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P08122 (CO4A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. 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-2(IV) chain

Cleaved into the following chain:

  1. Canstatin
Gene names
Name:Col4a2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1707 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.10

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. Ref.10

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.

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane By similarity.

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.

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.

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.

Sequence similarities

Belongs to the type IV collagen family.

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

Sequence caution

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525
Propeptide26 – 183158N-terminal propeptide (7S domain)
PRO_0000005826
Chain184 – 17071524Collagen alpha-2(IV) chain
PRO_0000005827
Chain1481 – 1707227Canstatin
PRO_0000390487

Regions

Domain1484 – 1707224Collagen IV NC1
Region184 – 14791296Triple-helical region

Amino acid modifications

Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation12701N-linked (GlcNAc...) Potential
Disulfide bond1499 ↔ 1588 By similarity
Disulfide bond1532 ↔ 1585 By similarity
Disulfide bond1544 ↔ 1550 By similarity
Disulfide bond1607 ↔ 1703 By similarity
Disulfide bond1641 ↔ 1700 By similarity
Disulfide bond1653 ↔ 1660 By similarity

Experimental info

Sequence conflict2751E → K in AAH80789. Ref.3
Sequence conflict6261E → R in AAA50293. Ref.1
Sequence conflict8371G → A in AAA50293. Ref.1
Sequence conflict10511P → R in CAA27998. Ref.8
Sequence conflict10971S → G in CAA26655. Ref.6
Sequence conflict11711G → S in CAA27998. Ref.8
Sequence conflict11791P → R in CAA27998. Ref.8
Sequence conflict12411Q → E in CAA27998. Ref.8
Sequence conflict13281P → A in CAA27998. Ref.8
Sequence conflict15731V → L in CAA28308. Ref.9
Sequence conflict15831S → I in AAR89902. Ref.11
Sequence conflict15831S → I in AAQ83370. Ref.11
Sequence conflict16231H → Y in AAA50293. Ref.1
Sequence conflict16231H → Y in AAA37341. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P08122 [UniParc].

Last modified February 20, 2007. Version 4.
Checksum: 67CB3E3CB2A5B1F6

FASTA1,707167,325
        10         20         30         40         50         60 
MDRVRFKASG PPLRGWLLLA TVTVGLLAQS VLGGVKKLDV PCGGRDCSGG CQCYPEKGAR 

        70         80         90        100        110        120 
GQPGAVGPQG YNGPPGLQGF PGLQGRKGDK GERGVPGPTG PKGDVGARGV SGFPGADGIP 

       130        140        150        160        170        180 
GHPGQGGPRG RPGYDGCNGT RGDAGPQGPS GSGGFPGLPG PQGPKGQKGE PYALSKEDRD 

       190        200        210        220        230        240 
KYRGEPGEPG LVGYQGPPGR PGPIGQMGPM GAPGRPGPPG PPGPKGQPGN RGLGFYGQKG 

       250        260        270        280        290        300 
EKGDIGQPGP NGIPSDITLV GPTTSTIHPD LYKGEKGDEG EQGIPGVISK GEEGIMGFPG 

       310        320        330        340        350        360 
IRGFPGLDGE KGVVGQKGSR GLDGFQGPSG PRGPKGERGE QGPPGPSVYS PHPSLAKGAR 

       370        380        390        400        410        420 
GDPGFQGAHG EPGSRGEPGE PGTAGPPGPS VGDEDSMRGL PGEMGPKGFS GEPGSPARYL 

       430        440        450        460        470        480 
GPPGADGRPG PQGVPGPAGP PGPDGFLFGL KGSEGRVGYP GPSGFPGTRG QKGWKGEAGD 

       490        500        510        520        530        540 
CQCGQVIGGL PGLPGPKGFP GVNGELGKKG DQGDPGLHGI PGFPGFKGAP GVAGAPGPKG 

       550        560        570        580        590        600 
IKGDSRTITT KGERGQPGIP GVHGMKGDDG VPGRDGLDGF PGLPGPPGDG IKGPPGDAGL 

       610        620        630        640        650        660 
PGVPGTKGFP GDIGPPGQGL PGPKGERGFP GDAGLPGPPG FPGPPGPPGT PGQRDCDTGV 

       670        680        690        700        710        720 
KRPIGGGQQV VVQPGCIEGP TGSPGQPGPP GPTGAKGVRG MPGFPGASGE QGLKGFPGDP 

       730        740        750        760        770        780 
GREGFPGPPG FMGPRGSKGT TGLPGPDGPP GPIGLPGPAG PPGDRGIPGE VLGAQPGTRG 

       790        800        810        820        830        840 
DAGLPGQPGL KGLPGETGAP GFRGSQGMPG MPGLKGQPGF PGPSGQPGQS GPPGQHGFPG 

       850        860        870        880        890        900 
TPGREGPLGQ PGSPGLGGLP GDRGEPGDPG VPGPVGMKGL SGDRGDAGMS GERGHPGSPG 

       910        920        930        940        950        960 
FKGMAGMPGI PGQKGDRGSP GMDGFQGMLG LKGRQGFPGT KGEAGFFGVP GLKGLPGEPG 

       970        980        990       1000       1010       1020 
VKGNRGDRGP PGPPPLILPG MKDIKGEKGD EGPMGLKGYL GLKGIQGMPG VPGVSGFPGL 

      1030       1040       1050       1060       1070       1080 
PGRPGFIKGV KGDIGVPGTP GLPGFPGVSG PPGITGFPGF TGSRGEKGTP GVAGVFGETG 

      1090       1100       1110       1120       1130       1140 
PTGDFGDIGD TVDLPGSPGL KGERGITGIP GLKGFFGEKG AAGDIGFPGI TGMAGAQGSP 

      1150       1160       1170       1180       1190       1200 
GLKGQTGFPG LTGLQGPQGE PGRIGIPGDK GDFGWPGVPG LPGFPGIRGI SGLHGLPGTK 

      1210       1220       1230       1240       1250       1260 
GFPGSPGVDA HGDPGFPGPT GDRGDRGEAN TLPGPVGVPG QKGERGTPGE RGPAGSPGLQ 

      1270       1280       1290       1300       1310       1320 
GFPGISPPSN ISGSPGDVGA PGIFGLQGYQ GPPGPPGPNA LPGIKGDEGS SGAAGFPGQK 

      1330       1340       1350       1360       1370       1380 
GWVGDPGPQG QPGVLGLPGE KGPKGEQGFM GNTGPSGAVG DRGPKGPKGD QGFPGAPGSM 

      1390       1400       1410       1420       1430       1440 
GSPGIPGIPQ KIAVQPGTLG PQGRRGLPGA LGEIGPQGPP GDPGFRGAPG KAGPQGRGGV 

      1450       1460       1470       1480       1490       1500 
SAVPGFRGDQ GPMGHQGPVG QEGEPGRPGS PGLPGMPGRS VSIGYLLVKH SQTDQEPMCP 

      1510       1520       1530       1540       1550       1560 
VGMNKLWSGY SLLYFEGQEK AHNQDLGLAG SCLARFSTMP FLYCNPGDVC YYASRNDKSY 

      1570       1580       1590       1600       1610       1620 
WLSTTAPLPM MPVAEEEIKP YISRCSVCEA PAVAIAVHSQ DTSIPHCPAG WRSLWIGYSF 

      1630       1640       1650       1660       1670       1680 
LMHTAAGDEG GGQSLVSPGS CLEDFRATPF IECNGGRGTC HYFANKYSFW LTTIPEQNFQ 

      1690       1700 
STPSADTLKA GLIRTHISRC QVCMKNL 

« Hide

References

« Hide 'large scale' references
[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. 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 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS40220.1.
PIRA33526.
RefSeqNP_034062.3. NM_009932.3.
UniGeneMm.181021.

3D structure databases

ProteinModelPortalP08122.
SMRP08122. Positions 1482-1706.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198817. 1 interaction.

PTM databases

PhosphoSiteP08122.

Proteomic databases

MaxQBP08122.
PaxDbP08122.
PRIDEP08122.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033899; ENSMUSP00000033899; ENSMUSG00000031503.
GeneID12827.
KEGGmmu:12827.
UCSCuc009kvc.2. mouse.

Organism-specific databases

CTD1284.
MGIMGI:88455. Col4a2.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00730000110538.
HOVERGENHBG004933.
InParanoidP08122.
KOK06237.
OMAGFKGMAG.
OrthoDBEOG7RZ5P3.
PhylomeDBP08122.
TreeFamTF344135.

Enzyme and pathway databases

ReactomeREACT_206066. Extracellular matrix organization.
REACT_213817. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP08122.
BgeeP08122.
CleanExMM_COL4A2.
GenevestigatorP08122.

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. 19 hits.
[Graphical view]
SMARTSM00111. C4. 2 hits.
[Graphical view]
SUPFAMSSF56436. SSF56436. 2 hits.
PROSITEPS51403. NC1_IV. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL4A2. mouse.
NextBio282318.
PROP08122.
SOURCESearch...

Entry information

Entry nameCO4A2_MOUSE
AccessionPrimary (citable) accession number: P08122
Secondary accession number(s): Q3B7C2 expand/collapse secondary AC list , Q3TPV9, Q61375, Q66JS5, Q6RCT6, Q6RCT7, Q6U9X1, Q8BPI9, Q8BPK3, Q91VI3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 149 of the entry and version 4 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