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P02462

- CO4A1_HUMAN

UniProt

P02462 - CO4A1_HUMAN

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Protein

Collagen alpha-1(IV) chain

Gene

COL4A1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. extracellular matrix constituent conferring elasticity Source: BHF-UCL
  2. extracellular matrix structural constituent Source: BHF-UCL
  3. platelet-derived growth factor binding Source: MGI

GO - Biological processi

  1. axon guidance Source: Reactome
  2. basement membrane organization Source: BHF-UCL
  3. blood vessel morphogenesis Source: BHF-UCL
  4. brain development Source: BHF-UCL
  5. cellular response to amino acid stimulus Source: Ensembl
  6. collagen catabolic process Source: Reactome
  7. epithelial cell differentiation Source: Ensembl
  8. extracellular matrix disassembly Source: Reactome
  9. extracellular matrix organization Source: Reactome
  10. neuromuscular junction development Source: Ensembl
  11. patterning of blood vessels Source: BHF-UCL
  12. renal tubule morphogenesis Source: BHF-UCL
  13. retinal blood vessel morphogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Angiogenesis

Enzyme and pathway databases

ReactomeiREACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_150401. Collagen degradation.
REACT_163699. Scavenging by Class A Receptors.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_16888. Signaling by PDGF.
REACT_169262. Laminin interactions.
REACT_18312. 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
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:2202. COL4A1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: BHF-UCL
  2. collagen type IV trimer Source: BHF-UCL
  3. endoplasmic reticulum lumen Source: Reactome
  4. extracellular matrix Source: UniProtKB
  5. 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 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.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti562 – 5621G → E in BSVDH. 1 Publication
VAR_030028
Natural varianti720 – 7201G → D in BSVDH; diffuse small vessel disease of the brain associated with Axenfeld-Rieger anomaly and leukoencephalopathy. 2 Publications
VAR_064496
Natural varianti755 – 7551G → R in BSVDH; associated with ocular anomalies of variable severity in some patients. 2 Publications
VAR_064497
Natural varianti805 – 8051G → R in BSVDH. 1 Publication
VAR_064498
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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti498 – 4981G → R in HANAC. 1 Publication
VAR_064493
Natural varianti498 – 4981G → V in HANAC. 1 Publication
VAR_044159
Natural varianti510 – 5101G → R in HANAC. 1 Publication
VAR_064494
Natural varianti519 – 5191G → R in HANAC. 1 Publication
VAR_044160
Natural varianti525 – 5251G → L in HANAC; requires 2 nucleotide substitutions. 1 Publication
VAR_064495
Natural varianti528 – 5281G → E in HANAC. 1 Publication
VAR_044161
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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti749 – 7491G → S in POREN1. 1 Publication
VAR_030029
Natural varianti1130 – 11301G → D in POREN1. 1 Publication
VAR_030030
Natural varianti1236 – 12361G → R in POREN1. 1 Publication
VAR_030031
Natural varianti1423 – 14231G → R in POREN1. 1 Publication
VAR_030032
Natural varianti1580 – 15801G → R in POREN1. 1 Publication
VAR_064499

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Propeptidei28 – 172145N-terminal propeptide (7S domain)PRO_0000005748Add
BLAST
Chaini173 – 16691497Collagen alpha-1(IV) chainPRO_0000005749Add
BLAST
Chaini1445 – 1669225ArrestenPRO_0000390482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi126 – 1261N-linked (GlcNAc...)
Disulfide bondi1460 ↔ 15511 PublicationPROSITE-ProRule annotation
Disulfide bondi1493 ↔ 15481 PublicationPROSITE-ProRule annotation
Disulfide bondi1505 ↔ 15111 PublicationPROSITE-ProRule annotation
Cross-linki1533 – 1533S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651)
Disulfide bondi1570 ↔ 16651 PublicationPROSITE-ProRule annotation
Disulfide bondi1604 ↔ 16621 PublicationPROSITE-ProRule annotation
Disulfide bondi1616 ↔ 16221 PublicationPROSITE-ProRule annotation
Cross-linki1651 – 1651S-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

MaxQBiP02462.
PaxDbiP02462.
PRIDEiP02462.

PTM databases

PhosphoSiteiP02462.

Expressioni

Tissue specificityi

Highly expressed in placenta.2 Publications

Gene expression databases

BgeeiP02462.
CleanExiHS_COL4A1.
ExpressionAtlasiP02462. baseline and differential.
GenevestigatoriP02462.

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

Protein-protein interaction databases

BioGridi107679. 14 interactions.
IntActiP02462. 24 interactions.
MINTiMINT-6743187.
STRINGi9606.ENSP00000364979.

Structurei

Secondary structure

1
1669
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1446 – 14516Combined sources
Beta strandi1453 – 14564Combined sources
Beta strandi1465 – 147814Combined sources
Beta strandi1481 – 14844Combined sources
Helixi1490 – 14923Combined sources
Beta strandi1493 – 14964Combined sources
Beta strandi1502 – 15054Combined sources
Beta strandi1509 – 15146Combined sources
Beta strandi1519 – 15246Combined sources
Helixi1538 – 15447Combined sources
Beta strandi1547 – 15559Combined sources
Beta strandi1557 – 15615Combined sources
Beta strandi1563 – 15664Combined sources
Beta strandi1574 – 158714Combined sources
Helixi1589 – 15913Combined sources
Beta strandi1593 – 15953Combined sources
Helixi1601 – 16033Combined sources
Beta strandi1604 – 16074Combined sources
Beta strandi1613 – 16175Combined sources
Beta strandi1620 – 16234Combined sources
Beta strandi1629 – 16346Combined sources
Helixi1638 – 16403Combined sources
Beta strandi1648 – 16514Combined sources
Helixi1655 – 16584Combined sources
Beta strandi1661 – 16677Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LI1X-ray1.90A/B/D/E1441-1669[»]
ProteinModelPortaliP02462.
SMRiP02462. Positions 1442-1669.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02462.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1445 – 1669225Collagen IV NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 14401268Triple-helical regionAdd
BLAST

Domaini

Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.

Sequence similaritiesi

Belongs to the type IV collagen family.PROSITE-ProRule annotation
Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00770000120455.
HOVERGENiHBG004933.
InParanoidiP02462.
KOiK06237.
OMAiSSMDHGF.
OrthoDBiEOG7RZ5P3.
PhylomeDBiP02462.
TreeFamiTF316865.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 21 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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti237 – 2382SG → KE AA sequence (PubMed:4043082)Curated
Sequence conflicti241 – 2411G → K AA sequence (PubMed:4043082)Curated
Sequence conflicti319 – 3191Q → A in CAA29075. (PubMed:3311751)Curated
Sequence conflicti719 – 7191N → D AA sequence (PubMed:6434307)Curated
Sequence conflicti837 – 8371D → Y AA sequence (PubMed:6434307)Curated
Sequence conflicti842 – 8421K → P AA sequence (PubMed:6434307)Curated
Sequence conflicti896 – 8961V → W in CAA68698. (PubMed:3691802)Curated
Sequence conflicti904 – 9041E → Q AA sequence (PubMed:6434307)Curated
Sequence conflicti914 – 9141S → K AA sequence (PubMed:6434307)Curated
Sequence conflicti998 – 9981S → K AA sequence (PubMed:6434307)Curated
Sequence conflicti1010 – 10101K → P AA sequence (PubMed:6434307)Curated
Sequence conflicti1012 – 10121S → K AA sequence (PubMed:6434307)Curated
Sequence conflicti1358 – 13581E → Q AA sequence (PubMed:6434307)Curated
Sequence conflicti1490 – 14901A → T in ABE73157. (PubMed:16481288)Curated
Sequence conflicti1507 – 15071I → T in ABE73157. (PubMed:16481288)Curated
Sequence conflicti1519 – 15191Y → C in ABE73157. (PubMed:16481288)Curated
Sequence conflicti1570 – 15701C → Y in AAM97359. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71V → L.1 Publication
Corresponds to variant rs9515185 [ dbSNP | Ensembl ].
VAR_030027
Natural varianti304 – 3041P → L.
Corresponds to variant rs34843786 [ dbSNP | Ensembl ].
VAR_044158
Natural varianti498 – 4981G → R in HANAC. 1 Publication
VAR_064493
Natural varianti498 – 4981G → V in HANAC. 1 Publication
VAR_044159
Natural varianti510 – 5101G → R in HANAC. 1 Publication
VAR_064494
Natural varianti519 – 5191G → R in HANAC. 1 Publication
VAR_044160
Natural varianti525 – 5251G → L in HANAC; requires 2 nucleotide substitutions. 1 Publication
VAR_064495
Natural varianti528 – 5281G → E in HANAC. 1 Publication
VAR_044161
Natural varianti555 – 5551T → P.5 Publications
Corresponds to variant rs536174 [ dbSNP | Ensembl ].
VAR_030511
Natural varianti562 – 5621G → E in BSVDH. 1 Publication
VAR_030028
Natural varianti720 – 7201G → D in BSVDH; diffuse small vessel disease of the brain associated with Axenfeld-Rieger anomaly and leukoencephalopathy. 2 Publications
VAR_064496
Natural varianti749 – 7491G → S in POREN1. 1 Publication
VAR_030029
Natural varianti755 – 7551G → R in BSVDH; associated with ocular anomalies of variable severity in some patients. 2 Publications
VAR_064497
Natural varianti805 – 8051G → R in BSVDH. 1 Publication
VAR_064498
Natural varianti1130 – 11301G → D in POREN1. 1 Publication
VAR_030030
Natural varianti1236 – 12361G → R in POREN1. 1 Publication
VAR_030031
Natural varianti1334 – 13341Q → H.2 Publications
Corresponds to variant rs3742207 [ dbSNP | Ensembl ].
VAR_020013
Natural varianti1423 – 14231G → R in POREN1. 1 Publication
VAR_030032
Natural varianti1580 – 15801G → R in POREN1. 1 Publication
VAR_064499

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei498 – 848351Missing in isoform 2. CuratedVSP_034644Add
BLAST

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_001836.2. NM_001845.4. [P02462-1]
UniGeneiHs.17441.

Genome annotation databases

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

Polymorphism databases

DMDMi125987809.

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 .
CCDSi CCDS9511.1. [P02462-1 ]
PIRi S16876. CGHU4B.
RefSeqi NP_001836.2. NM_001845.4. [P02462-1 ]
UniGenei Hs.17441.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LI1 X-ray 1.90 A/B/D/E 1441-1669 [» ]
ProteinModelPortali P02462.
SMRi P02462. Positions 1442-1669.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107679. 14 interactions.
IntActi P02462. 24 interactions.
MINTi MINT-6743187.
STRINGi 9606.ENSP00000364979.

Chemistry

ChEMBLi CHEMBL2364188.

PTM databases

PhosphoSitei P02462.

Polymorphism databases

DMDMi 125987809.

Proteomic databases

MaxQBi P02462.
PaxDbi P02462.
PRIDEi P02462.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375820 ; ENSP00000364979 ; ENSG00000187498 .
GeneIDi 1282.
KEGGi hsa:1282.
UCSCi uc001vqw.4. human. [P02462-1 ]

Organism-specific databases

CTDi 1282.
GeneCardsi GC13M110801.
GeneReviewsi COL4A1.
HGNCi HGNC:2202. COL4A1.
HPAi CAB001695.
HPA054039.
MIMi 120130. gene.
175780. phenotype.
607595. phenotype.
611773. phenotype.
neXtProti NX_P02462.
Orphaneti 73229. Autosomal dominant familial hematuria - retinal arteriolar tortuosity - contractures.
99810. Familial porencephaly.
36383. Familial vascular leukoencephalopathy.
799. Schizencephaly.
899. Walker-Warburg syndrome.
PharmGKBi PA26717.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00770000120455.
HOVERGENi HBG004933.
InParanoidi P02462.
KOi K06237.
OMAi SSMDHGF.
OrthoDBi EOG7RZ5P3.
PhylomeDBi P02462.
TreeFami TF316865.

Enzyme and pathway databases

Reactomei REACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_150401. Collagen degradation.
REACT_163699. Scavenging by Class A Receptors.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_16888. Signaling by PDGF.
REACT_169262. Laminin interactions.
REACT_18312. NCAM1 interactions.

Miscellaneous databases

ChiTaRSi COL4A1. human.
EvolutionaryTracei P02462.
GeneWikii Collagen,_type_IV,_alpha_1.
GenomeRNAii 1282.
NextBioi 5181.
PROi P02462.
SOURCEi Search...

Gene expression databases

Bgeei P02462.
CleanExi HS_COL4A1.
ExpressionAtlasi P02462. baseline and differential.
Genevestigatori P02462.

Family and domain databases

Gene3Di 2.170.240.10. 1 hit.
InterProi IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR001442. Collagen_VI_NC.
[Graphical view ]
Pfami PF01413. C4. 2 hits.
PF01391. Collagen. 21 hits.
[Graphical view ]
SMARTi SM00111. C4. 2 hits.
[Graphical view ]
SUPFAMi SSF56436. SSF56436. 2 hits.
PROSITEi PS51403. NC1_IV. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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. 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. 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. Cited for: VARIANT BSVDH GLU-562.
  24. Cited for: VARIANT BSVDH ASP-720.
  25. Cited for: VARIANTS HANAC VAL-498; ARG-519 AND GLU-528.
  26. 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.

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 26, 2014
This is version 168 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

External Data

Dasty 3