Col18a1
entrez
12822
canonical
uniprot
P39061
canonical
ensembl
ENSMUSG00000001435
resolver
ensp
ENSMUSP00000072538
resolver
ensp
ENSMUSP00000080358
resolver
ensp
ENSMUSP00000101049
resolver
ensp
ENSMUSP00000317565
resolver
enst
ENSMUST00000072755
resolver
genesymbol
Col18a1
resolver
uniprot
E9QPX1
resolver
uniprot
Q60672
resolver
uniprot
Q61434
resolver
uniprot
Q61437
resolver
uniprot
Q62001
resolver
uniprot
Q62002
resolver
uniprot
Q6NZK9
resolver
uniprot
Q6P1Y4
resolver
uniprot
Q8CCZ8
resolver
uniprot
Q9CRT2
resolver
uniprot
Q9JK63
resolver
uniprot_entry
COIA1_MOUSE
resolver
uniprot_entry
E9QPX1_MOUSE
resolver
uniprot_sec
Q60672
resolver
uniprot_sec
Q61434
resolver
uniprot_sec
Q61437
resolver
uniprot_sec
Q62001
resolver
uniprot_sec
Q62002
resolver
uniprot_sec
Q6NZK9
resolver
uniprot_sec
Q6P1Y4
resolver
uniprot_sec
Q8CCZ8
resolver
uniprot_sec
Q9CRT2
resolver
uniprot_sec
Q9JK63
resolver
amino_acid_sequence
MAPDPSRRLCLLLLLLLSCRLVPASADGNSLSPLNPLVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASSELPPEEEEEEDQKAGQGGSPATPAVPIPLVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSSAIPSSPDAQTTEAGTLAVPTQLPPFQSNLQAPLGRPSAPPDFPGRAFLSSSTDQGSSWGNQEPPRQPQHLEGKGFLPMTARSSQQHRHSDVHSDIHGHVPLLPLVTGPLVTASLSVHGLLSVPSSDPSGQLSQVAALPGFPGTWVSHVAPSSGTGLSNDSALAGNGSLTSTSRCLPLPPTLTLCSRLGIGHFWLPNHLHHTDSVEVEATVQAWGRFLHTNCHPFLAWFFCLLLAPSCGPGPPPPLPPCRQFCEALEDECWNYLAGDRLPVVCASLPSQEDGYCVFIGPAAENVAEEVGLLQLLGDPLPEKISQIDDPHVGPAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDAAQVVVSLGVKLSEVRDGQQNISLLYTEPGASQTQTGASFRLPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQGLELERGAGLFVGQAGTADPDKFQGMISELKVRKTPRVSPVHCLDEEDDDEDRASGDFGSGFEESSKSHKEDTSLLPGLPQPPPVTSPPLAGGSTTEDPRTEETEEDAAVDSIGAETLPGTGSSGAWDEAIQNPGRGLIKGGMKGQKGEPGAQGPPGPAGPQGPAGPVVQSPNSQPVPGAQGPPGPQGPPGKDGTPGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGEKGDPGIGPRGPPGPPGPPGPSFRQDKLTFIDMEGSGFSGDIESLRGPRGFPGPPGPPGVPGLPGEPGRFGINGSYAPGPAGLPGVPGKEGPPGFPGPPGPPGPPGKEGPPGVAGQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGSPGPVGPPGPPGPPGPPGPGFAAGFDDMEGSGIPLWTTARSSDGLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPPGPPGPVIYVSSEDKAIVSTPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPGTIFSPDGRALGHPQKGAKGEPGFRGPPGPYGRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASLGFSMRGLPGPPGPPGPPGPPGMPIYDSNAFVESGRPGLPGQQGVQGPSGPKGDKGEVGPPGPPGQFPIDLFHLEAEMKGDKGDRGDAGQKGERGEPGAPGGGFFSSSVPGPPGPPGYPGIPGPKGESIRGPPGPPGPQGPPGIGYEGRQGPPGPPGPPGPPSFPGPHRQTVSVPGPPGPPGPPGPPGAMGASAGQVRIWATYQTMLDKIREVPEGWLIFVAEREELYVRVRNGFRKVLLEARTALPRGTGNEVAALQPPLVQLHEGSPYTRREYSYSTARPWRADDILANPPRLPDRQPYPGVPHHHSSYVHLPPARPTLSLAHTHQDFQPVLHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSLFSGSQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCHNSYIVLCIENSFMTSFSK
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:0000250|UniProtKB:P39060}.; 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:0000250|UniProtKB:P39060}.; FUNCTION: [Endostatin]: Potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling (PubMed:9008168). Inhibits VEGFA isoform VEGF165-induced endothelial cell proliferation and migration. Seems to inhibit VEGFA-mediated signaling by blocking the interaction of VEGFA to its receptor KDR/VEGFR2 (PubMed:12029087). Modulates endothelial cell migration in an integrin-dependent manner implicating integrin ITGA5:ITGB1 and to a lesser extent ITGAV:ITGB3 and ITGAV:ITGB5 (PubMed:11158588). May negatively regulate the activity of homotrimeric non-collagenous domain 1 (By similarity). {ECO:0000250|UniProtKB:P39060, ECO:0000269|PubMed:11158588, ECO:0000269|PubMed:9008168}.
uniprot
proteins
mass_dalton
182172
uniprot
proteins
mutagenesis
MUTAGEN 1591; /note="H->A: No effect on zinc binding."; /evidence="ECO:0000269|PubMed:10704302"; MUTAGEN 1593; /note="H->A: Reduces zinc binding by 60%. Abolishes zinc binding; when associated with A-1595."; /evidence="ECO:0000269|PubMed:10704302"; MUTAGEN 1595; /note="D->A: No effect on zinc binding. Abolishes zinc binding; when associated with A-1593."; /evidence="ECO:0000269|PubMed:10704302"; MUTAGEN 1666; /note="D->A: Abolishes zinc binding."; /evidence="ECO:0000269|PubMed:10704302
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: Undergoes proteolytic processing by CTSL/cathepsin-L and elastase-like proteases to generate both non-collagenous domain 1 trimers and endostatin monomers (PubMed:10716919). 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. {ECO:0000250|UniProtKB:P39060, ECO:0000269|PubMed:10626789, ECO:0000269|PubMed:10716919, ECO:0000305|PubMed:9687493}.
uniprot
proteins
protein_family
Multiplexin collagen family
uniprot
proteins
pubmed
10626789
uniprot
proteins
pubmed
10704302
uniprot
proteins
pubmed
10716919
uniprot
proteins
pubmed
10966814
uniprot
proteins
pubmed
11158588
uniprot
proteins
pubmed
11321448
uniprot
proteins
pubmed
12029087
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
7876242
uniprot
proteins
pubmed
8183893
uniprot
proteins
pubmed
8183894
uniprot
proteins
pubmed
8188673
uniprot
proteins
pubmed
8240330
uniprot
proteins
pubmed
8838808
uniprot
proteins
pubmed
9008168
uniprot
proteins
pubmed
9501087
uniprot
proteins
pubmed
9687493
uniprot
proteins
sequence_length
1774
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:9687493}.; SUBCELLULAR LOCATION: [Non-collagenous domain 1]: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000305|PubMed:9687493}. Secreted {ECO:0000269|PubMed:10626789}.; SUBCELLULAR LOCATION: [Endostatin]: Secreted {ECO:0000269|PubMed:10626789, ECO:0000305|PubMed:9008168}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000305}.
uniprot
proteins