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P08122

- CO4A2_MOUSE

UniProt

P08122 - CO4A2_MOUSE

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Protein

Collagen alpha-2(IV) chain

Gene

Col4a2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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

  1. extracellular matrix structural constituent Source: InterPro

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cellular response to transforming growth factor beta stimulus Source: UniProtKB
  3. negative regulation of angiogenesis Source: UniProtKB
  4. transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Angiogenesis

Enzyme and pathway databases

ReactomeiREACT_196581. Scavenging by Class A Receptors.
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.
REACT_236183. NCAM1 interactions.
REACT_263353. Signaling by PDGF.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:88455. Col4a2.

Subcellular locationi

Secretedextracellular spaceextracellular matrixbasement membrane PROSITE-ProRule annotation

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. collagen type IV trimer Source: MGI
  3. extracellular matrix Source: UniProtKB
  4. extracellular region Source: Reactome
  5. extracellular vesicular exosome Source: Ensembl
  6. intracellular membrane-bounded organelle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Add
BLAST
Propeptidei26 – 183158N-terminal propeptide (7S domain)PRO_0000005826Add
BLAST
Chaini184 – 17071524Collagen alpha-2(IV) chainPRO_0000005827Add
BLAST
Chaini1481 – 1707227CanstatinPRO_0000390487Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1270 – 12701N-linked (GlcNAc...)Sequence Analysis
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

PhosphoSiteiP08122.

Expressioni

Gene expression databases

BgeeiP08122.
CleanExiMM_COL4A2.
ExpressionAtlasiP08122. baseline and differential.
GenevestigatoriP08122.

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 interaction.

Structurei

3D structure databases

ProteinModelPortaliP08122.
SMRiP08122. Positions 1482-1706.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1484 – 1707224Collagen IV NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 14791296Triple-helical regionAdd
BLAST

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

eggNOGiNOG12793.
GeneTreeiENSGT00770000120455.
HOVERGENiHBG004933.
InParanoidiP08122.
KOiK06237.
OMAiGFKGMAG.
OrthoDBiEOG7RZ5P3.
PhylomeDBiP08122.
TreeFamiTF344135.

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. 19 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.

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 AAH80789.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 277.Curated
The sequence AAI07686.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 277.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti275 – 2751E → K in AAH80789. (PubMed:15489334)Curated
Sequence conflicti626 – 6261E → R in AAA50293. (PubMed:2703491)Curated
Sequence conflicti837 – 8371G → A in AAA50293. (PubMed:2703491)Curated
Sequence conflicti1051 – 10511P → R in CAA27998. (PubMed:3758345)Curated
Sequence conflicti1097 – 10971S → G in CAA26655. (PubMed:3839908)Curated
Sequence conflicti1171 – 11711G → S in CAA27998. (PubMed:3758345)Curated
Sequence conflicti1179 – 11791P → R in CAA27998. (PubMed:3758345)Curated
Sequence conflicti1241 – 12411Q → E in CAA27998. (PubMed:3758345)Curated
Sequence conflicti1328 – 13281P → A in CAA27998. (PubMed:3758345)Curated
Sequence conflicti1573 – 15731V → L in CAA28308. (PubMed:3780963)Curated
Sequence conflicti1583 – 15831S → I in AAR89902. (PubMed:15592653)Curated
Sequence conflicti1583 – 15831S → I in AAQ83370. (PubMed:15592653)Curated
Sequence conflicti1623 – 16231H → Y in AAA50293. (PubMed:2703491)Curated
Sequence conflicti1623 – 16231H → Y in AAA37341. (PubMed:3597383)Curated

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_009932.3.
UniGeneiMm.181021.

Genome annotation databases

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

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 .
CCDSi CCDS40220.1.
PIRi A33526.
RefSeqi NP_034062.3. NM_009932.3.
UniGenei Mm.181021.

3D structure databases

ProteinModelPortali P08122.
SMRi P08122. Positions 1482-1706.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198817. 1 interaction.

PTM databases

PhosphoSitei P08122.

Proteomic databases

MaxQBi P08122.
PaxDbi P08122.
PRIDEi P08122.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033899 ; ENSMUSP00000033899 ; ENSMUSG00000031503 .
GeneIDi 12827.
KEGGi mmu:12827.
UCSCi uc009kvc.2. mouse.

Organism-specific databases

CTDi 1284.
MGIi MGI:88455. Col4a2.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00770000120455.
HOVERGENi HBG004933.
InParanoidi P08122.
KOi K06237.
OMAi GFKGMAG.
OrthoDBi EOG7RZ5P3.
PhylomeDBi P08122.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_196581. Scavenging by Class A Receptors.
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.
REACT_236183. NCAM1 interactions.
REACT_263353. Signaling by PDGF.

Miscellaneous databases

ChiTaRSi Col4a2. mouse.
NextBioi 282318.
PROi P08122.
SOURCEi Search...

Gene expression databases

Bgeei P08122.
CleanExi MM_COL4A2.
ExpressionAtlasi P08122. baseline and differential.
Genevestigatori P08122.

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. 19 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. "The complete primary structure of mouse alpha 2(IV) collagen. Alignment with mouse alpha 1(IV) collagen."
    Saus J., Quinones S., Mackrell A., Blumberg B., Muthukumaran G., Pihlajaniemi T., Kurkinen M.
    J. Biol. Chem. 264:6318-6324(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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 1-538 AND 1649-1707.
    Strain: C57BL/6J.
    Tissue: Eye and Spinal cord.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-276 AND 1339-1707.
    Tissue: Mammary gland.
  4. "Alpha 1(IV) and alpha 2(IV) collagen genes are regulated by a bidirectional promoter and a shared enhancer."
    Burbelo P.D., Martin G.R., Yamada Y.
    Proc. Natl. Acad. Sci. U.S.A. 85:9679-9682(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-60.
  5. "Head-to-head arrangement of murine type IV collagen genes."
    Kaytes P., Wood L., Theriault N., Kurkinen M., Vogeli G.
    J. Biol. Chem. 263:19274-19277(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
  6. "Characterization of 64-, 123- and 182-base-pair exons in the mouse alpha 2(IV) collagen gene."
    Kurkinen M., Bernard M.P., Barlow D.P., Chow L.T.
    Nature 317:177-179(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 964-1003; 1005-1085 AND 1087-1109.
  7. "Structure of mouse type IV collagen. Amino-acid sequence of the C-terminal 511-residue-long triple-helical segment of the alpha 2(IV) chain and its comparison with the alpha 1(IV) chain."
    Schwarz U., Schuppan D., Oberbaeumer I., Glanville R.W., Deutzmann R., Timpl R., Kuehn K.
    Eur. J. Biochem. 157:49-56(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 970-1480.
  8. "Proposed alignment of helical interruptions in the two subunits of the basement membrane (type IV) collagen."
    Vogeli G., Horn E., Carter J., Kaytes P.S.
    FEBS Lett. 206:29-32(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1041-1489.
  9. "cDNA and protein sequence of the NC1 domain of the alpha 2-chain of collagen IV and its comparison with alpha 1(IV)."
    Schwarz-Magdolen U., Oberbaeumer I., Kuehn K.
    FEBS Lett. 208:203-207(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1480-1707.
  10. "Extensive homology between the carboxyl-terminal peptides of mouse alpha 1(IV) and alpha 2(IV) collagen."
    Kurkinen M., Condon M.R., Blumberg B., Barlow D., Quinones S., Saus J., Pihlajaniemi T.
    J. Biol. Chem. 262:8496-8499(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1481-1707, FUNCTION OF CANSTATIN.
  11. "Recombinant mouse canstatin inhibits chicken embryo chorioallantoic membrane angiogenesis and endothelial cell proliferation."
    Hou W.H., Wang T.Y., Yuan B.M., Chai Y.R., Jia Y.L., Tian F., Wang J.M., Xue L.X.
    Acta Biochim. Biophys. Sin. 36:845-850(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1481-1707.
    Strain: BALB/c.

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 historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 20, 2007
Last modified: November 26, 2014
This is version 153 of the entry and version 4 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