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P02462 (CO4A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1669 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.12 Ref.17 Ref.18 Ref.19

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. Ref.12 Ref.17 Ref.18 Ref.19

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.

Tissue specificity

Highly expressed in placenta. Ref.12 Ref.17

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

Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in all cases and bind carbohydrates.

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.

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

Proteolytic processing produces the C-terminal NC1 peptide, arresten.

Involvement in disease

Brain small vessel disease with hemorrhage (BSVDH) [MIM:607595]: An autosomal dominant disease characterized by weakening of the blood vessels in the brain and retinal arteriolar tortuosity. In affected individuals, stroke is often the first symptom and is usually caused by bleeding in the brain (hemorrhagic stroke) rather than a lack of blood flow in the brain (ischemic stroke). Patients also have leukoencephalopathy and may experience seizures and migraine headaches accompanied by visual sensations known as auras.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 Ref.24 Ref.27 Ref.30 Ref.31

Hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC) [MIM:611773]: The clinical renal manifestations include hematuria and bilateral large cysts. Histologic analysis revealed complex basement membrane defects in kidney and skin. The systemic angiopathy appears to affect both small vessels and large arteries.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25 Ref.29

Porencephaly 1 (POREN1) [MIM:175780]: A neurologic disorder characterized by a fluid-filled cysts or cavities within the cerebral hemispheres, neurologic manifestations, facial paresis, and visual defects. Affected individuals typically have hemiplegia, seizures, and intellectual disability. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.22 Ref.28

Sequence similarities

Belongs to the type IV collagen family.

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

Ontologies

Keywords
   Biological processAngiogenesis
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainCollagen
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

basement membrane organization

Inferred from mutant phenotype Ref.25PubMed 19949034PubMed 23065703. Source: BHF-UCL

blood vessel morphogenesis

Inferred from mutant phenotype Ref.29. Source: BHF-UCL

brain development

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

collagen catabolic process

Traceable author statement. Source: Reactome

epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

neuromuscular junction development

Inferred from electronic annotation. Source: Ensembl

patterning of blood vessels

Inferred from mutant phenotype Ref.29. Source: BHF-UCL

renal tubule morphogenesis

Inferred from mutant phenotype Ref.25. Source: BHF-UCL

retinal blood vessel morphogenesis

Inferred from mutant phenotype Ref.29. Source: BHF-UCL

   Cellular_componentbasement membrane

Inferred by curator PubMed 23065703. Source: BHF-UCL

collagen type IV trimer

Inferred from mutant phenotype Ref.22. Source: BHF-UCL

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

   Molecular_functionextracellular matrix constituent conferring elasticity

Inferred by curator Ref.22. Source: BHF-UCL

extracellular matrix structural constituent

Inferred from mutant phenotype Ref.22Ref.29. Source: BHF-UCL

platelet-derived growth factor binding

Inferred from direct assay PubMed 8900172. Source: MGI

protein binding

Inferred from physical interaction Ref.20. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

COL4A2P085722EBI-2432478,EBI-2432506

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P02462-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P02462-2)

The sequence of this isoform differs from the canonical sequence as follows:
     498-848: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.6
Propeptide28 – 172145N-terminal propeptide (7S domain)
PRO_0000005748
Chain173 – 16691497Collagen alpha-1(IV) chain
PRO_0000005749
Chain1445 – 1669225Arresten
PRO_0000390482

Regions

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

Amino acid modifications

Glycosylation1261N-linked (GlcNAc...)
Disulfide bond1460 ↔ 1551 Ref.11
Disulfide bond1493 ↔ 1548 Ref.11
Disulfide bond1505 ↔ 1511 Ref.11
Disulfide bond1570 ↔ 1665 Ref.11
Disulfide bond1604 ↔ 1662 Ref.11
Disulfide bond1616 ↔ 1622 Ref.11
Cross-link1533S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651)
Cross-link1651S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533)

Natural variations

Alternative sequence498 – 848351Missing in isoform 2.
VSP_034644
Natural variant71V → L. Ref.32
Corresponds to variant rs9515185 [ dbSNP | Ensembl ].
VAR_030027
Natural variant3041P → L.
Corresponds to variant rs34843786 [ dbSNP | Ensembl ].
VAR_044158
Natural variant4981G → R in HANAC. Ref.29
VAR_064493
Natural variant4981G → V in HANAC. Ref.25
VAR_044159
Natural variant5101G → R in HANAC. Ref.29
VAR_064494
Natural variant5191G → R in HANAC. Ref.25
VAR_044160
Natural variant5251G → L in HANAC; requires 2 nucleotide substitutions. Ref.29
VAR_064495
Natural variant5281G → E in HANAC. Ref.25
VAR_044161
Natural variant5551T → P. Ref.1 Ref.3 Ref.4 Ref.7 Ref.32
Corresponds to variant rs536174 [ dbSNP | Ensembl ].
VAR_030511
Natural variant5621G → E in BSVDH. Ref.23
VAR_030028
Natural variant7201G → D in BSVDH; diffuse small vessel disease of the brain associated with Axenfeld-Rieger anomaly and leukoencephalopathy. Ref.24 Ref.30
VAR_064496
Natural variant7491G → S in POREN1. Ref.21
VAR_030029
Natural variant7551G → R in BSVDH; associated with ocular anomalies of variable severity in some patients. Ref.30 Ref.31
VAR_064497
Natural variant8051G → R in BSVDH. Ref.27
VAR_064498
Natural variant11301G → D in POREN1. Ref.22
VAR_030030
Natural variant12361G → R in POREN1. Ref.21
VAR_030031
Natural variant13341Q → H. Ref.3 Ref.32
Corresponds to variant rs3742207 [ dbSNP | Ensembl ].
VAR_020013
Natural variant14231G → R in POREN1. Ref.22
VAR_030032
Natural variant15801G → R in POREN1. Ref.28
VAR_064499

Experimental info

Sequence conflict237 – 2382SG → KE AA sequence Ref.6
Sequence conflict2411G → K AA sequence Ref.6
Sequence conflict3191Q → A in CAA29075. Ref.4
Sequence conflict7191N → D AA sequence Ref.8
Sequence conflict8371D → Y AA sequence Ref.8
Sequence conflict8421K → P AA sequence Ref.8
Sequence conflict8961V → W in CAA68698. Ref.7
Sequence conflict9041E → Q AA sequence Ref.8
Sequence conflict9141S → K AA sequence Ref.8
Sequence conflict9981S → K AA sequence Ref.8
Sequence conflict10101K → P AA sequence Ref.8
Sequence conflict10121S → K AA sequence Ref.8
Sequence conflict13581E → Q AA sequence Ref.8
Sequence conflict14901A → T in ABE73157. Ref.17
Sequence conflict15071I → T in ABE73157. Ref.17
Sequence conflict15191Y → C in ABE73157. Ref.17
Sequence conflict15701C → Y in AAM97359. Ref.16

Secondary structure

................................................. 1669
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 6, 2007. Version 3.
Checksum: 3C9BCD8E410A9ED1

FASTA1,669160,615
        10         20         30         40         50         60 
MGPRLSVWLL LLPAALLLHE EHSRAAAKGG CAGSGCGKCD CHGVKGQKGE RGLPGLQGVI 

        70         80         90        100        110        120 
GFPGMQGPEG PQGPPGQKGD TGEPGLPGTK GTRGPPGASG YPGNPGLPGI PGQDGPPGPP 

       130        140        150        160        170        180 
GIPGCNGTKG ERGPLGPPGL PGFAGNPGPP GLPGMKGDPG EILGHVPGML LKGERGFPGI 

       190        200        210        220        230        240 
PGTPGPPGLP GLQGPVGPPG FTGPPGPPGP PGPPGEKGQM GLSFQGPKGD KGDQGVSGPP 

       250        260        270        280        290        300 
GVPGQAQVQE KGDFATKGEK GQKGEPGFQG MPGVGEKGEP GKPGPRGKPG KDGDKGEKGS 

       310        320        330        340        350        360 
PGFPGEPGYP GLIGRQGPQG EKGEAGPPGP PGIVIGTGPL GEKGERGYPG TPGPRGEPGP 

       370        380        390        400        410        420 
KGFPGLPGQP GPPGLPVPGQ AGAPGFPGER GEKGDRGFPG TSLPGPSGRD GLPGPPGSPG 

       430        440        450        460        470        480 
PPGQPGYTNG IVECQPGPPG DQGPPGIPGQ PGFIGEIGEK GQKGESCLIC DIDGYRGPPG 

       490        500        510        520        530        540 
PQGPPGEIGF PGQPGAKGDR GLPGRDGVAG VPGPQGTPGL IGQPGAKGEP GEFYFDLRLK 

       550        560        570        580        590        600 
GDKGDPGFPG QPGMTGRAGS PGRDGHPGLP GPKGSPGSVG LKGERGPPGG VGFPGSRGDT 

       610        620        630        640        650        660 
GPPGPPGYGP AGPIGDKGQA GFPGGPGSPG LPGPKGEPGK IVPLPGPPGA EGLPGSPGFP 

       670        680        690        700        710        720 
GPQGDRGFPG TPGRPGLPGE KGAVGQPGIG FPGPPGPKGV DGLPGDMGPP GTPGRPGFNG 

       730        740        750        760        770        780 
LPGNPGVQGQ KGEPGVGLPG LKGLPGLPGI PGTPGEKGSI GVPGVPGEHG AIGPPGLQGI 

       790        800        810        820        830        840 
RGEPGPPGLP GSVGSPGVPG IGPPGARGPP GGQGPPGLSG PPGIKGEKGF PGFPGLDMPG 

       850        860        870        880        890        900 
PKGDKGAQGL PGITGQSGLP GLPGQQGAPG IPGFPGSKGE MGVMGTPGQP GSPGPVGAPG 

       910        920        930        940        950        960 
LPGEKGDHGF PGSSGPRGDP GLKGDKGDVG LPGKPGSMDK VDMGSMKGQK GDQGEKGQIG 

       970        980        990       1000       1010       1020 
PIGEKGSRGD PGTPGVPGKD GQAGQPGQPG PKGDPGISGT PGAPGLPGPK GSVGGMGLPG 

      1030       1040       1050       1060       1070       1080 
TPGEKGVPGI PGPQGSPGLP GDKGAKGEKG QAGPPGIGIP GLRGEKGDQG IAGFPGSPGE 

      1090       1100       1110       1120       1130       1140 
KGEKGSIGIP GMPGSPGLKG SPGSVGYPGS PGLPGEKGDK GLPGLDGIPG VKGEAGLPGT 

      1150       1160       1170       1180       1190       1200 
PGPTGPAGQK GEPGSDGIPG SAGEKGEPGL PGRGFPGFPG AKGDKGSKGE VGFPGLAGSP 

      1210       1220       1230       1240       1250       1260 
GIPGSKGEQG FMGPPGPQGQ PGLPGSPGHA TEGPKGDRGP QGQPGLPGLP GPMGPPGLPG 

      1270       1280       1290       1300       1310       1320 
IDGVKGDKGN PGWPGAPGVP GPKGDPGFQG MPGIGGSPGI TGSKGDMGPP GVPGFQGPKG 

      1330       1340       1350       1360       1370       1380 
LPGLQGIKGD QGDQGVPGAK GLPGPPGPPG PYDIIKGEPG LPGPEGPPGL KGLQGLPGPK 

      1390       1400       1410       1420       1430       1440 
GQQGVTGLVG IPGPPGIPGF DGAPGQKGEM GPAGPTGPRG FPGPPGPDGL PGSMGPPGTP 

      1450       1460       1470       1480       1490       1500 
SVDHGFLVTR HSQTIDDPQC PSGTKILYHG YSLLYVQGNE RAHGQDLGTA GSCLRKFSTM 

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

      1570       1580       1590       1600       1610       1620 
HSQTIQIPPC PSGWSSLWIG YSFVMHTSAG AEGSGQALAS PGSCLEEFRS APFIECHGRG 

      1630       1640       1650       1660 
TCNYYANAYS FWLATIERSE MFKKPTPSTL KAGELRTHVS RCQVCMRRT 

« Hide

Isoform 2 [UniParc].

Checksum: E313ADCF65DA7BEC
Show »

FASTA1,318127,981

References

« Hide 'large scale' references
[1]"Structural organization of the gene for the alpha 1 chain of human type IV collagen."
Soininen R., Huotari M., Ganguly A., Prockop D.J., Tryggvason K.
J. Biol. Chem. 264:13565-13571(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-555.
[2]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1), VARIANTS PRO-555 AND HIS-1334.
Tissue: Brain.
[4]"Completion of the amino acid sequence of the alpha 1 chain of human basement membrane collagen (type IV) reveals 21 non-triplet interruptions located within the collagenous domain."
Brazel D., Oberbaeumer I., Dieringer H., Babel W., Glanville R.W., Deutzmann R., Kuehn K.
Eur. J. Biochem. 168:529-536(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-943, VARIANT PRO-555.
Tissue: Placenta.
[5]"The structural genes for alpha 1 and alpha 2 chains of human type IV collagen are divergently encoded on opposite DNA strands and have an overlapping promoter region."
Soininen R., Huotari M., Hostikka S.L., Prockop D.J., Tryggvason K.
J. Biol. Chem. 263:17217-17220(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[6]"Amino acid sequence of the N-terminal aggregation and cross-linking region (7S domain) of the alpha 1 (IV) chain of human basement membrane collagen."
Glanville R.W., Qian R.Q., Siebold B., Risteli J., Kuehn K.
Eur. J. Biochem. 152:213-219(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-243.
[7]"Complete primary structure of the alpha 1-chain of human basement membrane (type IV) collagen."
Soininen R., Haka-Risku T., Prockop D.J., Tryggvason K.
FEBS Lett. 225:188-194(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-1257, VARIANT PRO-555.
Tissue: Placenta.
[8]"Structure of human-basement-membrane (type IV) collagen. Complete amino-acid sequence of a 914-residue-long pepsin fragment from the alpha 1(IV) chain."
Babel W., Glanville R.W.
Eur. J. Biochem. 143:545-556(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 534-1447.
[9]"cDNA clones coding for the pro-alpha1(IV) chain of human type IV procollagen reveal an unusual homology of amino acid sequences in two halves of the carboxyl-terminal domain."
Pihlajaniemi T., Tryggvason K., Myers J.C., Kurkinen M., Lebo R., Cheung M.-C., Prockop D.J., Boyd C.D.
J. Biol. Chem. 260:7681-7687(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1256-1669.
[10]"Restricted homology between human alpha 1 type IV and other procollagen chains."
Brinker J.M., Gudas L.J., Loidl H.R., Wang S.-Y., Rosenbloom J., Kefalides N.A., Myers J.C.
Proc. Natl. Acad. Sci. U.S.A. 82:3649-3653(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1259-1669.
[11]"The arrangement of intra- and intermolecular disulfide bonds in the carboxyterminal, non-collagenous aggregation and cross-linking domain of basement-membrane type IV collagen."
Siebold B., Deutzmann R., Kuehn K.
Eur. J. Biochem. 176:617-624(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1441-1669, DISULFIDE BONDS.
Tissue: Placenta.
[12]"Anti-angiogenic cues from vascular basement membrane collagen."
Colorado P.C., Torre A., Kamphaus G., Maeshima Y., Hopfer H., Takahashi K., Volk R., Zamborsky E.D., Herman S., Sarkar P.K., Ericksen M.B., Dhanabal M., Simons M., Post M., Kufe D.W., Weichselbaum R.R., Sukhatme V.P., Kalluri R.
Cancer Res. 60:2520-2526(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669, FUNCTION OF ARRESTEN, TISSUE SPECIFICITY.
[13]"Arresten, a collagen-derived inhibitor of angiogenesis."
Fu J., Bai X., Wang W., Ruan C.
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
[14]Peng X., Yin B., Yuan J., Qiang B.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
[15]"Molecular cloning and sequencing of human arresten gene."
Zheng Q.C., Song Z.F., Zheng Y.W., Li Y.Q., Shu X.
Zhonghua Shi Yan Wai Ke Za Zhi 19:46-47(2002)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
[16]"Cloning and expression of arresten in Escherichia coli and Pachia pastoris."
He A.B.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
[17]"Construction of recombinant plasmid and prokaryotic expression in E. coli and biological activity analysis of human placenta arresten gene."
Zheng J.P., Tang H.Y., Chen X.J., Yu B.F., Xie J., Wu T.C.
Hepatobiliary Pancreat. Dis. Int. 5:74-79(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669, FUNCTION, TISSUE SPECIFICITY.
Tissue: Placenta.
[18]"Human alpha1 type IV collagen NC1 domain exhibits distinct antiangiogenic activity mediated by alpha1beta1 integrin."
Sudhakar A., Nyberg P., Keshamouni V.G., Mannam A.P., Li J., Sugimoto H., Cosgrove D., Kalluri R.
J. Clin. Invest. 115:2801-2810(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF RECEPTOR, FUNCTION OF ARRESTEN.
[19]"Characterization of the anti-angiogenic properties of arresten, an alpha1beta1 integrin-dependent collagen-derived tumor suppressor."
Nyberg P., Xie L., Sugimoto H., Colorado P., Sund M., Holthaus K., Sudhakar A., Salo T., Kalluri R.
Exp. Cell Res. 314:3292-3305(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF RECEPTOR, FUNCTION OF ARRESTEN.
[20]"The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link."
Than M.E., Henrich S., Huber R., Ries A., Mann K., Kuhn K., Timpl R., Bourenkov G.P., Bartunik H.D., Bode W.
Proc. Natl. Acad. Sci. U.S.A. 99:6607-6612(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1441-1669, ADDITIONAL INTERCHAIN LINKS.
[21]"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: VARIANTS POREN1 SER-749 AND ARG-1236.
[22]"Novel mutations in three families confirm a major role of COL4A1 in hereditary porencephaly."
Breedveld G., de Coo I.F., Lequin M.H., Arts W.F.M., Heutink P., Gould D.B., John S.W.M., Oostra B., Mancini G.M.S.
J. Med. Genet. 43:490-495(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS POREN1 ASP-1130 AND ARG-1423.
[23]"Role of COL4A1 in small-vessel disease and hemorrhagic stroke."
Gould D.B., Phalan F.C., van Mil S.E., Sundberg J.P., Vahedi K., Massin P., Bousser M.G., Heutink P., Miner J.H., Tournier-Lasserve E., John S.W.M.
N. Engl. J. Med. 354:1489-1496(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSVDH GLU-562.
[24]"COL4A1 mutation in Axenfeld-Rieger anomaly with leukoencephalopathy and stroke."
Sibon I., Coupry I., Menegon P., Bouchet J.P., Gorry P., Burgelin I., Calvas P., Orignac I., Dousset V., Lacombe D., Orgogozo J.M., Arveiler B., Goizet C.
Ann. Neurol. 62:177-184(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSVDH ASP-720.
[25]"COL4A1 mutations and hereditary angiopathy, nephropathy, aneurysms, and muscle cramps."
Plaisier E., Gribouval O., Alamowitch S., Mougenot B., Prost C., Verpont M.C., Marro B., Desmettre T., Cohen S.Y., Roullet E., Dracon M., Fardeau M., Van Agtmael T., Kerjaschki D., Antignac C., Ronco P.
N. Engl. J. Med. 357:2687-2695(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HANAC VAL-498; ARG-519 AND GLU-528.
[26]"A sulfilimine bond identified in collagen IV."
Vanacore R., Ham A.-J.L., Voehler M., Sanders C.R., Conrads T.P., Veenstra T.D., Sharpless K.B., Dawson P.E., Hudson B.G.
Science 325:1230-1234(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERCHAIN SULFILIMINE BONDS.
[27]"COL4A1 mutation in a patient with sporadic, recurrent intracerebral hemorrhage."
Vahedi K., Kubis N., Boukobza M., Arnoult M., Massin P., Tournier-Lasserve E., Bousser M.G.
Stroke 38:1461-1464(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSVDH ARG-805.
[28]"COL4A1 mutation in two preterm siblings with antenatal onset of parenchymal hemorrhage."
de Vries L.S., Koopman C., Groenendaal F., Van Schooneveld M., Verheijen F.W., Verbeek E., Witkamp T.D., van der Worp H.B., Mancini G.
Ann. Neurol. 65:12-18(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT POREN1 ARG-1580.
[29]"Novel COL4A1 mutations associated with HANAC syndrome: a role for the triple helical CB3[IV] domain."
Plaisier E., Chen Z., Gekeler F., Benhassine S., Dahan K., Marro B., Alamowitch S., Paques M., Ronco P.
Am. J. Med. Genet. A 152:2550-2555(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HANAC ARG-498; ARG-510 AND LEU-525.
[30]"Ophthalmological features associated with COL4A1 mutations."
Coupry I., Sibon I., Mortemousque B., Rouanet F., Mine M., Goizet C.
Arch. Ophthalmol. 128:483-489(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BSVDH ASP-720 AND ARG-755.
[31]"A dominantly inherited mutation in collagen IV A1 (COL4A1) causing childhood onset stroke without porencephaly."
Shah S., Kumar Y., McLean B., Churchill A., Stoodley N., Rankin J., Rizzu P., van der Knaap M., Jardine P.
Eur. J. Paediatr. Neurol. 14:182-187(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSVDH ARG-755.
[32]"Sequence variants in COL4A1 and COL4A2 genes in Ecuadorian families with keratoconus."
Karolak J.A., Kulinska K., Nowak D.M., Pitarque J.A., Molinari A., Rydzanicz M., Bejjani B.A., Gajecka M.
Mol. Vis. 17:827-843(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LEU-7; PRO-555 AND HIS-1334.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26576 expand/collapse EMBL AC list , J04217, M26550, M26540, M26542, M26543, M26544, M26545, M26546, M26547, M26537, M26538, M26548, M26549, M26551, M26552, M26553, M26554, M26555, M26556, M26557, M26539, M26558, M26559, M26560, M26561, M26562, M26536, M26563, M26541, M26564, M26565, M26566, M26567, M26568, M26569, M26570, M26571, M26572, M26573, M26574, M26575 Genomic DNA. Translation: AAA53098.1.
AL161773, AL390755 Genomic DNA. Translation: CAH71365.1.
AL390755, AL161773 Genomic DNA. Translation: CAH74130.1.
AL161773, AL390755 Genomic DNA. Translation: CAM14222.1.
AL390755, AL161773 Genomic DNA. Translation: CAM20295.1.
BC047305 mRNA. Translation: AAH47305.1.
BC151220 mRNA. Translation: AAI51221.1.
X05561 mRNA. Translation: CAA29075.1.
Y00706 mRNA. Translation: CAA68698.1.
M10940 mRNA. Translation: AAA52006.1.
M11315 mRNA. Translation: AAA52042.1.
AF258349 mRNA. Translation: AAF72630.1.
AF363672 mRNA. Translation: AAK53382.1.
AF400431 mRNA. Translation: AAK92480.1.
AY285780 mRNA. Translation: AAP43112.1.
AF536207 mRNA. Translation: AAM97359.1.
DQ464183 mRNA. Translation: ABE73157.1.
CCDSCCDS9511.1. [P02462-1]
PIRCGHU4B. S16876.
RefSeqNP_001836.2. NM_001845.4. [P02462-1]
UniGeneHs.17441.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LI1X-ray1.90A/B/D/E1441-1669[»]
ProteinModelPortalP02462.
SMRP02462. Positions 1442-1669.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107679. 14 interactions.
IntActP02462. 24 interactions.
MINTMINT-6743187.
STRING9606.ENSP00000364979.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP02462.

Polymorphism databases

DMDM125987809.

Proteomic databases

MaxQBP02462.
PaxDbP02462.
PRIDEP02462.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375820; ENSP00000364979; ENSG00000187498. [P02462-1]
GeneID1282.
KEGGhsa:1282.
UCSCuc001vqw.4. human. [P02462-1]

Organism-specific databases

CTD1282.
GeneCardsGC13M110801.
GeneReviewsCOL4A1.
HGNCHGNC:2202. COL4A1.
HPACAB001695.
HPA054039.
MIM120130. gene.
175780. phenotype.
607595. phenotype.
611773. phenotype.
neXtProtNX_P02462.
Orphanet73229. Autosomal dominant familial hematuria - retinal arteriolar tortuosity - contractures.
99810. Familial porencephaly.
36383. Familial vascular leukoencephalopathy.
799. Schizencephaly.
899. Walker-Warburg syndrome.
PharmGKBPA26717.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG004933.
KOK06237.
OMASSMDHGF.
OrthoDBEOG7RZ5P3.
PhylomeDBP02462.
TreeFamTF316865.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP02462.
BgeeP02462.
CleanExHS_COL4A1.
GenevestigatorP02462.

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

Other

ChiTaRSCOL4A1. human.
EvolutionaryTraceP02462.
GeneWikiCollagen,_type_IV,_alpha_1.
GenomeRNAi1282.
NextBio5181.
PROP02462.
SOURCESearch...

Entry information

Entry nameCO4A1_HUMAN
AccessionPrimary (citable) accession number: P02462
Secondary accession number(s): A7E2W4 expand/collapse secondary AC list , B1AM70, Q1P9S9, Q5VWF6, Q86X41, Q8NF88, Q9NYC5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 6, 2007
Last modified: July 9, 2014
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM