P22855

PR
Gene name
AMS1 (YGL156W, G1861)
Protein name
Alpha-mannosidase
Names
Alpha-D-mannoside mannohydrolase
Species
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
KEGG Pathway
sce:YGL156W
EC number
3.2.1.24: Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

40-113 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

2 structures for P22855

Entry ID Method Resolution Chain Position Source
5JM0 EM 630 A A 1-1070 PDB
AF-P22855-F1 Predicted AlphaFoldDB

19 variants for P22855

Variant ID(s) Position Change Description Diseaes Association Provenance
s07-210787 123 S>A No SGRP
s07-210790 124 N>D No SGRP
s07-211180 254 D>N No SGRP
s07-211628 403 K>R No SGRP
s07-211889 490 Y>C No SGRP
s07-212155 579 K>Q No SGRP
s07-212445 675 M>I No SGRP
s07-212537 706 Y>S No SGRP
s07-212602 728 I>V No SGRP
s07-212684 755 Y>F No SGRP
s07-212744 775 Y>F No SGRP
s07-213124 902 D>N No SGRP
s07-213416 999 A>D No SGRP
s07-213443 1008 P>R No SGRP
s07-213442 1008 P>S No SGRP
s07-213472 1018 V>I No SGRP
s07-213514 1032 T>A No SGRP
s07-213604 1062 H>D No SGRP
s07-213653 1078 S>L No SGRP

No associated diseases with P22855

2 regional properties for P22855

Type Name Position InterPro Accession
domain Glycosyl transferase, family 1 288 - 446 IPR001296
domain Glycosyltransferase subfamily 4-like, N-terminal domain 75 - 245 IPR028098

Functions

Description
EC Number 3.2.1.24 Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Subcellular Localization
  • Vacuole
  • Localizes to the inner surface of the vacuolar membrane
  • Under nutrient-rich conditions, the protein is delivered to the vacuole by the cytoplasm to vacuole targeting (Cvt) pathway
  • Under starvation conditions, the protein is localized through autophagy
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
Cvt complex A protein complex that is involved in the Cvt pathway. In budding yeast, the Cvt complex consists of multimers of preApe1p.
fungal-type vacuole membrane The lipid bilayer surrounding a vacuole, the shape of which correlates with cell cycle phase. The membrane separates its contents from the cytoplasm of the cell. An example of this structure is found in Saccharomyces cerevisiae.

3 GO annotations of molecular function

Name Definition
alpha-mannosidase activity Catalysis of the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
carbohydrate binding Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
metal ion binding Binding to a metal ion.

2 GO annotations of biological process

Name Definition
mannose catabolic process The chemical reactions and pathways resulting in the breakdown of mannose, the aldohexose manno-hexose, the C-2 epimer of glucose.
oligosaccharide catabolic process The chemical reactions and pathways resulting in the breakdown of oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSSEDIIYDP QFKPVQGIYE NRLRQFIDTG GDYHDLNLPK FYDKKRISLD HDHVKVWWYQ
70 80 90 100 110 120
VSFERGSSPV SPDKRPSWKS IIERDKKGEL EFREANINQP FGPSWSTTWF KVKISLPEDW
130 140 150 160 170 180
VKSNEQLLFQ WDCSNEGIVI DPKTLIPVTA FSGGERTEYV LPKTSDGKHF FYIEAGNNGM
190 200 210 220 230 240
FGCGAGSTIN PPDDNRFFHL RKADIVWPDL DARALYIDFW MLGDAARELP GDSWQKHQAR
250 260 270 280 290 300
QLGNAVMNLF DPNDRSSVRK CRELLQREYF DSFLESSKVY EQGESQVLTN VYGIGNCHID
310 320 330 340 350 360
TAWLWPFAET RRKIVRSWSS QCTLMDRFPE YKFVASQAQQ FKWLLEDHPE FFNKVLIPKI
370 380 390 400 410 420
QQSQFFAVGG TWVENDTNIP SGESLARQFF FGQRFFLKHF GLKSKIFWLP DTFGYSSQMP
430 440 450 460 470 480
QLCRLSGIDK FLTQKLSWNN INSFPHSTFN WAGIDGSQLL THMPPGNTYT ADSHFGDVLR
490 500 510 520 530 540
TAKQNKTPEY YGSGLMLYGK GDGGGGPTEE MLQKMRRIRS MNNRNGNVIP KLQVGITVDE
550 560 570 580 590 600
FYDDILKRTN QGHDLPTWSG ELYFEFHRGT YTSQAQTKKL MRLSEIKLHD LEWIAAKTSV
610 620 630 640 650 660
LYPDSYKYPS KQINELWENV LLCQFHDVLP GSCIEMVYKY EAVPMLHNVV KECTSLIDKT
670 680 690 700 710 720
VQFLQSQSKA DLVEMRTLTW SKPEKVSEEC SLNGSYTSSV TGYDDYIVLA NGKLKVIICK
730 740 750 760 770 780
KTGVITSITD ETLGVEYLDT EHGRNKLGAN QFVIYDDKPL GWQAWDTELY SVNQYKYVTK
790 800 810 820 830 840
PKKVQVSCNT KEKCAVEVIF QISEKCKIKS VISLNATAVT DAKLSKVDIS TTVENWDARN
850 860 870 880 890 900
KFLKVEFPVN IRNDFASYET QFGITKRPTH YNTSWDVAKF EVCHHKFADY SEYSKGVSIL
910 920 930 940 950 960
NDCKYGFSTH GNLMRLSLLR SPKAPDAHAD MGTHEIKYAI YPHRGALSSD TVKLAHEFNY
970 980 990 1000 1010 1020
CFKYKLPKDI GMNFDDIISI SGDENVILSN IKRGEDDSAV KSNYSLNPRD EQSIVVRVYE
1030 1040 1050 1060 1070 1080
SLGGESFASL NTTLNLKRIE KVDNLEMKVY KSLTATRDES NHAINRIPIK LRPFEIASFR
LYF