UniProtKB/Swiss-Prot PTM Description

N-linked glycan contains N-acetyllactosamine, sialic acid and is core fucosylated. O-linked glycans consist of Gal-GalNAc disaccharide which is modified with up to 2 sialic acid residues (microheterogeneity), In the presence of the inhibitor, the activation involves only cleavage after Arg-579, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide

Glycosylation Sites

Position Structures Description Evidence
ASN-289, THR-340 Associated Structures: 14 global GlycoSuite
Site-Specific Information

A number of glycan structures have been assigned to specific glycosylation sites

Position Structures Description Evidence
THR-340 Associated Structures: 2 Site specific GlycoSuite
ASN-289 Associated Structures: 12 Site specific GlycoSuite

Notes

Accompanying information sourced from GlycoSuiteDB

  1. ASN-289 AND THR-340 [SCHALLER ET AL. (1987) FIBINOLYSIS 1:91-102

Sequence

MDHKEVVLLLLLFLKSGLGDSLDDYVNTQGAFLFSLSRKQVAARSVEECAAKCEAETNFICRAFQYHSKDQQCVVMAENSKTSPIARMRDVVLFEKRIYLSECKTGNGKNYRGTTSKTKSGVICQKWSVSSPHIPKYSPEKFPLAGLEENYCRNPDNDEKGPWCYTTDPETRFDYCDIPECEDECMHCSGEHYEGKISKTMSGIECQSWGSQSPHAHGYLPSKFPNKNLKMNYCRNPDGEPRPWCFTTDPNKRWEFCDIPRCTTPPPTSGPTYQCLKGRGENYRGTVSVTASGHTCQRWSAQSPHKHNRTPENFPCKNLEENYCRNPDGETAPWCYTTDSEVRWDYCKIPSCGSSTTSTEYLDAPVPPEQTPVAQDCYRGNGESYRGTSSTTITGRKCQSWVSMTPHRHEKTPGNFPNAGLTMNYCRNPDADKSPWCYTTDPRVRWEYCNLKKCSETEQQVTNFPAIAQVPSVEDLSEDCMFGNGKRYRGKRATTVAGVPCQEWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDDNGPWCYTTNPQKLFDYCDVPQCVTSSFDCGKPKVEPKKCPARVVGGCVSIPHSWPWQISLRHRYGGHFCGGTLISPEWVLTAKHCLEKSSSPSSYKVILGAHEEYHLGEGVQEIDVSKLFKEPSEADIALLKLSSPAIITDKVIPACLPTPNYVVADRTACYITGWGETKGTYGAGLLKEARLPVIENKVCNRYEYLGGKVSPNELCAGHLAGGIDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCALPNKPGVYVRVSRFVTWIEEIMRRN

Biological Associations

    Protein

References 0