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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 similarity3 Publications
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 similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1424 – 14252Cleavage; by collagenase By similarityBy 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
  8. response to glucose Source: Ensembl
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:Col4a3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:104688. Col4a3.

Subcellular locationi

Secretedextracellular spaceextracellular matrixbasement membrane
Note: Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL).1 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 – 2828 Reviewed prediction
Add
BLAST
Chaini29 – 16691641Collagen alpha-3(IV) chain
PRO_0000279698Add
BLAST
Chaini1424 – 1669246Tumstatin1 Publication
PRO_0000279699Add
BLAST

Amino acid modifications

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

ArrayExpressiQ9QZS0.
BgeeiQ9QZS0.
CleanExiMM_COL4A3.
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1444 – 1668225Collagen IV NC1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni29 – 42147S domain By similarityBy similarity
Add
BLAST
Regioni43 – 14361394Triple-helical regionBy similarity
Add
BLAST
Regioni1425 – 144319Epitope recognized by Goodpasture antibodies By similarityBy similarity
Add
BLAST
Regioni1478 – 155679Required for the anti-angiogenic activity of tumstatin By similarityBy similarity
Add
BLAST
Regioni1609 – 162719Required for the anti-tumor cell activity of tumstatin By similarityBy similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi830 – 8323Cell attachment site Reviewed prediction
Motifi994 – 9963Cell attachment site Reviewed prediction
Motifi1152 – 11543Cell attachment site Reviewed prediction
Motifi1304 – 13063Cell attachment site Reviewed prediction

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 similarity.By similarity

Sequence similaritiesi

Belongs to the type IV collagen family.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00720000108691.
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

MHSKTAPRFL VFLLLTLLLL LAASPVASKG CVCKGKGQCL CAGTKGEKGE     50
KGVPGSPGFP GQKGFPGPEG LPGPQGPKGS PGLPGLTGPK GIRGITGLPG 100
FAGPPGLPGL PGHPGPRGLA GLPGCNGSKG EQGFPGFPGT PGYAGLPGPD 150
GLKGQKGEPA QGEDRGFNGK GDPGPPGVPG FQGFPGLPGF PGPAGPPGPP 200
GFFGLPGAMG PRGPKGHMGD SVIGQKGERG MKGLTGPPGP PGTVIFTLTQ 250
PYNKSDFKGE KGDEGERGEP GPPGPSGPPG DSYGSEKGAP GEPGPRGKPG 300
KDGAPGFPGT EGAKGNRGFP GLRGEAGIKG RKGDIGPPGF PGPTEYYDAY 350
LEKGERGMPG LPGPKGARGP QGPSGPPGVP GSPGLSRPGL RGPIGWPGLK 400
GSKGERGPPG KDTVGPPGPL GCPGSPGPPG PPGPPGCPGD IVFKCSPGEH 450
GMPGDTGPPG VPGLDGPKGE PGSPCTECHC FPGPPGVPGF PGLDGIKGIP 500
GGRGVPGLKG NPGSPGSAGL PGFAGFPGDQ GHPGLKGDKG DTPLPWGQVG 550
NPGDPGLRGL PGRKGFDGTP GGPGAKGPPG PQGEPALSGR KGDQGPPGPP 600
GFPGPPGPAG PAGPPGYGPQ GEPGPKGAQG VPGVLGPPGE AGLKGEPSTS 650
TPDLGPPGPP GPPGQAGPRG LPGLPGPVGK CDPGLPGPDG EPGIPEAGCP 700
GPPGPKGNQG FPGTKGSPGC PGEMGKPGRP GEPGIPGAKG EPSVGRPGKP 750
GKPGFPGERG NAGENGDIGL PGLPGLPGTP GRGGLDGPPG DPGQPGSPGA 800
KGSPGRCIPG PRGTQGLPGL NGLKGQPGRR GDTGPKGDPG IPGMDRSGVP 850
GDPGPPGTPG CPGEMGPPGQ KGYPGAPGFP GPPGEKGEVG MMGYPGTTGP 900
PGLPGKPGSQ GQRGSLGIPG MKGEKGRPGA KGERGEKGKP GPSQTTLLKG 950
DKGEPGLKGF VGNPGEKGNR GNPGLPGPKG LEGLPGLPGP PGPRGDTGSR 1000
GNPGRPGPHG MPGSMGIMGV PGPKGRKGTS GLPGLAGRPG LTGIHGPQGD 1050
KGEPGYSEGA RPGPPGPKGD PGLPGDKGKK GERGVPGPPG QSGPAGPDGA 1100
PGSPGSPGHP GKPGPAGDLG LKGQKGFPGP PGSTGPPGPP GLPGLPGPMG 1150
MRGDQGRDGI PGPPGEKGET GLLGAYPGPK GSPGVPGAKG DRGVPGLSGL 1200
PGRKGVMGDV GPQGPPGTAG LPGPPGLPGA IIPGPKGDRG LPGLRGNPGE 1250
PGPPGPPGPI GKGIKGDKGF MGPPGPKGLP GTVGDMGPPG FPGAPGTPGL 1300
PGVRGDPGFP GFPGIKGEKG NPGFLGPIGH PGPVGPKGPP GPRGKPGTLK 1350
VISLPGSPGP PGVPGQPGMK GDPGPLGLPG IPGPCGPRGK PGKDGKPGTP 1400
GPAGTKGNKG LKGQQGPPGL DGLPGLKGNP GDRGTPATGT RMRGFIFTRH 1450
SQTTAIPSCP EGTQPLYSGF SLLFVQGNKR AHGQDLGTLG SCLQRFTTMP 1500
FLFCNINNVC NFASRNDYSY WLSTPALMPM DMAPISGRAL EPYISRCTVC 1550
EGPAMAIAVH SQTTAIPPCP QDWVSLWKGF SFIMFTSAGS EGAGQALASP 1600
GSCLEEFRAS PFIECHGRGT CNYYSNSYSF WLASLNPERM FRKPIPSTVK 1650
AGDLEKIISR CQVCMKKRH 1669
Length:1,669
Mass (Da):161,726
Last modified:March 6, 2007 - v2
Checksum:i2E976B2F2E66D28E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1041 – 10411L → R in AAD50449. 1 Publication
Sequence conflicti1594 – 15941G → R in CAA57689. 1 Publication

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 ENSGT00720000108691.
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

ArrayExpressi Q9QZS0.
Bgeei Q9QZS0.
CleanExi MM_COL4A3.
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 kidney.
  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/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.
    , 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.

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: September 3, 2014
This is version 103 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

Similar proteinsi