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 P46971

Entry ID Method Resolution Chain Position Source
AF-P46971-F1 Predicted AlphaFoldDB

10 variants for P46971

Variant ID(s) Position Change Description Diseaes Association Provenance
s10-699845 255 A>V No SGRP
s10-699690 307 S>T No SGRP
s10-699429 394 S>G No SGRP
s10-699269 447 L>S No SGRP
s10-699102 503 I>V No SGRP
s10-699052 519 D>E No SGRP
s10-699015 532 I>V No SGRP
s10-698460 717 V>I No SGRP
s10-698433 726 V>I No SGRP
s10-698384 742 S>T No SGRP

No associated diseases with P46971

3 regional properties for P46971

Type Name Position InterPro Accession
domain Glycosyl transferase family 39/83 58 - 305 IPR003342
domain MIR motif 331 - 521 IPR016093
domain Protein O-mannosyl-transferase, C-terminal four TM domain 541 - 755 IPR032421

Functions

Description
EC Number 2.4.1.109 Hexosyltransferases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
dolichyl-phosphate-mannose-protein mannosyltransferase Pmt4p homodimer complex A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt4p.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
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.

2 GO annotations of molecular function

Name Definition
dolichyl-phosphate-mannose-protein mannosyltransferase activity Catalysis of the reaction: dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.
identical protein binding Binding to an identical protein or proteins.

3 GO annotations of biological process

Name Definition
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.
protein O-linked mannosylation The transfer of mannose from dolichyl activated mannose to the hydroxyl group of a seryl or threonyl residue of a protein acceptor molecule, to form an O-linked protein-sugar linkage.
regulation of endoplasmic reticulum unfolded protein response Any process that modulates the frequency, rate or extent of endoplasmic reticulum unfolded protein response.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P47190 PMT3 Dolichyl-phosphate-mannose--protein mannosyltransferase 3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P31382 PMT2 Dolichyl-phosphate-mannose--protein mannosyltransferase 2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9VTK2 rt Protein O-mannosyltransferase 1 Drosophila melanogaster (Fruit fly) PR
10 20 30 40 50 60
MSVPKKRNHG KLPPSTKDVD DPSLKYTKAA PKCEQVAEHW LLQPLPEPES RYSFWVTIVT
70 80 90 100 110 120
LLAFAARFYK IWYPKEVVFD EVHFGKFASY YLERSYFFDV HPPFAKMMIA FIGWLCGYDG
130 140 150 160 170 180
SFKFDEIGYS YETHPAPYIA YRSFNAILGT LTVPIMFNTL KELNFRAITC AFASLLVAID
190 200 210 220 230 240
TAHVTETRLI LLDAILIISI AATMYCYVRF YKCQLRQPFT WSWYIWLHAT GLSLSFVIST
250 260 270 280 290 300
KYVGVMTYSA IGFAAVVNLW QLLDIKAGLS LRQFMRHFSK RLNGLVLIPF VIYLFWFWVH
310 320 330 340 350 360
FTVLNTSGPG DAFMSAEFQE TLKDSPLSVD SKTVNYFDII TIKHQDTDAF LHSHLARYPQ
370 380 390 400 410 420
RYEDGRISSA GQQVTGYTHP DFNNQWEVLP PHGSDVGKGQ AVLLNQHIRL RHVATDTYLL
430 440 450 460 470 480
AHDVASPFYP TNEEITTVTL EEGDGELYPE TLFAFQPLKK SDEGHVLKSK TVSFRLFHVD
490 500 510 520 530 540
TSVALWTHND ELLPDWGFQQ QEINGNKKVI DPSNNWVVDE IVNLDEVRKV YIPKVVKPLP
550 560 570 580 590 600
FLKKWIETQK SMFEHNNKLS SEHPFASEPY SWPGSLSGVS FWTNGDEKKQ IYFIGNIIGW
610 620 630 640 650 660
WFQVISLAVF VGIIVADLIT RHRGYYALNK MTREKLYGPL MFFFVSWCCH YFPFFLMARQ
670 680 690 700 710 720
KFLHHYLPAH LIACLFSGAL WEVIFSDCKS LDLEKDEDIS GASYERNPKV YVKPYTVFLV
730 740 750 760
CVSCAVAWFF VYFSPLVYGD VSLSPSEVVS REWFDIELNF SK