Basic Information
Name | Probable 1,3-beta-glucanosyltransferase GAS3 (EC 2.4.1.-) (Glycolipid-anchored surface protein 3) |
Uniprot ID | Q03655 |
Systematic gene name | YMR215W |
Standard gene name | GAS3 |
Gene names | GAS3 YMR215W YM8261.09 |
Description from SGD | YMR215W GAS3 SGDID:S000004828, Chr XIII from 696796-698370, Genome Release 64-3-1, Verified ORF, "Putative 1,3-beta-glucanosyltransferase; has similarity go other GAS family members; low abundance, possibly inactive member of the GAS family of GPI-containing proteins; localizes to the cell wall; mRNA induced during sporulation" |
Protein length | 524 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MQLSKSILLA ALAATPSLVN AMLPIHIKNY RFIKPSSATN SESDNEVFFV
KGVDYQPGGS SGYDADSDTD ILSDPEVCAR DAYAFQQLGV NTVRIYSLNP
DLNHDKCMTI FNNAGIYAIL DVNSGNYGES LNRADPSGTY DSLYLSRVFK
FIDAFKNYPN VLGFFSGNEV INDQSDYAKI DPPYIRAVQR DMKQYISKHA
NRSIPVGYSA ADNTDLRLAT FKYLQCNSLD GNKVNDDLDI SKSDFFGLNT
YEWCSGTSSW ESSGYDKLNS TFEDAVIPLI FSEYGCNKNT PRTFDEVSEG
LYGGLKNVFS GGLVYEYTEE ANNYGLVKLD DSGSLTYKDD FVNLESQLKN
VSLPTTKESE ISSDSIYKCD NSAITNIYSG FGTNNFTLPS QPAEIANMIE
YGVNGTNTGK ILTDYAVPTT FNYTIKNNKD DTISATISYD KANSLNELDV
TATTVAKSAS TSQSSSRSLT SSTSPSSSTG SSSSTGSSSA SSSSKSKGVG
NIVNVSFSQS GYLALFAGLI SALL
KGVDYQPGGS SGYDADSDTD ILSDPEVCAR DAYAFQQLGV NTVRIYSLNP
DLNHDKCMTI FNNAGIYAIL DVNSGNYGES LNRADPSGTY DSLYLSRVFK
FIDAFKNYPN VLGFFSGNEV INDQSDYAKI DPPYIRAVQR DMKQYISKHA
NRSIPVGYSA ADNTDLRLAT FKYLQCNSLD GNKVNDDLDI SKSDFFGLNT
YEWCSGTSSW ESSGYDKLNS TFEDAVIPLI FSEYGCNKNT PRTFDEVSEG
LYGGLKNVFS GGLVYEYTEE ANNYGLVKLD DSGSLTYKDD FVNLESQLKN
VSLPTTKESE ISSDSIYKCD NSAITNIYSG FGTNNFTLPS QPAEIANMIE
YGVNGTNTGK ILTDYAVPTT FNYTIKNNKD DTISATISYD KANSLNELDV
TATTVAKSAS TSQSSSRSLT SSTSPSSSTG SSSSTGSSSA SSSSKSKGVG
NIVNVSFSQS GYLALFAGLI SALL
Legend
- X Phoshorylation
- X Glycosylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[228, Phos] | Rekstina, V.V., Bykova, A.A., Ziganshin, R.H., Kalebina, T.S. (2019). GPI-Modified Proteins Non-covalently Attached to Saccharomyces cerevisiae Yeast Cell Wall. Biochemistry (Mosc) 84: 1513-1520 (Publication) (All modifications) |
[269, 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) |
[269, Glyc] | Yeo, K.Y.B., Chrysanthopoulos, P.K., Nouwens, A.S., Marcellin, E., Schulz, B.L. (2016). High-performance targeted mass spectrometry with precision data-independent acquisition reveals site-specific glycosylation macroheterogeneity. Anal Biochem 510: 106-113. (Publication) (All modifications) |
[350, 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) |
[404, 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) |