P32329

Name	Aspartic proteinase 3 (EC 3.4.23.41) (Proprotein convertase) (Yapsin-1) [Cleaved into: Aspartic proteinase 3 subunit alpha; Aspartic proteinase 3 subunit beta]
Uniprot ID	P32329
Systematic gene name	YLR120C
Standard gene name	YPS1
Gene names	YPS1 YAP3 YLR120C L2961 L9233.9
Description from SGD	YLR120C YPS1 SGDID:S000004110, Chr XII from 388220-386511, Genome Release 64-3-1, reverse complement, Verified ORF, "Aspartic protease; hyperglycosylated member of the yapsin family of proteases, attached to the plasma membrane via a glycosylphosphatidylinositol (GPI) anchor; involved in nutrient limitation-induced cleavage of the extracellular inhibitory domain of signaling mucin Msb2p, resulting in activation of the filamentous growth MAPK pathway; involved with other yapsins in the cell wall integrity response; role in KEX2-independent processing of the alpha factor precursor"
Protein length	569
Download	sequence (fasta, from Uniprot), modifications (csv format)
Database links	Uniprot, SGD, TheCellVision.org, FungiDB

MKLKTVRSAV LSSLFASQVL GKIIPAANKR DDDSNSKFVK LPFHKLYGDS
LENVGSDKKP EVRLLKRADG YEEIIITNQQ SFYSVDLEVG TPPQNVTVLV
DTGSSDLWIM GSDNPYCSSN SMGSSRRRVI DKRDDSSSGG SLINDINPFG
WLTGTGSAIG PTATGLGGGS GTATQSVPAS EATMDCQQYG TFSTSGSSTF
RSNNTYFSIS YGDGTFASGT FGTDVLDLSD LNVTGLSFAV ANETNSTMGV
LGIGLPELEV TYSGSTASHS GKAYKYDNFP IVLKNSGAIK SNTYSLYLND
SDAMHGTILF GAVDHSKYTG TLYTIPIVNT LSASGFSSPI QFDVTINGIG
ISDSGSSNKT LTTTKIPALL DSGTTLTYLP QTVVSMIATE LGAQYSSRIG
YYVLDCPSDD SMEIVFDFGG FHINAPLSSF ILSTGTTCLL GIIPTSDDTG
TILGDSFLTN AYVVYDLENL EISMAQARYN TTSENIEIIT SSVPSAVKAP
GYTNTWSTSA SIVTGGNIFT VNSSQTASFS GNLTTSTASA TSTSSKRNVG
DHIVPSLPLT LISLLFAFI

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[95, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[232, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[242, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[245, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[358, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)
[480, Glyc]	Zielinska, D.F.,  Gnad, F.,  Schropp, K.,  Wiśniewski, J.R.,  Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications)