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P02463 (CO4A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. 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-1(IV) chain

Cleaved into the following chain:

  1. Arresten
Gene names
Name:Col4a1
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 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.

Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin By similarity.

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.

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, arresten By similarity.

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

Disruption phenotype

Mice develop perinatal cerebral hemorrhage and porencephaly. The mutant protein inhibits the secretion of mutant and normal proteins into the basement membrane of embryonic origin. The mutation is semidominant. Ref.13

Sequence similarities

Belongs to the type IV collagen family.

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

Sequence caution

The sequence AAH72650.1 differs from that shown. Reason: Frameshift at position 1547.

The sequence AAH72650.1 differs from that shown. Reason: Insertion sequence.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Propeptide28 – 172145N-terminal propeptide (7S domain)
PRO_0000005750
Chain173 – 16691497Collagen alpha-1(IV) chain
PRO_0000005751
Chain1445 – 1669225Arresten
PRO_0000390483

Regions

Domain1445 – 1669225Collagen IV NC1
Region173 – 14401268Triple-helical region

Amino acid modifications

Glycosylation1261N-linked (GlcNAc...) Potential
Disulfide bond1460 ↔ 1551Or C-1460 with C-1548 By similarity
Disulfide bond1493 ↔ 1548Or C-1493 with C-1551 By similarity
Disulfide bond1505 ↔ 1511 By similarity
Disulfide bond1570 ↔ 1665Or C-1570 with C-1662 By similarity
Disulfide bond1604 ↔ 1662Or C-1604 with C-1665 By similarity
Disulfide bond1616 ↔ 1622 By similarity
Cross-link1533S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651) By similarity
Cross-link1651S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533) By similarity

Experimental info

Sequence conflict261A → P in CAA29946. Ref.4
Sequence conflict1861S → L in CAA29946. Ref.4
Sequence conflict3191Q → S in CAA29946. Ref.4
Sequence conflict3691Q → L in CAA29946. Ref.4
Sequence conflict4031L → F in CAA29946. Ref.4
Sequence conflict4811P → L in CAA29946. Ref.4
Sequence conflict4931Q → H in CAA29946. Ref.4
Sequence conflict6211G → S in BAE27208. Ref.2
Sequence conflict7121S → I in CAA29946. Ref.4
Sequence conflict8131Q → E in AAA50292. Ref.1
Sequence conflict9821Q → H in CAA29946. Ref.4
Sequence conflict13971V → S in AAA37342. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P02463 [UniParc].

Last modified February 20, 2007. Version 4.
Checksum: EFEEC72AF301E5CF

FASTA1,669160,679
        10         20         30         40         50         60 
MGPRLSVWLL LLFAALLLHE ERSRAAAKGD CGGSGCGKCD CHGVKGQKGE RGLPGLQGVI 

        70         80         90        100        110        120 
GFPGMQGPEG PHGPPGQKGD AGEPGLPGTK GTRGPPGAAG YPGNPGLPGI PGQDGPPGPP 

       130        140        150        160        170        180 
GIPGCNGTKG ERGPLGPPGL PGFSGNPGPP GLPGMKGDPG EILGHVPGTL LKGERGFPGI 

       190        200        210        220        230        240 
PGMPGSPGLP GLQGPVGPPG FTGPPGPPGP PGPPGEKGQM GSSFQGPKGD KGEQGVSGPP 

       250        260        270        280        290        300 
GVPGQAQVKE KGDFAPTGEK GQKGEPGFPG VPGYGEKGEP GKQGPRGKPG KDGEKGERGS 

       310        320        330        340        350        360 
PGIPGDSGYP GLPGRQGPQG EKGEAGLPGP PGTVIGTMPL GEKGDRGYPG APGLRGEPGP 

       370        380        390        400        410        420 
KGFPGTPGQP GPPGFPTPGQ AGAPGFPGER GEKGDQGFPG VSLPGPSGRD GAPGPPGPPG 

       430        440        450        460        470        480 
PPGQPGHTNG IVECQPGPPG DQGPPGTPGQ PGLTGEVGQK GQKGESCLAC DTEGLRGPPG 

       490        500        510        520        530        540 
PQGPPGEIGF PGQPGAKGDR GLPGRDGLEG LPGPQGSPGL IGQPGAKGEP GEIFFDMRLK 

       550        560        570        580        590        600 
GDKGDPGFPG QPGMPGRAGT PGRDGHPGLP GPKGSPGSIG LKGERGPPGG VGFPGSRGDI 

       610        620        630        640        650        660 
GPPGPPGVGP IGPVGEKGQA GFPGGPGSPG LPGPKGEAGK VVPLPGPPGA AGLPGSPGFP 

       670        680        690        700        710        720 
GPQGDRGFPG TPGRPGIPGE KGAVGQPGIG FPGLPGPKGV DGLPGEIGRP GSPGRPGFNG 

       730        740        750        760        770        780 
LPGNPGPQGQ KGEPGIGLPG LKGQPGLPGI PGTPGEKGSI GGPGVPGEQG LTGPPGLQGI 

       790        800        810        820        830        840 
RGDPGPPGVQ GPAGPPGVPG IGPPGAMGPP GGQGPPGSSG PPGIKGEKGF PGFPGLDMPG 

       850        860        870        880        890        900 
PKGDKGSQGL PGLTGQSGLP GLPGQQGTPG VPGFPGSKGE MGVMGTPGQP GSPGPAGTPG 

       910        920        930        940        950        960 
LPGEKGDHGL PGSSGPRGDP GFKGDKGDVG LPGMPGSMEH VDMGSMKGQK GDQGEKGQIG 

       970        980        990       1000       1010       1020 
PTGDKGSRGD PGTPGVPGKD GQAGHPGQPG PKGDPGLSGT PGSPGLPGPK GSVGGMGLPG 

      1030       1040       1050       1060       1070       1080 
SPGEKGVPGI PGSQGVPGSP GEKGAKGEKG QSGLPGIGIP GRPGDKGDQG LAGFPGSPGE 

      1090       1100       1110       1120       1130       1140 
KGEKGSAGTP GMPGSPGPRG SPGNIGHPGS PGLPGEKGDK GLPGLDGVPG VKGEAGLPGT 

      1150       1160       1170       1180       1190       1200 
PGPTGPAGQK GEPGSDGIPG SAGEKGEQGV PGRGFPGFPG SKGDKGSKGE VGFPGLAGSP 

      1210       1220       1230       1240       1250       1260 
GIPGVKGEQG FMGPPGPQGQ PGLPGTPGHP VEGPKGDRGP QGQPGLPGHP GPMGPPGFPG 

      1270       1280       1290       1300       1310       1320 
INGPKGDKGN QGWPGAPGVP GPKGDPGFQG MPGIGGSPGI TGSKGDMGLP GVPGFQGQKG 

      1330       1340       1350       1360       1370       1380 
LPGLQGVKGD QGDQGVPGPK GLQGPPGPPG PYDVIKGEPG LPGPEGPPGL KGLQGPPGPK 

      1390       1400       1410       1420       1430       1440 
GQQGVTGSVG LPGPPGVPGF DGAPGQKGET GPFGPPGPRG FPGPPGPDGL PGSMGPPGTP 

      1450       1460       1470       1480       1490       1500 
SVDHGFLVTR HSQTTDDPLC PPGTKILYHG YSLLYVQGNE RAHGQDLGTA GSCLRKFSTM 

      1510       1520       1530       1540       1550       1560 
PFLFCNINNV CNFASRNDYS YWLSTPEPMP MSMAPISGDN IRPFISRCAV CEAPAMVMAV 

      1570       1580       1590       1600       1610       1620 
HSQTIQIPQC PNGWSSLWIG YSFVMHTSAG AEGSGQALAS PGSCLEEFRS APFIECHGRG 

      1630       1640       1650       1660 
TCNYYANAYS FWLATIERSE MFKKPTPSTL KAGELRTHVS RCQVCMRRT 

« Hide

References

« Hide 'large scale' references
[1]"The complete primary structure for the alpha 1-chain of mouse collagen IV. Differential evolution of collagen IV domains."
Muthukumaran G., Blumberg B., Kurkinen M.
J. Biol. Chem. 264:6310-6317(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].
Strain: C57BL/6 and C57BL/6J.
Tissue: Brain, Eye, Heart and Placenta.
[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].
Strain: C57BL/6 and FVB/N.
Tissue: Brain, Colon and Mammary gland.
[4]"cDNA clones completing the nucleotide and derived amino acid sequence of the alpha 1 chain of basement membrane (type IV) collagen from mouse."
Wood L., Theriault N., Vogeli G.
FEBS Lett. 227:5-8(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1154.
[5]"Structure of the amino-terminal portion of the murine alpha 1(IV) collagen chain and the corresponding region of the gene."
Killen P.D., Burbelo P.D., Sakurai Y., Yamada Y.
J. Biol. Chem. 263:8706-8709(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-129.
[6]"Characterization of the promoter for the alpha 1 (IV) collagen gene. DNA sequences within the first intron enhance transcription."
Killen P.D., Burbelo P.D., Martin G.R., Yamada Y.
J. Biol. Chem. 263:12310-12314(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[7]"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 1-28.
[8]"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] OF 1-28.
[9]"Alpha 1 type IV collagen gene evolved differently from fibrillar collagen genes."
Sakurai Y., Sullivan M., Yamada Y.
J. Biol. Chem. 261:6654-6657(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1110-1135.
[10]"Isolation of an alpha 1 type-IV collagen cDNA clone using a synthetic oligodeoxynucleotide."
Nath P., Laurent M., Horn E., Sobel M.E., Zon G., Vogeli G.
Gene 43:301-304(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1149-1424.
[11]"Amino acid sequence of the non-collagenous globular domain (NC1) of the alpha 1(IV) chain of basement membrane collagen as derived from complementary DNA."
Oberbaeumer I., Laurent M., Schwarz U., Sakurai Y., Yamada Y., Vogeli G., Voss T., Siebold B., Glanville R.W., Kuhn K.
Eur. J. Biochem. 147:217-224(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1276-1669.
[12]"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 1441-1669.
[13]"Mutations in Col4a1 cause perinatal cerebral hemorrhage and porencephaly."
Gould D.B., Phalan F.C., Breedveld G.J., van Mil S.E., Smith R.S., Schimenti J.C., Aguglia U., van der Knaap M.S., Heutink P., John S.W.M.
Science 308:1167-1171(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04694 mRNA. Translation: AAA50292.1.
AK142097 mRNA. Translation: BAE24936.1.
AK146487 mRNA. Translation: BAE27208.1.
AK147284 mRNA. Translation: BAE27820.1.
AK147355 mRNA. Translation: BAE27863.1.
AK147661 mRNA. Translation: BAE28055.1.
BC002269 mRNA. Translation: AAH02269.1.
BC056620 mRNA. Translation: AAH56620.1.
BC072650 mRNA. Translation: AAH72650.1. Sequence problems.
X06777 mRNA. Translation: CAA29946.1.
J03758 mRNA. Translation: AAA37439.1.
J03944 Genomic DNA. Translation: AAA37442.1.
J04448 Genomic DNA. Translation: AAA37437.1.
M23333 Genomic DNA. Translation: AAA51625.1.
M12879 Genomic DNA. Translation: AAA37343.1.
M13024 Genomic DNA. No translation available.
M13025 Genomic DNA. No translation available.
M13026 Genomic DNA. Translation: AAA37344.1.
M13027 Genomic DNA. Translation: AAA37345.1.
M13043 Genomic DNA. Translation: AAA37346.1.
M14042 mRNA. Translation: AAA37342.1.
X02201 mRNA. Translation: CAA26132.1.
M15832 mRNA. Translation: AAA37340.1.
CCDSCCDS40219.1.
PIRCGMS4B. A33525.
RefSeqNP_034061.2. NM_009931.2.
UniGeneMm.738.

3D structure databases

ProteinModelPortalP02463.
SMRP02463. Positions 1442-1669.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198816. 1 interaction.
IntActP02463. 1 interaction.
MINTMINT-4388747.

PTM databases

PhosphoSiteP02463.

Proteomic databases

MaxQBP02463.
PaxDbP02463.
PRIDEP02463.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033898; ENSMUSP00000033898; ENSMUSG00000031502.
GeneID12826.
KEGGmmu:12826.
UCSCuc009kvb.2. mouse.

Organism-specific databases

CTD1282.
MGIMGI:88454. Col4a1.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00720000108691.
HOVERGENHBG004933.
InParanoidP02463.
KOK06237.
OMAGVPGQKX.
OrthoDBEOG7RZ5P3.
PhylomeDBP02463.
TreeFamTF316865.

Enzyme and pathway databases

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

Gene expression databases

BgeeP02463.
CleanExMM_COL4A1.
GenevestigatorP02463.

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

NextBio282314.
PROP02463.
SOURCESearch...

Entry information

Entry nameCO4A1_MOUSE
AccessionPrimary (citable) accession number: P02463
Secondary accession number(s): Q3UHJ4 expand/collapse secondary AC list , Q3UJE7, Q3UQV2, Q53X35, Q6GQS7, Q6PHB5, Q99LQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 20, 2007
Last modified: July 9, 2014
This is version 140 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