COL4A1
entrez
1282
canonical
uniprot
P02462
canonical
ensembl
ENSG00000187498
resolver
ensp
ENSP00000364979
resolver
ensp
ENSP00000443348
resolver
genesymbol
COL4A1
resolver
hgnc
HGNC:2202
resolver
uniprot
A5PKV2
resolver
uniprot
A7E2W4
resolver
uniprot
B1AM70
resolver
uniprot
F5H5K0
resolver
uniprot
Q1P9S9
resolver
uniprot
Q5VWF6
resolver
uniprot
Q86X41
resolver
uniprot
Q8NF88
resolver
uniprot
Q9NYC5
resolver
uniprot_entry
A5PKV2_HUMAN
resolver
uniprot_entry
CO4A1_HUMAN
resolver
uniprot_sec
A7E2W4
resolver
uniprot_sec
B1AM70
resolver
uniprot_sec
F5H5K0
resolver
uniprot_sec
Q1P9S9
resolver
uniprot_sec
Q5VWF6
resolver
uniprot_sec
Q86X41
resolver
uniprot_sec
Q8NF88
resolver
uniprot_sec
Q9NYC5
resolver
amino_acid_sequence
MGPRLSVWLLLLPAALLLHEEHSRAAAKGGCAGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPQGPPGQKGDTGEPGLPGTKGTRGPPGASGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFAGNPGPPGLPGMKGDPGEILGHVPGMLLKGERGFPGIPGTPGPPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGLSFQGPKGDKGDQGVSGPPGVPGQAQVQEKGDFATKGEKGQKGEPGFQGMPGVGEKGEPGKPGPRGKPGKDGDKGEKGSPGFPGEPGYPGLIGRQGPQGEKGEAGPPGPPGIVIGTGPLGEKGERGYPGTPGPRGEPGPKGFPGLPGQPGPPGLPVPGQAGAPGFPGERGEKGDRGFPGTSLPGPSGRDGLPGPPGSPGPPGQPGYTNGIVECQPGPPGDQGPPGIPGQPGFIGEIGEKGQKGESCLICDIDGYRGPPGPQGPPGEIGFPGQPGAKGDRGLPGRDGVAGVPGPQGTPGLIGQPGAKGEPGEFYFDLRLKGDKGDPGFPGQPGMPGRAGSPGRDGHPGLPGPKGSPGSVGLKGERGPPGGVGFPGSRGDTGPPGPPGYGPAGPIGDKGQAGFPGGPGSPGLPGPKGEPGKIVPLPGPPGAEGLPGSPGFPGPQGDRGFPGTPGRPGLPGEKGAVGQPGIGFPGPPGPKGVDGLPGDMGPPGTPGRPGFNGLPGNPGVQGQKGEPGVGLPGLKGLPGLPGIPGTPGEKGSIGVPGVPGEHGAIGPPGLQGIRGEPGPPGLPGSVGSPGVPGIGPPGARGPPGGQGPPGLSGPPGIKGEKGFPGFPGLDMPGPKGDKGAQGLPGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDPGLKGDKGDVGLPGKPGSMDKVDMGSMKGQKGDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPGDKGAKGEKGQAGPPGIGIPGLRGEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEPGLPGRGFPGFPGAKGDKGSKGEVGFPGLAGSPGIPGSKGEQGFMGPPGPQGQPGLPGSPGHATEGPKGDRGPQGQPGLPGLPGPMGPPGLPGIDGVKGDKGNPGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMGPPGVPGFQGPKGLPGLQGIKGDQGDQGVPGAKGLPGPPGPPGPYDIIKGEPGLPGPEGPPGLKGLQGLPGPKGQQGVTGLVGIPGPPGIPGFDGAPGQKGEMGPAGPTGPRGFPGPPGPDGLPGSMGPPGTPSVDHGFLVTRHSQTIDDPQCPSGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLSTPEPMPMSMAPITGENIRPFISRCAVCEAPAMVMAVHSQTIQIPPCPSGWSSLWIGYSFVMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRRT
uniprot
proteins
disease_involvement
DISEASE: 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. {ECO:0000269|PubMed:18160688, ECO:0000269|PubMed:20818663}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Brain small vessel disease 1 with or without ocular anomalies (BSVD1) [MIM:175780]: An autosomal dominant cerebrovascular disorder with variable manifestations reflecting the location and severity of the vascular defect. BSVD1 features include cerebral hemorrage, unilateral fluid-filled cysts or cavities within the cerebral hemispheres, leukoencephalopathy, hemiplegia, seizures, intellectual disability, and facial paresis. Affected individuals may manifest variable visual defects and ocular anomalies. {ECO:0000269|PubMed:15905400, ECO:0000269|PubMed:16107487, ECO:0000269|PubMed:16598045, ECO:0000269|PubMed:17379824, ECO:0000269|PubMed:17696175, ECO:0000269|PubMed:19194877, ECO:0000269|PubMed:19477666, ECO:0000269|PubMed:20385946, ECO:0000269|PubMed:22574627, ECO:0000269|PubMed:23394911, ECO:0000269|PubMed:24628545}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Intracerebral hemorrhage (ICH) [MIM:614519]: A 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. {ECO:0000269|PubMed:22522439}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Tortuosity of retinal arteries (RATOR) [MIM:180000]: A 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. {ECO:0000269|PubMed:25228067}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Schizencephaly (SCHZC) [MIM:269160]: Extremely 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. {ECO:0000269|PubMed:23225343}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Microangiopathy and leukoencephalopathy, pontine, autosomal dominant (PADMAL) [MIM:618564]: A form of cerebral small vessel disease characterized by the recurrence of ischemic strokes starting in the thirties or forties, and associated with progressive imbalance and cognitive impairment. MRI examination shows ischemic lacunas in the pons and cerebral hemispheres, and diffuse leukoencephalopathy affecting various brain regions. {ECO:0000269|PubMed:27666438, ECO:0000269|PubMed:28369186}. Note=The disease is caused by variants affecting the gene represented in this entry. Causative mutations affect a binding site for miR-29 microRNA located within the 3'UTR of COL4A1 and lead to an up-regulation of this gene. {ECO:0000269|PubMed:27666438}.
uniprot
proteins
function
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. {ECO:0000250|UniProtKB:P02463}.; FUNCTION: 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. {ECO:0000269|PubMed:10811134, ECO:0000269|PubMed:18775695}.
uniprot
proteins
mass_dalton
160611
uniprot
proteins
post_translational_modification
PTM: Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated. The modified lysines can be O-glycosylated. {ECO:0000269|PubMed:6434307}.; PTM: Contains 4-hydroxyproline (Probable). Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains (By similarity). {ECO:0000250|UniProtKB:P02463, ECO:0000305|PubMed:6434307}.; PTM: Contains 3-hydroxyproline. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P02463, ECO:0000250|UniProtKB:Q7SIB2}.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding (PubMed:2844531). 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. {ECO:0000269|PubMed:2844531, ECO:0000305}.; PTM: The trimeric structure of the NC1 domains is stabilized by covalent bonds (sulfilimine cross-links) between Lys and Met residues (PubMed:12011424). These cross-links are important for the mechanical stability of the basement membrane (By similarity). Sulfilimine cross-link is catalyzed by PXDN (By similarity). {ECO:0000250|UniProtKB:P02463, ECO:0000269|PubMed:12011424}.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, arresten. {ECO:0000269|PubMed:10811134}.
uniprot
proteins
protein_family
Type IV collagen family
uniprot
proteins
pubmed
10811134
uniprot
proteins
pubmed
12011424
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15905400
uniprot
proteins
pubmed
16107487
uniprot
proteins
pubmed
16151532
uniprot
proteins
pubmed
16481288
uniprot
proteins
pubmed
16598045
uniprot
proteins
pubmed
17379824
uniprot
proteins
pubmed
17696175
uniprot
proteins
pubmed
18160688
uniprot
proteins
pubmed
18775695
uniprot
proteins
pubmed
19194877
uniprot
proteins
pubmed
19477666
uniprot
proteins
pubmed
20385946
uniprot
proteins
pubmed
20818663
uniprot
proteins
pubmed
21527998
uniprot
proteins
pubmed
22522439
uniprot
proteins
pubmed
22574627
uniprot
proteins
pubmed
23225343
uniprot
proteins
pubmed
23394911
uniprot
proteins
pubmed
24628545
uniprot
proteins
pubmed
25228067
uniprot
proteins
pubmed
2581969
uniprot
proteins
pubmed
2582422
uniprot
proteins
pubmed
2701944
uniprot
proteins
pubmed
27666438
uniprot
proteins
pubmed
28369186
uniprot
proteins
pubmed
2844531
uniprot
proteins
pubmed
3182844
uniprot
proteins
pubmed
31895054
uniprot
proteins
pubmed
3311751
uniprot
proteins
pubmed
3691802
uniprot
proteins
pubmed
4043082
uniprot
proteins
pubmed
6434307
uniprot
proteins
sequence_length
1669
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:P02463}.
uniprot
proteins