Basic Information
Name | Mannosyl-oligosaccharide glucosidase (EC 3.2.1.106) (Processing A-glucosidase I) (Glucosidase I) |
Uniprot ID | P53008 |
Systematic gene name | YGL027C |
Standard gene name | CWH41 |
Gene names | CWH41 GLS1 YGL027C |
Description from SGD | YGL027C CWH41 SGDID:S000002995, Chr VII from 446143-443642, Genome Release 64-3-1, reverse complement, Verified ORF, "Processing alpha glucosidase I; ER type II integral membrane N-glycoprotein involved in assembly of cell wall beta 1,6 glucan and asparagine-linked protein glycosylation; also involved in ER protein quality control and sensing of ER stress" |
Protein length | 833 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLISKSKMFK TFWILTSIVL LASATVDISK LQEFEEYQKF TNESLLWAPY
RSNCYFGMRP RYVHESPLIM GIMWFNSLSQ DGLHSLRHFA TPQDKLQKYG
WEVYDPRIGG KEVFIDEKNN LNLTVYFVKS KNGENWSVRV QGEPLDPKRP
STASVVLYFS QNGGEIDGKS SLAMIGHDGP NDMKFFGYSK ELGEYHLTVK
DNFGHYFKNP EYETMEVAPG SDCSKTSHLS LQIPDKEVWK ARDVFQSLVS
DSIRDILEKE ETKQRPADLI PSVLTIRNLY NFNPGNFHYI QKTFDLTKKD
GFQFDITYNK LGTTQSISTR EQVTELITWS LNEINARFDK QFSFGEGPDS
IESVEVKRRF ALETLSNLLG GIGYFYGNQL IDRETEFDES QFTEIKLLNA
KEEGPFELFT SVPSRGFFPR GFYWDEGFHL LQIMEYDFDL AFEILASWFE
MIEDDSGWIA REIILGNEAR SKVPQEFQVQ NPNIANPPTL LLAFSEMLSR
AIENIGDFNS DSYHQVMFNS RTAKFMTNNL EANPGLLTEY AKKIYPKLLK
HYNWFRKSQT GLIDEYEEIL EDEGIWDKIH KNEVYRWVGR TFTHCLPSGM
DDYPRAQPPD VAELNVDALA WVGVMTRSMK QIAHVLKLTQ DEQRYAQIEQ
EVVENLDLLH WSENDNCYCD ISIDPEDDEI REFVCHEGYV SVLPFALKLI
PKNSPKLEKV VALMSDPEKI FSDYGLLSLS RQDDYFGKDE NYWRGPIWMN
INYLCLDAMR YYYPEVILDV AGEASNAKKL YQSLKINLSN NIYKVWEEQG
YCYENYSPID GHGTGAEHFT GWTALVVNIL GRF
RSNCYFGMRP RYVHESPLIM GIMWFNSLSQ DGLHSLRHFA TPQDKLQKYG
WEVYDPRIGG KEVFIDEKNN LNLTVYFVKS KNGENWSVRV QGEPLDPKRP
STASVVLYFS QNGGEIDGKS SLAMIGHDGP NDMKFFGYSK ELGEYHLTVK
DNFGHYFKNP EYETMEVAPG SDCSKTSHLS LQIPDKEVWK ARDVFQSLVS
DSIRDILEKE ETKQRPADLI PSVLTIRNLY NFNPGNFHYI QKTFDLTKKD
GFQFDITYNK LGTTQSISTR EQVTELITWS LNEINARFDK QFSFGEGPDS
IESVEVKRRF ALETLSNLLG GIGYFYGNQL IDRETEFDES QFTEIKLLNA
KEEGPFELFT SVPSRGFFPR GFYWDEGFHL LQIMEYDFDL AFEILASWFE
MIEDDSGWIA REIILGNEAR SKVPQEFQVQ NPNIANPPTL LLAFSEMLSR
AIENIGDFNS DSYHQVMFNS RTAKFMTNNL EANPGLLTEY AKKIYPKLLK
HYNWFRKSQT GLIDEYEEIL EDEGIWDKIH KNEVYRWVGR TFTHCLPSGM
DDYPRAQPPD VAELNVDALA WVGVMTRSMK QIAHVLKLTQ DEQRYAQIEQ
EVVENLDLLH WSENDNCYCD ISIDPEDDEI REFVCHEGYV SVLPFALKLI
PKNSPKLEKV VALMSDPEKI FSDYGLLSLS RQDDYFGKDE NYWRGPIWMN
INYLCLDAMR YYYPEVILDV AGEASNAKKL YQSLKINLSN NIYKVWEEQG
YCYENYSPID GHGTGAEHFT GWTALVVNIL GRF
Legend
- X Glycosylation
- X Phoshorylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[42, 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) |
[99, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[99, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[122, 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) |
[510, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[510, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[513, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[513, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[520, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[520, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[540, Phos] | Studer RA, Rodriguez-Mias RA, Haas KM, et al (2016) Evolution of protein phosphorylation across 18 fungal species. Science 354:229–232. (Publication) (All modifications) |
[540, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[542, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |