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

4 structures for P38631

Entry ID Method Resolution Chain Position Source
7XE4 EM 340 A F 1-1876 PDB
7YUY EM 350 A F 1-1876 PDB
8JZN EM 247 A A 1-1876 PDB
AF-P38631-F1 Predicted AlphaFoldDB

62 variants for P38631

Variant ID(s) Position Change Description Diseaes Association Provenance
s12-810052 19 G>D No SGRP
s12-810163 56 M>K No SGRP
s12-810282 96 Y>H No SGRP
s12-810333 113 A>P No SGRP
s12-810333 113 A>S No SGRP
s12-810376 127 S>L No SGRP
s12-810615 207 L>I No SGRP
s12-810702 236 I>V No SGRP
s12-810835 280 N>T No SGRP
s12-811065 357 V>I No SGRP
s12-811113 373 V>I No SGRP
s12-811123 376 R>L No SGRP
s12-811471 492 K>R No SGRP
s12-811617 541 I>V No SGRP
s12-811798 601 V>G No SGRP
s12-811797 601 V>I No SGRP
s12-812411 805 E>D No SGRP
s12-813115 1040 T>N No SGRP
s12-813409 1138 R>K No SGRP
s12-814003 1336 K>I No SGRP
s12-814012 1339 V>A No SGRP
s12-814018 1341 V>D No SGRP
s12-814017 1341 V>F No SGRP
s12-814017 1341 V>I No SGRP
s12-814023 1343 I>F No SGRP
s12-814024 1343 I>N No SGRP
s12-814248 1418 A>T No SGRP
s12-814367 1457 M>I No SGRP
s12-814572 1526 V>M No SGRP
s12-814963 1656 A>V No SGRP
s12-815005 1670 V>A No SGRP
s12-815004 1670 V>I No SGRP
s12-815052 1686 I>V No SGRP
s12-815071 1692 A>V No SGRP
s12-815254 1753 C>F No SGRP
s12-815271 1759 I>L No SGRP
s12-815365 1790 T>S No SGRP
s12-815377 1794 K>R No SGRP
s12-815401 1802 S>C No SGRP
s12-815424 1810 I>L No SGRP
s12-815463 1823 A>S No SGRP
s12-815466 1824 K>Q No SGRP
s12-815472 1826 H>N No SGRP
s12-815474 1826 H>Q No SGRP
s12-815475 1827 K>E No SGRP
s12-815477 1827 K>N No SGRP
s12-815476 1827 K>R No SGRP
s12-815480 1828 H>Q No SGRP
s12-815490 1832 S>A No SGRP
s12-815497 1834 D>A No SGRP
s12-815498 1834 D>E No SGRP
s12-815496 1834 D>N No SGRP
s12-815527 1844 I>K No SGRP
s12-815526 1844 I>V No SGRP
s12-815529 1845 N>D No SGRP
s12-815530 1845 N>S No SGRP
s12-815533 1846 T>K No SGRP
s12-815535 1847 T>S No SGRP
s12-815541 1849 N>D No SGRP
s12-815554 1853 S>F No SGRP
s12-815561 1855 M>I No SGRP
s12-815571 1859 Q>E No SGRP

No associated diseases with P38631

5 regional properties for P38631

Type Name Position InterPro Accession
domain TolB, N-terminal 23 - 121 IPR007195
repeat WD40-like beta propeller 199 - 223 IPR011659-1
repeat WD40-like beta propeller 237 - 272 IPR011659-2
repeat WD40-like beta propeller 281 - 315 IPR011659-3
repeat WD40-like beta propeller 369 - 396 IPR011659-4

Functions

Description
EC Number 2.4.1.34 Hexosyltransferases
Subcellular Localization
  • Mitochondrion
  • Cell membrane ; Multi-pass membrane protein
  • Localizes to the sites of polarized growth
  • Colocalizes with cortical actin patches and moves on the cell surface at the sites of cell wall remodeling
  • Actin patch motility is required for the movement
  • Early at the cell cycle, localizes at the presumed bud site of the mother cell and at the tip of the small bud
  • As the bud enlarges, appears as discernible spots in the medium-sized bud and these spots colocalize with actin patches
  • Late in the cell cycle, disappears in large budded cells, while the actin patches disperse over the cell
  • During cytokinesis, is concentrated in the neck, overlapping with the location of cortical actin patches
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

10 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.
actin cortical patch An endocytic patch that consists of an actin-containing structure found at the plasma membrane in cells; formed of networks of branched actin filaments that lie just beneath the plasma membrane and assemble, move, and disassemble rapidly. An example of this is the actin cortical patch found in Saccharomyces cerevisiae.
cell periphery The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures.
cellular bud A protuberance from a cell of an organism that reproduces by budding, which will grow larger and become a separate daughter cell after nuclear division, cytokinesis, and cell wall formation (when appropriate). The daughter cell may completely separate from the mother cell, or the mother and daughter cells may remain associated.
cellular bud neck The constriction between the mother cell and daughter cell (bud) in an organism that reproduces by budding.
cellular bud tip The end of a cellular bud distal to the site of attachment to the mother cell.
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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

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.

7 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 biogenesis A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a fungal-type cell wall. The fungal-type cell wall contains beta-glucan and may contain chitin.
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.
positive regulation of endocytosis Any process that activates or increases the frequency, rate or extent of endocytosis.
regulation of cell shape Any process that modulates the surface configuration of a cell.
regulation of cell size Any process that modulates the size 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
P40989 GSC2 1,3-beta-glucan synthase component GSC2 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
MNTDQQPYQG QTDYTQGPGN GQSQEQDYDQ YGQPLYPSQA DGYYDPNVAA GTEADMYGQQ
70 80 90 100 110 120
PPNESYDQDY TNGEYYGQPP NMAAQDGENF SDFSSYGPPG TPGYDSYGGQ YTASQMSYGE
130 140 150 160 170 180
PNSSGTSTPI YGNYDPNAIA MALPNEPYPA WTADSQSPVS IEQIEDIFID LTNRLGFQRD
190 200 210 220 230 240
SMRNMFDHFM VLLDSRSSRM SPDQALLSLH ADYIGGDTAN YKKWYFAAQL DMDDEIGFRN
250 260 270 280 290 300
MSLGKLSRKA RKAKKKNKKA MEEANPEDTE ETLNKIEGDN SLEAADFRWK AKMNQLSPLE
310 320 330 340 350 360
RVRHIALYLL CWGEANQVRF TAECLCFIYK CALDYLDSPL CQQRQEPMPE GDFLNRVITP
370 380 390 400 410 420
IYHFIRNQVY EIVDGRFVKR ERDHNKIVGY DDLNQLFWYP EGIAKIVLED GTKLIELPLE
430 440 450 460 470 480
ERYLRLGDVV WDDVFFKTYK ETRTWLHLVT NFNRIWVMHI SIFWMYFAYN SPTFYTHNYQ
490 500 510 520 530 540
QLVDNQPLAA YKWASCALGG TVASLIQIVA TLCEWSFVPR KWAGAQHLSR RFWFLCIIFG
550 560 570 580 590 600
INLGPIIFVF AYDKDTVYST AAHVVAAVMF FVAVATIIFF SIMPLGGLFT SYMKKSTRRY
610 620 630 640 650 660
VASQTFTAAF APLHGLDRWM SYLVWVTVFA AKYSESYYFL VLSLRDPIRI LSTTAMRCTG
670 680 690 700 710 720
EYWWGAVLCK VQPKIVLGLV IATDFILFFL DTYLWYIIVN TIFSVGKSFY LGISILTPWR
730 740 750 760 770 780
NIFTRLPKRI YSKILATTDM EIKYKPKVLI SQVWNAIIIS MYREHLLAID HVQKLLYHQV
790 800 810 820 830 840
PSEIEGKRTL RAPTFFVSQD DNNFETEFFP RDSEAERRIS FFAQSLSTPI PEPLPVDNMP
850 860 870 880 890 900
TFTVLTPHYA ERILLSLREI IREDDQFSRV TLLEYLKQLH PVEWECFVKD TKILAEETAA
910 920 930 940 950 960
YEGNENEAEK EDALKSQIDD LPFYCIGFKS AAPEYTLRTR IWASLRSQTL YRTISGFMNY
970 980 990 1000 1010 1020
SRAIKLLYRV ENPEIVQMFG GNAEGLEREL EKMARRKFKF LVSMQRLAKF KPHELENAEF
1030 1040 1050 1060 1070 1080
LLRAYPDLQI AYLDEEPPLT EGEEPRIYSA LIDGHCEILD NGRRRPKFRV QLSGNPILGD
1090 1100 1110 1120 1130 1140
GKSDNQNHAL IFYRGEYIQL IDANQDNYLE ECLKIRSVLA EFEELNVEQV NPYAPGLRYE
1150 1160 1170 1180 1190 1200
EQTTNHPVAI VGAREYIFSE NSGVLGDVAA GKEQTFGTLF ARTLSQIGGK LHYGHPDFIN
1210 1220 1230 1240 1250 1260
ATFMTTRGGV SKAQKGLHLN EDIYAGMNAM LRGGRIKHCE YYQCGKGRDL GFGTILNFTT
1270 1280 1290 1300 1310 1320
KIGAGMGEQM LSREYYYLGT QLPVDRFLTF YYAHPGFHLN NLFIQLSLQM FMLTLVNLSS
1330 1340 1350 1360 1370 1380
LAHESIMCIY DRNKPKTDVL VPIGCYNFQP AVDWVRRYTL SIFIVFWIAF VPIVVQELIE
1390 1400 1410 1420 1430 1440
RGLWKATQRF FCHLLSLSPM FEVFAGQIYS SALLSDLAIG GARYISTGRG FATSRIPFSI
1450 1460 1470 1480 1490 1500
LYSRFAGSAI YMGARSMLML LFGTVAHWQA PLLWFWASLS SLIFAPFVFN PHQFAWEDFF
1510 1520 1530 1540 1550 1560
LDYRDYIRWL SRGNNQYHRN SWIGYVRMSR ARITGFKRKL VGDESEKAAG DASRAHRTNL
1570 1580 1590 1600 1610 1620
IMAEIIPCAI YAAGCFIAFT FINAQTGVKT TDDDRVNSVL RIIICTLAPI AVNLGVLFFC
1630 1640 1650 1660 1670 1680
MGMSCCSGPL FGMCCKKTGS VMAGIAHGVA VIVHIAFFIV MWVLESFNFV RMLIGVVTCI
1690 1700 1710 1720 1730 1740
QCQRLIFHCM TALMLTREFK NDHANTAFWT GKWYGKGMGY MAWTQPSREL TAKVIELSEF
1750 1760 1770 1780 1790 1800
AADFVLGHVI LICQLPLIII PKIDKFHSIM LFWLKPSRQI RPPIYSLKQT RLRKRMVKKY
1810 1820 1830 1840 1850 1860
CSLYFLVLAI FAGCIIGPAV ASAKIHKHIG DSLDGVVHNL FQPINTTNND TGSQMSTYQS
1870
HYYTHTPSLK TWSTIK