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Q9QZS0

- CO4A3_MOUSE

UniProt

Q9QZS0 - CO4A3_MOUSE

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Protein

Collagen alpha-3(IV) chain

Gene

Col4a3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- 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.By similarity1 Publication
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.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1424 – 14252Cleavage; by collagenaseBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro
  2. integrin binding Source: UniProtKB

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  2. cell adhesion Source: UniProtKB-KW
  3. cell proliferation Source: UniProtKB
  4. cell surface receptor signaling pathway Source: UniProtKB
  5. endothelial cell apoptotic process Source: UniProtKB
  6. glomerular basement membrane development Source: UniProtKB
  7. negative regulation of angiogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_196595. Anchoring fibril formation.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_202342. Laminin interactions.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-3(IV) chain
Cleaved into the following chain:
Gene namesi
Name:Col4a3Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:104688. Col4a3.

Subcellular locationi

Secretedextracellular spaceextracellular matrixbasement membrane 1 PublicationPROSITE-ProRule annotation
Note: Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL).By similarity1 Publication

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. collagen type IV trimer Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 16691641Collagen alpha-3(IV) chainSequence AnalysisPRO_0000279698Add
BLAST
Chaini1424 – 1669246Tumstatin1 PublicationPRO_0000279699Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence Analysis
Cross-linki1412 – 1412Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Disulfide bondi1459 ↔ 1550Or C-1459 with C-1547By similarityPROSITE-ProRule annotation
Disulfide bondi1492 ↔ 1547Or C-1492 with C-1550By similarityPROSITE-ProRule annotation
Disulfide bondi1504 ↔ 1510By similarityPROSITE-ProRule annotation
Cross-linki1532 – 1532S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1650)By similarity
Disulfide bondi1569 ↔ 1664Or C-1569 with C-1661By similarityPROSITE-ProRule annotation
Disulfide bondi1603 ↔ 1661Or C-1603 with C-1664By similarityPROSITE-ProRule annotation
Disulfide bondi1615 ↔ 1621By similarityPROSITE-ProRule annotation
Cross-linki1650 – 1650S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1532)By similarity

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.By similarityPROSITE-ProRule annotation
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 similarityPROSITE-ProRule annotation
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

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9QZS0.
PRIDEiQ9QZS0.

PTM databases

PhosphoSiteiQ9QZS0.

Expressioni

Tissue specificityi

Highly expressed in kidney and lung. Detected at lower levels in heart, muscle and skin.1 Publication

Gene expression databases

BgeeiQ9QZS0.
CleanExiMM_COL4A3.
ExpressionAtlasiQ9QZS0. baseline and differential.
GenevestigatoriQ9QZS0.

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. 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.By similarity2 Publications

Structurei

3D structure databases

ProteinModelPortaliQ9QZS0.
SMRiQ9QZS0. Positions 1444-1667.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1444 – 1668225Collagen IV NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 42147S domainBy similarityAdd
BLAST
Regioni43 – 14361394Triple-helical regionAdd
BLAST
Regioni1425 – 144319Epitope recognized by Goodpasture antibodiesBy similarityAdd
BLAST
Regioni1478 – 155679Required for the anti-angiogenic activity of tumstatinBy similarityAdd
BLAST
Regioni1609 – 162719Required for the anti-tumor cell activity of tumstatinBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi830 – 8323Cell attachment siteSequence Analysis
Motifi994 – 9963Cell attachment siteSequence Analysis
Motifi1152 – 11543Cell attachment siteSequence Analysis
Motifi1304 – 13063Cell attachment siteSequence Analysis

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.By similarityPROSITE-ProRule annotation

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

eggNOGiNOG12793.
GeneTreeiENSGT00760000118776.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiQ9QZS0.
KOiK06237.
OMAiPKRMFRK.
OrthoDBiEOG7RZ5P3.
PhylomeDBiQ9QZS0.
TreeFamiTF316865.

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. 20 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.

Q9QZS0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHSKTAPRFL VFLLLTLLLL LAASPVASKG CVCKGKGQCL CAGTKGEKGE
60 70 80 90 100
KGVPGSPGFP GQKGFPGPEG LPGPQGPKGS PGLPGLTGPK GIRGITGLPG
110 120 130 140 150
FAGPPGLPGL PGHPGPRGLA GLPGCNGSKG EQGFPGFPGT PGYAGLPGPD
160 170 180 190 200
GLKGQKGEPA QGEDRGFNGK GDPGPPGVPG FQGFPGLPGF PGPAGPPGPP
210 220 230 240 250
GFFGLPGAMG PRGPKGHMGD SVIGQKGERG MKGLTGPPGP PGTVIFTLTQ
260 270 280 290 300
PYNKSDFKGE KGDEGERGEP GPPGPSGPPG DSYGSEKGAP GEPGPRGKPG
310 320 330 340 350
KDGAPGFPGT EGAKGNRGFP GLRGEAGIKG RKGDIGPPGF PGPTEYYDAY
360 370 380 390 400
LEKGERGMPG LPGPKGARGP QGPSGPPGVP GSPGLSRPGL RGPIGWPGLK
410 420 430 440 450
GSKGERGPPG KDTVGPPGPL GCPGSPGPPG PPGPPGCPGD IVFKCSPGEH
460 470 480 490 500
GMPGDTGPPG VPGLDGPKGE PGSPCTECHC FPGPPGVPGF PGLDGIKGIP
510 520 530 540 550
GGRGVPGLKG NPGSPGSAGL PGFAGFPGDQ GHPGLKGDKG DTPLPWGQVG
560 570 580 590 600
NPGDPGLRGL PGRKGFDGTP GGPGAKGPPG PQGEPALSGR KGDQGPPGPP
610 620 630 640 650
GFPGPPGPAG PAGPPGYGPQ GEPGPKGAQG VPGVLGPPGE AGLKGEPSTS
660 670 680 690 700
TPDLGPPGPP GPPGQAGPRG LPGLPGPVGK CDPGLPGPDG EPGIPEAGCP
710 720 730 740 750
GPPGPKGNQG FPGTKGSPGC PGEMGKPGRP GEPGIPGAKG EPSVGRPGKP
760 770 780 790 800
GKPGFPGERG NAGENGDIGL PGLPGLPGTP GRGGLDGPPG DPGQPGSPGA
810 820 830 840 850
KGSPGRCIPG PRGTQGLPGL NGLKGQPGRR GDTGPKGDPG IPGMDRSGVP
860 870 880 890 900
GDPGPPGTPG CPGEMGPPGQ KGYPGAPGFP GPPGEKGEVG MMGYPGTTGP
910 920 930 940 950
PGLPGKPGSQ GQRGSLGIPG MKGEKGRPGA KGERGEKGKP GPSQTTLLKG
960 970 980 990 1000
DKGEPGLKGF VGNPGEKGNR GNPGLPGPKG LEGLPGLPGP PGPRGDTGSR
1010 1020 1030 1040 1050
GNPGRPGPHG MPGSMGIMGV PGPKGRKGTS GLPGLAGRPG LTGIHGPQGD
1060 1070 1080 1090 1100
KGEPGYSEGA RPGPPGPKGD PGLPGDKGKK GERGVPGPPG QSGPAGPDGA
1110 1120 1130 1140 1150
PGSPGSPGHP GKPGPAGDLG LKGQKGFPGP PGSTGPPGPP GLPGLPGPMG
1160 1170 1180 1190 1200
MRGDQGRDGI PGPPGEKGET GLLGAYPGPK GSPGVPGAKG DRGVPGLSGL
1210 1220 1230 1240 1250
PGRKGVMGDV GPQGPPGTAG LPGPPGLPGA IIPGPKGDRG LPGLRGNPGE
1260 1270 1280 1290 1300
PGPPGPPGPI GKGIKGDKGF MGPPGPKGLP GTVGDMGPPG FPGAPGTPGL
1310 1320 1330 1340 1350
PGVRGDPGFP GFPGIKGEKG NPGFLGPIGH PGPVGPKGPP GPRGKPGTLK
1360 1370 1380 1390 1400
VISLPGSPGP PGVPGQPGMK GDPGPLGLPG IPGPCGPRGK PGKDGKPGTP
1410 1420 1430 1440 1450
GPAGTKGNKG LKGQQGPPGL DGLPGLKGNP GDRGTPATGT RMRGFIFTRH
1460 1470 1480 1490 1500
SQTTAIPSCP EGTQPLYSGF SLLFVQGNKR AHGQDLGTLG SCLQRFTTMP
1510 1520 1530 1540 1550
FLFCNINNVC NFASRNDYSY WLSTPALMPM DMAPISGRAL EPYISRCTVC
1560 1570 1580 1590 1600
EGPAMAIAVH SQTTAIPPCP QDWVSLWKGF SFIMFTSAGS EGAGQALASP
1610 1620 1630 1640 1650
GSCLEEFRAS PFIECHGRGT CNYYSNSYSF WLASLNPERM FRKPIPSTVK
1660
AGDLEKIISR CQVCMKKRH
Length:1,669
Mass (Da):161,726
Last modified:March 6, 2007 - v2
Checksum:i2E976B2F2E66D28E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1041 – 10411L → R in AAD50449. (PubMed:10534397)Curated
Sequence conflicti1594 – 15941G → R in CAA57689. (PubMed:7962065)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35631.1.
PIRiI48302.
S49488.
RefSeqiNP_031760.2. NM_007734.2.
UniGeneiMm.389135.

Genome annotation databases

EnsembliENSMUST00000113457; ENSMUSP00000109084; ENSMUSG00000079465.
GeneIDi12828.
KEGGimmu:12828.
UCSCiuc007brv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35631.1.
PIRi I48302.
S49488.
RefSeqi NP_031760.2. NM_007734.2.
UniGenei Mm.389135.

3D structure databases

ProteinModelPortali Q9QZS0.
SMRi Q9QZS0. Positions 1444-1667.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9QZS0.

Proteomic databases

PaxDbi Q9QZS0.
PRIDEi Q9QZS0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000113457 ; ENSMUSP00000109084 ; ENSMUSG00000079465 .
GeneIDi 12828.
KEGGi mmu:12828.
UCSCi uc007brv.1. mouse.

Organism-specific databases

CTDi 1285.
MGIi MGI:104688. Col4a3.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118776.
HOGENOMi HOG000085652.
HOVERGENi HBG004933.
InParanoidi Q9QZS0.
KOi K06237.
OMAi PKRMFRK.
OrthoDBi EOG7RZ5P3.
PhylomeDBi Q9QZS0.
TreeFami TF316865.

Enzyme and pathway databases

Reactomei REACT_196595. Anchoring fibril formation.
REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.
REACT_202342. Laminin interactions.
REACT_206066. Extracellular matrix organization.
REACT_216309. Integrin cell surface interactions.

Miscellaneous databases

ChiTaRSi COL4A3. mouse.
NextBioi 282322.
PROi Q9QZS0.
SOURCEi Search...

Gene expression databases

Bgeei Q9QZS0.
CleanExi MM_COL4A3.
ExpressionAtlasi Q9QZS0. baseline and differential.
Genevestigatori Q9QZS0.

Family and domain databases

Gene3Di 2.170.240.10. 1 hit.
InterProi IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view ]
Pfami PF01413. C4. 2 hits.
PF01391. Collagen. 20 hits.
[Graphical view ]
SMARTi SM00111. C4. 2 hits.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 2 hits.
PROSITEi PS51403. NC1_IV. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 kidneyImported.
  2. 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/cImported.
    Tissue: KidneyImported.
  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: 129Imported.
    Tissue: EpitheliumImported.
  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.
    , 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/6JImported.
    Tissue: Embryonic lungImported.
  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.

Entry informationi

Entry nameiCO4A3_MOUSE
AccessioniPrimary (citable) accession number: Q9QZS0
Secondary accession number(s): Q61430, Q61435, Q8CCD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 6, 2007
Last modified: October 29, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3