GLRGEAGIKG RKGDIGPPGF PGPTEYYDAY LEKGERGMPG 

       370        380        390        400        410        420 
LPGPKGARGP QGPSGPPGVP GSPGLSRPGL RGPIGWPGLK GSKGERGPPG KDTVGPPGPL 

       430        440        450        460        470        480 
GCPGSPGPPG PPGPPGCPGD IVFKCSPGEH GMPGDTGPPG VPGLDGPKGE PGSPCTECHC 

       490        500        510        520        530        540 
FPGPPGVPGF PGLDGIKGIP GGRGVPGLKG NPGSPGSAGL PGFAGFPGDQ GHPGLKGDKG 

       550        560        570        580        590        600 
DTPLPWGQVG NPGDPGLRGL PGRKGFDGTP GGPGAKGPPG PQGEPALSGR KGDQGPPGPP 

       610        620        630        640        650        660 
GFPGPPGPAG PAGPPGYGPQ GEPGPKGAQG VPGVLGPPGE AGLKGEPSTS TPDLGPPGPP 

       670        680        690        700        710        720 
GPPGQAGPRG LPGLPGPVGK CDPGLPGPDG EPGIPEAGCP GPPGPKGNQG FPGTKGSPGC 

       730        740        750        760        770        780 
PGEMGKPGRP GEPGIPGAKG EPSVGRPGKP GKPGFPGERG NAGENGDIGL PGLPGLPGTP 

       790        800        810        820        830        840 
GRGGLDGPPG DPGQPGSPGA KGSPGRCIPG PRGTQGLPGL NGLKGQPGRR GDTGPKGDPG 

       850        860        870        880        890        900 
IPGMDRSGVP GDPGPPGTPG CPGEMGPPGQ KGYPGAPGFP GPPGEKGEVG MMGYPGTTGP 

       910        920        930        940        950        960 
PGLPGKPGSQ GQRGSLGIPG MKGEKGRPGA KGERGEKGKP GPSQTTLLKG DKGEPGLKGF 

       970        980        990       1000       1010       1020 
VGNPGEKGNR GNPGLPGPKG LEGLPGLPGP PGPRGDTGSR GNPGRPGPHG MPGSMGIMGV 

      1030       1040       1050       1060       1070       1080 
PGPKGRKGTS GLPGLAGRPG LTGIHGPQGD KGEPGYSEGA RPGPPGPKGD PGLPGDKGKK 

      1090       1100       1110       1120       1130       1140 
GERGVPGPPG QSGPAGPDGA PGSPGSPGHP GKPGPAGDLG LKGQKGFPGP PGSTGPPGPP 

      1150       1160       1170       1180       1190       1200 
GLPGLPGPMG MRGDQGRDGI PGPPGEKGET GLLGAYPGPK GSPGVPGAKG DRGVPGLSGL 

      1210       1220       1230       1240       1250       1260 
PGRKGVMGDV GPQGPPGTAG LPGPPGLPGA IIPGPKGDRG LPGLRGNPGE PGPPGPPGPI 

      1270       1280       1290       1300       1310       1320 
GKGIKGDKGF MGPPGPKGLP GTVGDMGPPG FPGAPGTPGL PGVRGDPGFP GFPGIKGEKG 

      1330       1340       1350       1360       1370       1380 
NPGFLGPIGH PGPVGPKGPP GPRGKPGTLK VISLPGSPGP PGVPGQPGMK GDPGPLGLPG 

      1390       1400       1410       1420       1430       1440 
IPGPCGPRGK PGKDGKPGTP GPAGTKGNKG LKGQQGPPGL DGLPGLKGNP GDRGTPATGT 

      1450       1460       1470       1480       1490       1500 
RMRGFIFTRH SQTTAIPSCP EGTQPLYSGF SLLFVQGNKR AHGQDLGTLG SCLQRFTTMP 

      1510       1520       1530       1540       1550       1560 
FLFCNINNVC NFASRNDYSY WLSTPALMPM DMAPISGRAL EPYISRCTVC EGPAMAIAVH 

      1570       1580       1590       1600       1610       1620 
SQTTAIPPCP QDWVSLWKGF SFIMFTSAGS EGAGQALASP GSCLEEFRAS PFIECHGRGT 

      1630       1640       1650       1660 
CNYYSNSYSF WLASLNPERM FRKPIPSTVK AGDLEKIISR CQVCMKKRH 

« Hide

References

« Hide 'large scale' references
[1]"Insertional mutation of the collagen genes Col4a3 and Col4a4 in a mouse model of Alport syndrome."
Lu W., Phillips C.L., Killen P.D., Hlaing T., Harrison W.R., Elder F.F.B., Miner J.H., Overbeek P.A., Meisler M.H.
Genomics 61:113-124(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryonic kidney.
[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].
Strain: C57BL/6J.
[3]"Collagen IV alpha 3, alpha 4, and alpha 5 chains in rodent basal laminae: sequence, distribution, association with laminins, and developmental switches."
Miner J.H., Sanes J.R.
J. Cell Biol. 127:879-891(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1424-1669, FUNCTION, INTERACTION WITH LAMB2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Kidney.
[4]"Cloning of the NC1 domains fo the minor collagen IV chains of mouse via PCR (RACE) reveals the presence of the mRNAs for alpha3 (IV) and alpha5 (IV) in differentiated teratocarcinoma cells."
Oberbaeumer I.
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1491-1651.
Strain: 129.
Tissue: Epithelium.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1558-1669.
Strain: C57BL/6J.
Tissue: Embryonic lung.
[6]"Collagen COL4A3 knockout: a mouse model for autosomal Alport syndrome."
Cosgrove D., Meehan D.T., Grunkemeyer J.A., Kornak J.M., Sayers R., Hunter W.J., Samuelson G.C.
Genes Dev. 10:2981-2992(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[7]"Physiological levels of tumstatin, a fragment of collagen IV alpha3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via alphaV beta3 integrin."
Hamano Y., Zeisberg M., Sugimoto H., Lively J.C., Maeshima Y., Yang C., Hynes R.O., Werb Z., Sudhakar A., Kalluri R.
Cancer Cell 3:589-601(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Characterization of assembly of recombinant type IV collagen alpha3, alpha4, and alpha5 chains in transfected cell strains."
Kobayashi T., Uchiyama M.
Kidney Int. 64:1986-1996(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH COL4A4 AND COL4A5.
[9]"Tumor-specific expression of the RGD-alpha3(IV)NC1 domain suppresses endothelial tube formation and tumor growth in mice."
Miyoshi T., Hirohata S., Ogawa H., Doi M., Obika M., Yonezawa T., Sado Y., Kusachi S., Kyo S., Kondo S., Shiratori Y., Hudson B.G., Ninomiya Y.
FASEB J. 20:1904-1906(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF169387 mRNA. Translation: AAD50449.1.
AC123746 Genomic DNA. No translation available.
AC138214 Genomic DNA. No translation available.
Z35166 mRNA. Translation: CAA84529.1.
X82205 mRNA. Translation: CAA57689.1.
AK033387 mRNA. Translation: BAC28260.1.
CCDSCCDS35631.1.
PIRI48302.
S49488.
RefSeqNP_031760.2. NM_007734.2.
UniGeneMm.389135.

3D structure databases

ProteinModelPortalQ9QZS0.
SMRQ9QZS0. Positions 1444-1667.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9QZS0.

Proteomic databases

PaxDbQ9QZS0.
PRIDEQ9QZS0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000113457; ENSMUSP00000109084; ENSMUSG00000079465.
GeneID12828.
KEGGmmu:12828.
UCSCuc007brv.1. mouse.

Organism-specific databases

CTD1285.
MGIMGI:104688. Col4a3.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00720000108691.
HOGENOMHOG000085652.
HOVERGENHBG004933.
InParanoidQ9QZS0.
KOK06237.
OMAPKRMFRK.
OrthoDBEOG7RZ5P3.
PhylomeDBQ9QZS0.
TreeFamTF316865.

Gene expression databases

ArrayExpressQ9QZS0.
BgeeQ9QZS0.
CleanExMM_COL4A3.
GenevestigatorQ9QZS0.

Family and domain databases

Gene3D2.170.240.10. 1 hit.
InterProIPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamPF01413. C4. 2 hits.
PF01391. Collagen. 20 hits.
[Graphical view]
SMARTSM00111. C4. 2 hits.
[Graphical view]
SUPFAMSSF56436. SSF56436. 2 hits.
PROSITEPS51403. NC1_IV. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL4A3. mouse.
NextBio282322.
PROQ9QZS0.
SOURCESearch...

Entry information

Entry nameCO4A3_MOUSE
AccessionPrimary (citable) accession number: Q9QZS0
Secondary accession number(s): Q61430, Q61435, Q8CCD6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 102 of the entry and version 2 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