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 P27810

Entry ID Method Resolution Chain Position Source
AF-P27810-F1 Predicted AlphaFoldDB

5 variants for P27810

Variant ID(s) Position Change Description Diseaes Association Provenance
s15-512257 144 E>D No SGRP
s15-512567 248 A>S No SGRP
s15-512727 301 R>H No SGRP
s15-512730 302 E>A No SGRP
s15-512990 389 Q>K No SGRP

No associated diseases with P27810

No regional properties for P27810

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P27810

Functions

Description
EC Number
Subcellular Localization
  • Golgi apparatus membrane; Single-pass type II membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
fungal-type vacuole A vacuole that has both lytic and storage functions. The fungal vacuole is a large, membrane-bounded organelle that functions as a reservoir for the storage of small molecules (including polyphosphate, amino acids, several divalent cations (e.g. calcium), other ions, and other small molecules) as well as being the primary compartment for degradation. It is an acidic compartment, containing an ensemble of acid hydrolases. At least in S. cerevisiae, there are indications that the morphology of the vacuole is variable and correlated with the cell cycle, with logarithmically growing cells having a multilobed, reticulated vacuole, while stationary phase cells contain a single large structure.
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.
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
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.

1 GO annotations of molecular function

Name Definition
alpha-1,2-mannosyltransferase activity Catalysis of the transfer of a mannose residue to an oligosaccharide, forming an alpha-(1->2) linkage.

4 GO annotations of biological process

Name Definition
cell wall mannoprotein biosynthetic process The chemical reactions and pathways resulting in the formation of cell wall mannoproteins, any cell wall protein that contains covalently bound mannose residues.
mannosylation The covalent attachment of a mannose residue to a substrate molecule.
protein N-linked glycosylation A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
protein O-linked glycosylation A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P27809 KRE2 Glycolipid 2-alpha-mannosyltransferase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
10 20 30 40 50 60
MAKIMIPASK QPVYKKLGLL LVAVFTVYVF FHGAQYARGS APSPKYSTVL SSGSGYKYSK
70 80 90 100 110 120
VELPKYTGPR EKATFVTLVR NRDLYSLAES IKSVEDRFNS KFNYDWVFLN DEEFTDEFKN
130 140 150 160 170 180
VTSALVSGTT KYGVIPKEHW SFPEWIDEEK AAQVRKEMGE KRIIYGDSIS YRHMCRFESG
190 200 210 220 230 240
FFYRHPLMDD YDWYWRVEPD IKLHCDIDYD VFKFMKDNKK KYAFAISIKE YEATIPTLWE
250 260 270 280 290 300
TTRKFMEAHP ELIHENNMLD FVSDDQGLSY NLCHFWSNFE IAALDLWRSP AYSAYFDYLD
310 320 330 340 350 360
REGGFFYERW GDAPVHSIGA ALFLDRSEIH HFGDIGYYHV PFHSCPIDTS IRLANKCDCD
370 380 390
PSKDFTWHSY SCTTKFYNIN KLPKPAGWQN HIG