Basic Information

NameProbable 1,3-beta-glucanosyltransferase GAS3 (EC 2.4.1.-) (Glycolipid-anchored surface protein 3)
Uniprot IDQ03655
Systematic gene nameYMR215W
Standard gene nameGAS3
Gene namesGAS3 YMR215W YM8261.09
Description from SGDYMR215W 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 length524
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, 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

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)