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Protein

Collagen alpha-1(IV) chain

Gene

COL4A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.
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.

GO - Molecular functioni

  • extracellular matrix constituent conferring elasticity Source: BHF-UCL
  • extracellular matrix structural constituent Source: BHF-UCL
  • platelet-derived growth factor binding Source: MGI

GO - Biological processi

  • basement membrane organization Source: BHF-UCL
  • blood vessel morphogenesis Source: BHF-UCL
  • brain development Source: BHF-UCL
  • cellular response to amino acid stimulus Source: Ensembl
  • collagen-activated tyrosine kinase receptor signaling pathway Source: Ensembl
  • collagen catabolic process Source: Reactome
  • epithelial cell differentiation Source: Ensembl
  • extracellular matrix organization Source: Reactome
  • neuromuscular junction development Source: Ensembl
  • patterning of blood vessels Source: BHF-UCL
  • renal tubule morphogenesis Source: BHF-UCL
  • retinal blood vessel morphogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Angiogenesis

Enzyme and pathway databases

BioCyciZFISH:G66-33301-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474244. Extracellular matrix organization.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-186797. Signaling by PDGF.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-2214320. Anchoring fibril formation.
R-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-419037. NCAM1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(IV) chain
Cleaved into the following chain:
Gene namesi
Name:COL4A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:2202. COL4A1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: BHF-UCL
  • collagen type IV trimer Source: BHF-UCL
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Brain small vessel disease with or without ocular anomalies (BSVD)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:607595
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030028562G → E in BSVD. 1 Publication1
Natural variantiVAR_073813708G → R in BSVD. 1 Publication1
Natural variantiVAR_064496720G → D in BSVD; diffuse small vessel disease of the brain associated with Axenfeld-Rieger anomaly and leukoencephalopathy. 2 Publications1
Natural variantiVAR_064497755G → R in BSVD; associated with ocular anomalies of variable severity in some patients. 3 Publications1
Natural variantiVAR_073814773G → R in BSVD. 2 Publications1
Natural variantiVAR_064498805G → R in BSVD. 1 Publication1
Natural variantiVAR_073816882G → D in BSVD. 1 Publication1
Natural variantiVAR_0738211266G → R in BSVD. 1 Publication1
Natural variantiVAR_0738261627N → K in BSVD. 1 Publication1
Hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionThe 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.
See also OMIM:611773
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_064493498G → R in HANAC. 1 Publication1
Natural variantiVAR_044159498G → V in HANAC. 1 Publication1
Natural variantiVAR_064494510G → R in HANAC and RATOR. 2 Publications1
Natural variantiVAR_044160519G → R in HANAC. 1 Publication1
Natural variantiVAR_064495525G → L in HANAC; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_044161528G → E in HANAC. 1 Publication1
Porencephaly 1 (POREN1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:175780
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030029749G → S in POREN1. 1 Publication1
Natural variantiVAR_0300301130G → D in POREN1. 1 Publication1
Natural variantiVAR_0300311236G → R in POREN1. 1 Publication1
Natural variantiVAR_0300321423G → R in POREN1. 1 Publication1
Natural variantiVAR_0644991580G → R in POREN1. 1 Publication1
Intracerebral hemorrhage (ICH)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.
See also OMIM:614519
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073810352P → L in ICH; the mutant protein is retained intracellularly and is not secreted normally. 1 Publication1
Natural variantiVAR_073811538R → G in ICH; the mutant protein is retained intracellularly and is not secreted normally. 1 Publication1
Tortuosity of retinal arteries (RATOR)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by marked tortuosity of second- and third-order retinal arteries with normal first-order arteries and venous system. Most patients manifest variable degrees of symptomatic transient vision loss due to retinal hemorrhage following minor stress or trauma.
See also OMIM:180000
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_064494510G → R in HANAC and RATOR. 2 Publications1
Schizencephaly (SCHZC)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionExtremely rare human congenital disorder characterized by a full-thickness cleft within the cerebral hemispheres. These clefts are lined with gray matter and most commonly involve the parasylvian regions. Large portions of the cerebral hemispheres may be absent and replaced by cerebro-spinal fluid.
See also OMIM:269160
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073812655G → R in SCHZC. 1 Publication1
Natural variantiVAR_073815870G → R in SCHZC. 1 Publication1
Natural variantiVAR_073817897G → S in SCHZC. 1 Publication1
Natural variantiVAR_073818948G → S in SCHZC. 1 Publication1
Natural variantiVAR_0738191041G → E in SCHZC. 1 Publication1
Natural variantiVAR_0738201082G → E in SCHZC. 1 Publication1
Natural variantiVAR_0738221326G → R in SCHZC. 1 Publication1
Natural variantiVAR_0738231332G → D in SCHZC. 1 Publication1
Natural variantiVAR_0738251615E → K in SCHZC. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1282.
MalaCardsiCOL4A1.
MIMi175780. phenotype.
180000. phenotype.
269160. phenotype.
607595. phenotype.
611773. phenotype.
614519. phenotype.
Orphaneti73229. Autosomal dominant familial hematuria - retinal arteriolar tortuosity - contractures.
99810. Familial porencephaly.
36383. Familial vascular leukoencephalopathy.
799. Schizencephaly.
899. Walker-Warburg syndrome.
PharmGKBiPA26717.

Chemistry databases

ChEMBLiCHEMBL2364188.

Polymorphism and mutation databases

BioMutaiCOL4A1.
DMDMi125987809.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
PropeptideiPRO_000000574828 – 172N-terminal propeptide (7S domain)Add BLAST145
ChainiPRO_0000005749173 – 1669Collagen alpha-1(IV) chainAdd BLAST1497
ChainiPRO_00003904821445 – 1669ArrestenAdd BLAST225

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi126N-linked (GlcNAc...)1
Disulfide bondi1460 ↔ 1551PROSITE-ProRule annotation1 Publication
Disulfide bondi1493 ↔ 1548PROSITE-ProRule annotation1 Publication
Disulfide bondi1505 ↔ 1511PROSITE-ProRule annotation1 Publication
Cross-linki1533S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651)
Disulfide bondi1570 ↔ 1665PROSITE-ProRule annotation1 Publication
Disulfide bondi1604 ↔ 1662PROSITE-ProRule annotation1 Publication
Disulfide bondi1616 ↔ 1622PROSITE-ProRule annotation1 Publication
Cross-linki1651S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533)

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

EPDiP02462.
MaxQBiP02462.
PaxDbiP02462.
PeptideAtlasiP02462.
PRIDEiP02462.

PTM databases

iPTMnetiP02462.
PhosphoSitePlusiP02462.
SwissPalmiP02462.

Expressioni

Tissue specificityi

Highly expressed in placenta.2 Publications

Gene expression databases

BgeeiENSG00000187498.
CleanExiHS_COL4A1.
ExpressionAtlasiP02462. baseline and differential.
GenevisibleiP02462. HS.

Organism-specific databases

HPAiCAB001695.
HPA054039.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
COL4A2P085722EBI-2432478,EBI-2432506

GO - Molecular functioni

  • platelet-derived growth factor binding Source: MGI

Protein-protein interaction databases

BioGridi107679. 21 interactors.
IntActiP02462. 26 interactors.
MINTiMINT-6743187.
STRINGi9606.ENSP00000364979.

Structurei

Secondary structure

11669
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1446 – 1451Combined sources6
Beta strandi1453 – 1456Combined sources4
Beta strandi1465 – 1478Combined sources14
Beta strandi1481 – 1484Combined sources4
Helixi1490 – 1492Combined sources3
Beta strandi1493 – 1496Combined sources4
Beta strandi1502 – 1505Combined sources4
Beta strandi1509 – 1514Combined sources6
Beta strandi1519 – 1524Combined sources6
Helixi1538 – 1544Combined sources7
Beta strandi1547 – 1555Combined sources9
Beta strandi1557 – 1561Combined sources5
Beta strandi1563 – 1566Combined sources4
Beta strandi1574 – 1587Combined sources14
Helixi1589 – 1591Combined sources3
Beta strandi1593 – 1595Combined sources3
Helixi1601 – 1603Combined sources3
Beta strandi1604 – 1607Combined sources4
Beta strandi1613 – 1617Combined sources5
Beta strandi1620 – 1623Combined sources4
Beta strandi1629 – 1634Combined sources6
Helixi1638 – 1640Combined sources3
Beta strandi1648 – 1651Combined sources4
Helixi1655 – 1658Combined sources4
Beta strandi1661 – 1667Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LI1X-ray1.90A/B/D/E1441-1669[»]
ProteinModelPortaliP02462.
SMRiP02462.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02462.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1445 – 1669Collagen IV NC1PROSITE-ProRule annotationAdd BLAST225

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni173 – 1440Triple-helical regionAdd BLAST1268

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

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
HOVERGENiHBG004933.
InParanoidiP02462.
KOiK06237.
OrthoDBiEOG091G0613.
PhylomeDBiP02462.
TreeFamiTF316865.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR008160. Collagen.
IPR001442. Collagen_VI_NC.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 15 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P02462-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGPRLSVWLL LLPAALLLHE EHSRAAAKGG CAGSGCGKCD CHGVKGQKGE
60 70 80 90 100
RGLPGLQGVI GFPGMQGPEG PQGPPGQKGD TGEPGLPGTK GTRGPPGASG
110 120 130 140 150
YPGNPGLPGI PGQDGPPGPP GIPGCNGTKG ERGPLGPPGL PGFAGNPGPP
160 170 180 190 200
GLPGMKGDPG EILGHVPGML LKGERGFPGI PGTPGPPGLP GLQGPVGPPG
210 220 230 240 250
FTGPPGPPGP PGPPGEKGQM GLSFQGPKGD KGDQGVSGPP GVPGQAQVQE
260 270 280 290 300
KGDFATKGEK GQKGEPGFQG MPGVGEKGEP GKPGPRGKPG KDGDKGEKGS
310 320 330 340 350
PGFPGEPGYP GLIGRQGPQG EKGEAGPPGP PGIVIGTGPL GEKGERGYPG
360 370 380 390 400
TPGPRGEPGP KGFPGLPGQP GPPGLPVPGQ AGAPGFPGER GEKGDRGFPG
410 420 430 440 450
TSLPGPSGRD GLPGPPGSPG PPGQPGYTNG IVECQPGPPG DQGPPGIPGQ
460 470 480 490 500
PGFIGEIGEK GQKGESCLIC DIDGYRGPPG PQGPPGEIGF PGQPGAKGDR
510 520 530 540 550
GLPGRDGVAG VPGPQGTPGL IGQPGAKGEP GEFYFDLRLK GDKGDPGFPG
560 570 580 590 600
QPGMTGRAGS PGRDGHPGLP GPKGSPGSVG LKGERGPPGG VGFPGSRGDT
610 620 630 640 650
GPPGPPGYGP AGPIGDKGQA GFPGGPGSPG LPGPKGEPGK IVPLPGPPGA
660 670 680 690 700
EGLPGSPGFP GPQGDRGFPG TPGRPGLPGE KGAVGQPGIG FPGPPGPKGV
710 720 730 740 750
DGLPGDMGPP GTPGRPGFNG LPGNPGVQGQ KGEPGVGLPG LKGLPGLPGI
760 770 780 790 800
PGTPGEKGSI GVPGVPGEHG AIGPPGLQGI RGEPGPPGLP GSVGSPGVPG
810 820 830 840 850
IGPPGARGPP GGQGPPGLSG PPGIKGEKGF PGFPGLDMPG PKGDKGAQGL
860 870 880 890 900
PGITGQSGLP GLPGQQGAPG IPGFPGSKGE MGVMGTPGQP GSPGPVGAPG
910 920 930 940 950
LPGEKGDHGF PGSSGPRGDP GLKGDKGDVG LPGKPGSMDK VDMGSMKGQK
960 970 980 990 1000
GDQGEKGQIG PIGEKGSRGD PGTPGVPGKD GQAGQPGQPG PKGDPGISGT
1010 1020 1030 1040 1050
PGAPGLPGPK GSVGGMGLPG TPGEKGVPGI PGPQGSPGLP GDKGAKGEKG
1060 1070 1080 1090 1100
QAGPPGIGIP GLRGEKGDQG IAGFPGSPGE KGEKGSIGIP GMPGSPGLKG
1110 1120 1130 1140 1150
SPGSVGYPGS PGLPGEKGDK GLPGLDGIPG VKGEAGLPGT PGPTGPAGQK
1160 1170 1180 1190 1200
GEPGSDGIPG SAGEKGEPGL PGRGFPGFPG AKGDKGSKGE VGFPGLAGSP
1210 1220 1230 1240 1250
GIPGSKGEQG FMGPPGPQGQ PGLPGSPGHA TEGPKGDRGP QGQPGLPGLP
1260 1270 1280 1290 1300
GPMGPPGLPG IDGVKGDKGN PGWPGAPGVP GPKGDPGFQG MPGIGGSPGI
1310 1320 1330 1340 1350
TGSKGDMGPP GVPGFQGPKG LPGLQGIKGD QGDQGVPGAK GLPGPPGPPG
1360 1370 1380 1390 1400
PYDIIKGEPG LPGPEGPPGL KGLQGLPGPK GQQGVTGLVG IPGPPGIPGF
1410 1420 1430 1440 1450
DGAPGQKGEM GPAGPTGPRG FPGPPGPDGL PGSMGPPGTP SVDHGFLVTR
1460 1470 1480 1490 1500
HSQTIDDPQC PSGTKILYHG YSLLYVQGNE RAHGQDLGTA GSCLRKFSTM
1510 1520 1530 1540 1550
PFLFCNINNV CNFASRNDYS YWLSTPEPMP MSMAPITGEN IRPFISRCAV
1560 1570 1580 1590 1600
CEAPAMVMAV HSQTIQIPPC PSGWSSLWIG YSFVMHTSAG AEGSGQALAS
1610 1620 1630 1640 1650
PGSCLEEFRS APFIECHGRG TCNYYANAYS FWLATIERSE MFKKPTPSTL
1660
KAGELRTHVS RCQVCMRRT
Length:1,669
Mass (Da):160,615
Last modified:February 6, 2007 - v3
Checksum:i3C9BCD8E410A9ED1
GO
Isoform 2 (identifier: P02462-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     498-848: Missing.

Note: No experimental confirmation available.
Show »
Length:1,318
Mass (Da):127,981
Checksum:iE313ADCF65DA7BEC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti237 – 238SG → KE AA sequence (PubMed:4043082).Curated2
Sequence conflicti241G → K AA sequence (PubMed:4043082).Curated1
Sequence conflicti319Q → A in CAA29075 (PubMed:3311751).Curated1
Sequence conflicti719N → D AA sequence (PubMed:6434307).Curated1
Sequence conflicti837D → Y AA sequence (PubMed:6434307).Curated1
Sequence conflicti842K → P AA sequence (PubMed:6434307).Curated1
Sequence conflicti896V → W in CAA68698 (PubMed:3691802).Curated1
Sequence conflicti904E → Q AA sequence (PubMed:6434307).Curated1
Sequence conflicti914S → K AA sequence (PubMed:6434307).Curated1
Sequence conflicti998S → K AA sequence (PubMed:6434307).Curated1
Sequence conflicti1010K → P AA sequence (PubMed:6434307).Curated1
Sequence conflicti1012S → K AA sequence (PubMed:6434307).Curated1
Sequence conflicti1358E → Q AA sequence (PubMed:6434307).Curated1
Sequence conflicti1490A → T in ABE73157 (PubMed:16481288).Curated1
Sequence conflicti1507I → T in ABE73157 (PubMed:16481288).Curated1
Sequence conflicti1519Y → C in ABE73157 (PubMed:16481288).Curated1
Sequence conflicti1570C → Y in AAM97359 (Ref. 16) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0300277V → L.1 PublicationCorresponds to variant rs9515185dbSNPEnsembl.1
Natural variantiVAR_073809144A → V.1 Publication1
Natural variantiVAR_044158304P → L.Corresponds to variant rs34843786dbSNPEnsembl.1
Natural variantiVAR_073810352P → L in ICH; the mutant protein is retained intracellularly and is not secreted normally. 1 Publication1
Natural variantiVAR_064493498G → R in HANAC. 1 Publication1
Natural variantiVAR_044159498G → V in HANAC. 1 Publication1
Natural variantiVAR_064494510G → R in HANAC and RATOR. 2 Publications1
Natural variantiVAR_044160519G → R in HANAC. 1 Publication1
Natural variantiVAR_064495525G → L in HANAC; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_044161528G → E in HANAC. 1 Publication1
Natural variantiVAR_073811538R → G in ICH; the mutant protein is retained intracellularly and is not secreted normally. 1 Publication1
Natural variantiVAR_030511555T → P.5 PublicationsCorresponds to variant rs536174dbSNPEnsembl.1
Natural variantiVAR_030028562G → E in BSVD. 1 Publication1
Natural variantiVAR_073812655G → R in SCHZC. 1 Publication1
Natural variantiVAR_073813708G → R in BSVD. 1 Publication1
Natural variantiVAR_064496720G → D in BSVD; diffuse small vessel disease of the brain associated with Axenfeld-Rieger anomaly and leukoencephalopathy. 2 Publications1
Natural variantiVAR_030029749G → S in POREN1. 1 Publication1
Natural variantiVAR_064497755G → R in BSVD; associated with ocular anomalies of variable severity in some patients. 3 Publications1
Natural variantiVAR_073814773G → R in BSVD. 2 Publications1
Natural variantiVAR_064498805G → R in BSVD. 1 Publication1
Natural variantiVAR_073815870G → R in SCHZC. 1 Publication1
Natural variantiVAR_073816882G → D in BSVD. 1 Publication1
Natural variantiVAR_073817897G → S in SCHZC. 1 Publication1
Natural variantiVAR_073818948G → S in SCHZC. 1 Publication1
Natural variantiVAR_0738191041G → E in SCHZC. 1 Publication1
Natural variantiVAR_0738201082G → E in SCHZC. 1 Publication1
Natural variantiVAR_0300301130G → D in POREN1. 1 Publication1
Natural variantiVAR_0300311236G → R in POREN1. 1 Publication1
Natural variantiVAR_0738211266G → R in BSVD. 1 Publication1
Natural variantiVAR_0738221326G → R in SCHZC. 1 Publication1
Natural variantiVAR_0738231332G → D in SCHZC. 1 Publication1
Natural variantiVAR_0200131334Q → H.2 PublicationsCorresponds to variant rs3742207dbSNPEnsembl.1
Natural variantiVAR_0300321423G → R in POREN1. 1 Publication1
Natural variantiVAR_0738241531M → V.1 Publication1
Natural variantiVAR_0644991580G → R in POREN1. 1 Publication1
Natural variantiVAR_0738251615E → K in SCHZC. 1 Publication1
Natural variantiVAR_0738261627N → K in BSVD. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_034644498 – 848Missing in isoform 2. CuratedAdd BLAST351

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26576
, 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.
CCDSiCCDS9511.1. [P02462-1]
PIRiS16876. CGHU4B.
RefSeqiNP_001290039.1. NM_001303110.1.
NP_001836.3. NM_001845.5.
UniGeneiHs.17441.

Genome annotation databases

EnsembliENST00000375820; ENSP00000364979; ENSG00000187498.
GeneIDi1282.
KEGGihsa:1282.
UCSCiuc001vqw.4. human. [P02462-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26576
, 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.
CCDSiCCDS9511.1. [P02462-1]
PIRiS16876. CGHU4B.
RefSeqiNP_001290039.1. NM_001303110.1.
NP_001836.3. NM_001845.5.
UniGeneiHs.17441.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LI1X-ray1.90A/B/D/E1441-1669[»]
ProteinModelPortaliP02462.
SMRiP02462.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107679. 21 interactors.
IntActiP02462. 26 interactors.
MINTiMINT-6743187.
STRINGi9606.ENSP00000364979.

Chemistry databases

ChEMBLiCHEMBL2364188.

PTM databases

iPTMnetiP02462.
PhosphoSitePlusiP02462.
SwissPalmiP02462.

Polymorphism and mutation databases

BioMutaiCOL4A1.
DMDMi125987809.

Proteomic databases

EPDiP02462.
MaxQBiP02462.
PaxDbiP02462.
PeptideAtlasiP02462.
PRIDEiP02462.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375820; ENSP00000364979; ENSG00000187498.
GeneIDi1282.
KEGGihsa:1282.
UCSCiuc001vqw.4. human. [P02462-1]

Organism-specific databases

CTDi1282.
DisGeNETi1282.
GeneCardsiCOL4A1.
GeneReviewsiCOL4A1.
HGNCiHGNC:2202. COL4A1.
HPAiCAB001695.
HPA054039.
MalaCardsiCOL4A1.
MIMi120130. gene.
175780. phenotype.
180000. phenotype.
269160. phenotype.
607595. phenotype.
611773. phenotype.
614519. phenotype.
neXtProtiNX_P02462.
Orphaneti73229. Autosomal dominant familial hematuria - retinal arteriolar tortuosity - contractures.
99810. Familial porencephaly.
36383. Familial vascular leukoencephalopathy.
799. Schizencephaly.
899. Walker-Warburg syndrome.
PharmGKBiPA26717.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
HOVERGENiHBG004933.
InParanoidiP02462.
KOiK06237.
OrthoDBiEOG091G0613.
PhylomeDBiP02462.
TreeFamiTF316865.

Enzyme and pathway databases

BioCyciZFISH:G66-33301-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474244. Extracellular matrix organization.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-186797. Signaling by PDGF.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-2214320. Anchoring fibril formation.
R-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-419037. NCAM1 interactions.

Miscellaneous databases

ChiTaRSiCOL4A1. human.
EvolutionaryTraceiP02462.
GeneWikiiCollagen,_type_IV,_alpha_1.
GenomeRNAii1282.
PROiP02462.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000187498.
CleanExiHS_COL4A1.
ExpressionAtlasiP02462. baseline and differential.
GenevisibleiP02462. HS.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR008160. Collagen.
IPR001442. Collagen_VI_NC.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 15 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO4A1_HUMAN
AccessioniPrimary (citable) accession number: P02462
Secondary accession number(s): A7E2W4
, B1AM70, Q1P9S9, Q5VWF6, Q86X41, Q8NF88, Q9NYC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 6, 2007
Last modified: November 30, 2016
This is version 187 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.