Associated Structures
Accession: P00750 UniProtKB/Swiss-Prot Entry
UniProtKB/Swiss-Prot PTM Description
The single chain, almost fully active enzyme, can be further processed into a two-chain fully active form by a cleavage after Arg-310 catalyzed by plasmin, tissue kallikrein or factor Xa, Differential cell-specific N-linked glycosylation gives rise to two glycoforms, type I (glycosylated at Asn-219) and type II (not glycosylated at Asn-219). The single chain type I glycoform is less readily converted into the two-chain form by plasmin, and the two-chain type I glycoform has a lower activity than the two-chain type II glycoform in the presence of fibrin, N-glycosylation of Asn-152; the bound oligomannosidic glycan is involved in the interaction with the mannose receptor, Characterization of O-linked glycan was studied in Bowes melanoma cell line
Glycosylation Sites
Position | Structures | Description | Evidence |
---|---|---|---|
ASN-152, ASN-219, ASN-483 | Associated Structures: 20 | global | GlycoSuite |
Position | Structures | Description | Evidence |
---|---|---|---|
ASN-219 OF P00750, ASN-322 OF P00749 | Associated Structures: 16 | global | GlycoSuite |
Position | Structures | Description | Evidence |
---|---|---|---|
THR-96, ASN-152, ASN-219, ASN-483 | Associated Structures: 15 | global | GlycoSuite |
Site-Specific Information
A number of glycan structures have been assigned to specific glycosylation sites
Position | Structures | Description | Evidence |
---|---|---|---|
ASN-322 OF P00749 | Associated Structures: 13 | Site specific | GlycoSuite |
ASN-219 AND ASN-483 | Associated Structures: 6 | Site specific | GlycoSuite |
THR-96 | Associated Structures: 1 | Site specific | GlycoSuite |
ASN-322 OF P00749 | Associated Structures: 0 | Site specific | GlycoSuite |
Notes
Accompanying information sourced from GlycoSuiteDB
- ASN-152, ASN-219{partial} AND ASN-483 [PFEIFFER ET AL. (1989) EUR. J. BIOCHEM. 186:273-286
- THR-96 [HARRIS ET AL. (1991) BIOCHEMISTRY 30:2311-2314
- ASN-152, ASN-219 AND ASN-483 [POHL ET AL. (1987) EUR. J. BIOCHEM. 170:69-75