P40989
Gene name |
GSC2 (FKS2, GLS2, YGR032W) |
Protein name |
1,3-beta-glucan synthase component GSC2 |
Names |
1,3-beta-D-glucan-UDP glucosyltransferase, FK506 sensitivity protein 2, Glucan synthase of cerevisiae protein 2 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YGR032W |
EC number |
2.4.1.34: Hexosyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P40989
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P40989-F1 | Predicted | AlphaFoldDB |
17 variants for P40989
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s07-548807 | 180 | I>M | No | SGRP | |
| s07-549399 | 378 | T>S | No | SGRP | |
| s07-549411 | 382 | R>C | No | SGRP | |
| s07-550224 | 653 | A>S | No | SGRP | |
| s07-550638 | 791 | V>I | No | SGRP | |
| s07-550758 | 831 | D>N | No | SGRP | |
| s07-551443 | 1059 | N>S | strain: SK1 [UniProt] | No | SGRP |
| s07-552012 | 1249 | V>I | No | SGRP | |
| s07-552309 | 1348 | V>I | No | SGRP | |
| s07-552661 | 1465 | A>V | No | SGRP | |
| s07-553250 | 1661 | M>I | No | SGRP | |
| s07-553800 | 1845 | P>S | No | SGRP | |
| s07-553825 | 1853 | T>K | No | SGRP | |
| 1853 | T>KD | strain: SK1 [UniProt] | No | ||
| s07-553828 | 1854 | G>D | No | SGRP | |
| s07-553882 | 1872 | S>F | No | SGRP | |
| s07-553881 | 1872 | S>P | No | SGRP |
No associated diseases with P40989
1 regional properties for P40989
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | 1,3-beta-glucan synthase component FKS1-like, domain-1 | 318 - 430 | IPR026899 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.34 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| 1,3-beta-D-glucan synthase complex | A protein complex that catalyzes the transfer of a glucose group from UDP-glucose to a (1->3)-beta-D-glucan chain. |
| cell periphery | The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures. |
| cellular bud neck | The constriction between the mother cell and daughter cell (bud) in an organism that reproduces by budding. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| prospore membrane | The prospore membrane is a double-membraned structure that extends from the cytoplasmic face of the spindle pole bodies to encompass the spindle pole bodies and the four nuclear lobes that are formed during meiosis. It helps isolate the meiotic nuclei from the cytoplasm during spore formation and serves as a foundation for the formation of the spore walls. An example of this component is found in Schizosaccharomyces pombe. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 1,3-beta-D-glucan synthase activity | Catalysis of the reaction: UDP-glucose + [(1->3)-beta-D-glucosyl](n) = UDP + [(1->3)-beta-D-glucosyl](n+1). |
| glucosyltransferase activity | Catalysis of the transfer of a glucosyl group to an acceptor molecule, typically another carbohydrate or a lipid. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| (1->3)-beta-D-glucan biosynthetic process | The chemical reactions and pathways resulting in the formation of (1->3)-beta-D-glucans, compounds composed of glucose residues linked by (1->3)-beta-D-glucosidic bonds. |
| ascospore wall assembly | The aggregation, arrangement and bonding together of a set of components to form an ascospore wall. During sporulation in Ascomycota, each ascospore nucleus becomes surrounded by a specialized spore wall, formed by deposition of spore wall components in the lumenal space between the outer and inner leaflets of the prospore membrane. An example of this process is found in Saccharomyces cerevisiae. |
| fungal-type cell wall polysaccharide biosynthetic process | The chemical reactions and pathways resulting in the formation of the polysaccharides which make up the fungal-type cell wall. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
3 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q04952 | FKS3 | 1,3-beta-glucan synthase component FKS3 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| P38631 | FKS1 | 1,3-beta-glucan synthase component FKS1 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q9ZT82 | CALS12 | Callose synthase 12 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSYNDPNLNG | QYYSNGDGTG | DGNYPTYQVT | QDQSAYDEYG | QPIYTQNQLD | DGYYDPNEQY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VDGTQFPQGQ | DPSQDQGPYN | NDASYYNQPP | NMMNPSSQDG | ENFSDFSSYG | PPSGTYPNDQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YTPSQMSYPD | QDGSSGASTP | YGNGVVNGNG | QYYDPNAIEM | ALPNDPYPAW | TADPQSPLPI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EQIEDIFIDL | TNKFGFQRDS | MRNMFDHFMT | LLDSRSSRMS | PEQALLSLHA | DYIGGDTANY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KKWYFAAQLD | MDDEIGFRNM | KLGKLSRKAR | KAKKKNKKAM | QEASPEDTEE | TLNQIEGDNS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LEAADFRWKS | KMNQLSPFEM | VRQIALFLLC | WGEANQVRFT | PECLCFIYKC | ASDYLDSAQC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QQRPDPLPEG | DFLNRVITPL | YRFIRSQVYE | IVDGRYVKSE | KDHNKVIGYD | DVNQLFWYPE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GIAKIVMEDG | TRLIDLPAEE | RYLKLGEIPW | DDVFFKTYKE | TRSWLHLVTN | FNRIWIMHIS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VYWMYCAYNA | PTFYTHNYQQ | LVDNQPLAAY | KWATAALGGT | VASLIQVAAT | LCEWSFVPRK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| WAGAQHLSRR | FWFLCVIMGI | NLGPVIFVFA | YDKDTVYSTA | AHVVGAVMFF | VAVATLVFFS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VMPLGGLFTS | YMKKSTRSYV | ASQTFTASFA | PLHGLDRWMS | YLVWVTVFAA | KYAESYFFLI |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LSLRDPIRIL | STTSMRCTGE | YWWGNKICKV | QPKIVLGLMI | ATDFILFFLD | TYLWYIVVNT |
| 730 | 740 | 750 | 760 | 770 | 780 |
| VFSVGKSFYL | GISILTPWRN | IFTRLPKRIY | SKILATTDME | IKYKPKVLIS | QIWNAIIISM |
| 790 | 800 | 810 | 820 | 830 | 840 |
| YREHLLAIDH | VQKLLYHQVP | SEIEGKRTLR | APTFFVSQDD | NNFETEFFPR | DSEAERRISF |
| 850 | 860 | 870 | 880 | 890 | 900 |
| FAQSLSTPIP | EPLPVDNMPT | FTVLTPHYAE | RILLSLREII | REDDQFSRVT | LLEYLKQLHP |
| 910 | 920 | 930 | 940 | 950 | 960 |
| VEWDCFVKDT | KILAEETAAY | ENNEDEPEKE | DALKSQIDDL | PFYCIGFKSA | APEYTLRTRI |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| WASLRSQTLY | RTISGFMNYS | RAIKLLYRVE | NPEIVQMFGG | NADGLERELE | KMARRKFKFL |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| VSMQRLAKFK | PHELENAEFL | LRAYPDLQIA | YLDEEPPLNE | GEEPRIYSAL | IDGHCEILEN |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| GRRRPKFRVQ | LSGNPILGDG | KSDNQNHALI | FYRGEYIQLI | DANQDNYLEE | CLKIRSVLAE |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| FEELGIEQIH | PYTPGLKYED | QSTNHPVAIV | GAREYIFSEN | SGVLGDVAAG | KEQTFGTLFA |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| RTLAQIGGKL | HYGHPDFINA | TFMTTRGGVS | KAQKGLHLNE | DIYAGMNAVL | RGGRIKHCEY |
| 1270 | 1280 | 1290 | 1300 | 1310 | 1320 |
| YQCGKGRDLG | FGTILNFTTK | IGAGMGEQML | SREYYYLGTQ | LPIDRFLTFY | YAHPGFHLNN |
| 1330 | 1340 | 1350 | 1360 | 1370 | 1380 |
| LFIQLSLQMF | MLTLVNLHAL | AHESILCVYD | RDKPITDVLY | PIGCYNFHPA | IDWVRRYTLS |
| 1390 | 1400 | 1410 | 1420 | 1430 | 1440 |
| IFIVFWIAFV | PIVVQELIER | GLWKATQRFF | RHILSLSPMF | EVFAGQIYSS | ALLSDIAVGG |
| 1450 | 1460 | 1470 | 1480 | 1490 | 1500 |
| ARYISTGRGF | ATSRIPFSIL | YSRFAGSAIY | MGSRSMLMLL | FGTVAHWQAP | LLWFWASLSA |
| 1510 | 1520 | 1530 | 1540 | 1550 | 1560 |
| LIFAPFIFNP | HQFAWEDFFL | DYRDYIRWLS | RGNNKYHRNS | WIGYVRMSRS | RVTGFKRKLV |
| 1570 | 1580 | 1590 | 1600 | 1610 | 1620 |
| GDESEKSAGD | ASRAHRTNLI | MAEIIPCAIY | AAGCFIAFTF | INAQTGVKTT | DEDRVNSTLR |
| 1630 | 1640 | 1650 | 1660 | 1670 | 1680 |
| IIICTLAPIV | IDIGVLFFCM | GLSCCSGPLL | GMCCKKTGSV | MAGIAHGIAV | VVHIVFFIVM |
| 1690 | 1700 | 1710 | 1720 | 1730 | 1740 |
| WVLEGFSFVR | MLIGVVTCIQ | CQRLIFHCMT | VLLLTREFKN | DHANTAFWTG | KWYSTGLGYM |
| 1750 | 1760 | 1770 | 1780 | 1790 | 1800 |
| AWTQPTRELT | AKVIELSEFA | ADFVLGHVIL | IFQLPVICIP | KIDKFHSIML | FWLKPSRQIR |
| 1810 | 1820 | 1830 | 1840 | 1850 | 1860 |
| PPIYSLKQAR | LRKRMVRRYC | SLYFLVLIIF | AGCIVGPAVA | SAHVPKDLGS | GLTGTFHNLV |
| 1870 | 1880 | 1890 | |||
| QPRNVSNNDT | GSQMSTYKSH | YYTHTPSLKT | WSTIK |