COL18A1
entrez
80781
canonical
uniprot
P39060
canonical
ensembl
ENSG00000182871
resolver
ensembl
ENSG00000292234
resolver
ensp
ENSP00000347665
resolver
ensp
ENSP00000352798
resolver
ensp
ENSP00000498485
resolver
ensp
ENSP00000518184
resolver
ensp
ENSP00000518185
resolver
enst
ENST00000710294
resolver
enst
ENST00000710295
resolver
genesymbol
COL18A1
resolver
hgnc
HGNC:2195
resolver
uniprot
A0AAG2UW65
resolver
uniprot
A0AAG2UXZ5
resolver
uniprot
A8MVI4
resolver
uniprot
Q58EX6
resolver
uniprot
Q6RZ39
resolver
uniprot
Q6RZ40
resolver
uniprot
Q6RZ41
resolver
uniprot
Q8N4S4
resolver
uniprot
Q8WXI5
resolver
uniprot
Q96T70
resolver
uniprot
Q9UK38
resolver
uniprot
Q9Y6Q7
resolver
uniprot
Q9Y6Q8
resolver
uniprot_entry
A0AAG2UW65_HUMAN
resolver
uniprot_entry
A0AAG2UXZ5_HUMAN
resolver
uniprot_entry
COIA1_HUMAN
resolver
uniprot_sec
A8MVI4
resolver
uniprot_sec
Q58EX6
resolver
uniprot_sec
Q6RZ39
resolver
uniprot_sec
Q6RZ40
resolver
uniprot_sec
Q6RZ41
resolver
uniprot_sec
Q8N4S4
resolver
uniprot_sec
Q8WXI5
resolver
uniprot_sec
Q96T70
resolver
uniprot_sec
Q9UK38
resolver
uniprot_sec
Q9Y6Q7
resolver
uniprot_sec
Q9Y6Q8
resolver
amino_acid_sequence
MAPYPCGCHILLLLFCCLAAARANLLNLNWLWFNNEDTSHAATTIPEPQGPLPVQPTADTTTHVTPRNGSTEPATAPGSPEPPSELLEDGQDTPTSAESPDAPEENIAGVGAEILNVAKGIRSFVQLWNDTVPTESLARAETLVLETPVGPLALAGPSSTPQENGTTLWPSRGIPSSPGAHTTEAGTLPAPTPSPPSLGRPWAPLTGPSVPPPSSGRASLSSLLGGAPPWGSLQDPDSQGLSPAAAAPSQQLQRPDVRLRTPLLHPLVMGSLGKHAAPSAFSSGLPGALSQVAVTTLTRDSGAWVSHVANSVGPGLANNSALLGADPEAPAGRCLPLPPSLPVCGHLGISRFWLPNHLHHESGEQVRAGARAWGGLLQTHCHPFLAWFFCLLLVPPCGSVPPPAPPPCCQFCEALQDACWSRLGGGRLPVACASLPTQEDGYCVLIGPAAERISEEVGLLQLLGDPPPQQVTQTDDPDVGLAYVFGPDANSGQVARYHFPSLFFRDFSLLFHIRPATEGPGVLFAITDSAQAMVLLGVKLSGVQDGHQDISLLYTEPGAGQTHTAASFRLPAFVGQWTHLALSVAGGFVALYVDCEEFQRMPLARSSRGLELEPGAGLFVAQAGGADPDKFQGVIAELKVRRDPQVSPMHCLDEEGDDSDGASGDSGSGLGDARELLREETGAALKPRLPAPPPVTTPPLAGGSSTEDSRSEEVEEQTTVASLGAQTLPGSDSVSTWDGSVRTPGGRVKEGGLKGQKGEPGVPGPPGRAGPPGSPCLPGPPGLPCPVSPLGPAGPALQTVPGPQGPPGPPGRDGTPGRDGEPGDPGEDGKPGDTGPQGFPGTPGDVGPKGDKGDPGVGERGPPGPQGPPGPPGPSFRHDKLTFIDMEGSGFGGDLEALRGPRGFPGPPGPPGVPGLPGEPGRFGVNSSDVPGPAGLPGVPGREGPPGFPGLPGPPGPPGREGPPGRTGQKGSLGEAGAPGHKGSKGAPGPAGARGESGLAGAPGPAGPPGPPGPPGPPGPGLPAGFDDMEGSGGPFWSTARSADGPQGPPGLPGLKGDPGVPGLPGAKGEVGADGVPGFPGLPGREGIAGPQGPKGDRGSRGEKGDPGKDGVGQPGLPGPPGPPGPVVYVSEQDGSVLSVPGPEGRPGFAGFPGPAGPKGNLGSKGERGSPGPKGEKGEPGSIFSPDGGALGPAQKGAKGEPGFRGPPGPYGRPGYKGEIGFPGRPGRPGMNGLKGEKGEPGDASLGFGMRGMPGPPGPPGPPGPPGTPVYDSNVFAESSRPGPPGLPGNQGPPGPKGAKGEVGPPGPPGQFPFDFLQLEAEMKGEKGDRGDAGQKGERGEPGGGGFFGSSLPGPPGPPGPPGPRGYPGIPGPKGESIRGQPGPPGPQGPPGIGYEGRQGPPGPPGPPGPPSFPGPHRQTISVPGPPGPPGPPGPPGTMGASSGVRLWATRQAMLGQVHEVPEGWLIFVAEQEELYVRVQNGFRKVQLEARTPLPRGTDNEVAALQPPVVQLHDSNPYPRREHPHPTARPWRADDILASPPRLPEPQPYPGAPHHSSYVHLRPARPTSPPAHSHRDFQPVLHLVALNSPLSGGMRGIRGADFQCFQQARAVGLAGTFRAFLSSRLQDLYSIVRRADRAAVPIVNLKDELLFPSWEALFSGSEGPLKPGARIFSFDGKDVLRHPTWPQKSVWHGSDPNGRRLTESYCETWRTEAPSATGQASSLLGGRLLGQSAASCHHAYIVLCIENSFMTASK
uniprot
proteins
disease_involvement
DISEASE: Knobloch syndrome 1 (KNO1) [MIM:267750]: A developmental disorder primarily characterized by typical eye abnormalities, including high myopia, cataracts, dislocated lens, vitreoretinal degeneration, and retinal detachment, with occipital skull defects, which can range from occipital encephalocele to occult cutis aplasia. {ECO:0000269|PubMed:10942434, ECO:0000269|PubMed:23667181}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Glaucoma, primary closed-angle (GLCC) [MIM:618880]: An autosomal dominant form of primary glaucoma, an ocular disease characterized by a marked increase of intraocular pressure causing damage to eye structures and function. GLCC is characterized by elevated intraocular pressure due to iridocorneal angle closure with retention of the aqueous humor in the anterior chamber. Iridocorneal angle changes are apparent in the fourth to fifth decade of life, and patients manifest age-related variation in the severity of glaucomatous damage. {ECO:0000269|PubMed:30007336}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Probably plays a major role in determining the retinal structure as well as in the closure of the neural tube. {ECO:0000269|PubMed:10942434}.; FUNCTION: [Non-collagenous domain 1]: May regulate extracellular matrix-dependent motility and morphogenesis of endothelial and non-endothelial cells; the function requires homotrimerization and implicates MAPK signaling. {ECO:0000269|PubMed:11257123}.; FUNCTION: [Endostatin]: Potently inhibits endothelial cell proliferation and angiogenesis (PubMed:9459295). May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling (By similarity). Inhibits VEGFA-induced endothelial cell proliferation and migration. Seems to inhibit VEGFA-mediated signaling by blocking the interaction of VEGFA to its receptor KDR/VEGFR2. Modulates endothelial cell migration in an integrin-dependent manner implicating integrin ITGA5:ITGB1 and to a lesser extent ITGAV:ITGB3 and ITGAV:ITGB5 (By similarity). May negatively regulate the activity of homotrimeric non-collagenous domain 1 (PubMed:11257123). {ECO:0000250|UniProtKB:P39061, ECO:0000269|PubMed:11257123, ECO:0000269|PubMed:9459295}.
uniprot
proteins
mass_dalton
178188
uniprot
proteins
post_translational_modification
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) of the triple-helical regions are hydroxylated.; PTM: Circulating endostatins are found as sialoglycoprotein and asialoglycoprotein structures. {ECO:0000269|PubMed:10441114}.; PTM: Undergoes proteolytic processing by CTSL/cathepsin-L and elastase-like proteases to generate both non-collagenous domain 1 trimers and endostatin monomers (PubMed:10626789). In tissue extracts (brain, skeletal muscle, heart, kidney, testis and liver) predominantly bands of approximately 38 kDa are detected; recombinant non-collagenous domain 1 shows similar mobility. In vitro, several proteolytic cleavage sites in the non-collagenous domain 1 hinge region generating different endostatin-like peptides are reported (By similarity). {ECO:0000250|UniProtKB:P39061, ECO:0000269|PubMed:10626789}.
uniprot
proteins
protein_family
Multiplexin collagen family
uniprot
proteins
pubmed
10441114
uniprot
proteins
pubmed
10626789
uniprot
proteins
pubmed
10830953
uniprot
proteins
pubmed
10942434
uniprot
proteins
pubmed
11257123
uniprot
proteins
pubmed
11517600
uniprot
proteins
pubmed
11606364
uniprot
proteins
pubmed
14614989
uniprot
proteins
pubmed
14695535
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17644065
uniprot
proteins
pubmed
18987736
uniprot
proteins
pubmed
23667181
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
30007336
uniprot
proteins
pubmed
32337544
uniprot
proteins
pubmed
8188291
uniprot
proteins
pubmed
9459295
uniprot
proteins
pubmed
9503365
uniprot
proteins
pubmed
9724722
uniprot
proteins
sequence_length
1754
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:P39061}.; SUBCELLULAR LOCATION: [Non-collagenous domain 1]: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:P39061}. Secreted {ECO:0000250|UniProtKB:P39061}.; SUBCELLULAR LOCATION: [Endostatin]: Secreted {ECO:0000269|PubMed:10441114}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000305}.
uniprot
proteins