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

2 structures for P47190

Entry ID Method Resolution Chain Position Source
6ZQQ X-ray 190 A A/B/C/D 331-532 PDB
AF-P47190-F1 Predicted AlphaFoldDB

10 variants for P47190

Variant ID(s) Position Change Description Diseaes Association Provenance
s15-916091 22 T>R No SGRP
s15-916136 37 K>M No SGRP
s15-916163 46 V>A No SGRP
s15-916801 259 S>G No SGRP
s15-916873 283 I>V No SGRP
s15-916876 284 F>V No SGRP
s15-917460 478 K>N No SGRP
s15-917621 532 E>G No SGRP
s15-917886 620 F>L No SGRP
s15-918225 733 D>E No SGRP

No associated diseases with P47190

3 regional properties for P47190

Type Name Position InterPro Accession
domain Glycosyl transferase family 39/83 63 - 305 IPR003342
domain MIR motif 332 - 523 IPR016093
domain Protein O-mannosyl-transferase, C-terminal four TM domain 541 - 744 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 Pmt1p-Pmt3p dimer complex A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt1p-Pmt3p.
dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt3p dimer complex A protein dimer complex that possesses dolichyl-phosphate-mannose-protein mannosyltransferase activity and, in S. cerevisiae, is composed of Pmt5p-Pmt3p.
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).
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
dolichyl-phosphate-mannose-protein mannosyltransferase activity Catalysis of the reaction: dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.

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
P31382 PMT2 Dolichyl-phosphate-mannose--protein mannosyltransferase 2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P46971 PMT4 Dolichyl-phosphate-mannose--protein mannosyltransferase 4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9UKY4 POMT2 Protein O-mannosyl-transferase 2 Homo sapiens (Human) PR
10 20 30 40 50 60
MPYRVATGYS EKSTDDDLIW RTPIVKEELE DADNFLKDDA ELYDKVKNES AVSHLDTIVM
70 80 90 100 110 120
PIIFTVLGMF TRMYKIGRNN HVVWDEAHFG KFGSYYLRHE FYHDVHPPLG KMLVGLSGYL
130 140 150 160 170 180
AGYNGSWDFP SGEVYPDYID YVKMRLFQAM FSSLCVPLAY FTGRAIGFSR LSVWLFTILV
190 200 210 220 230 240
IFENSYATLG KFILLDSMLL FFTVSSYFCL AKFHTMRKSP FSARWWLWLC LTGLNLGCAI
250 260 270 280 290 300
SVKMVGLFII SVVGIYTISE LWNLLSDRSV SWKVYVNHWL ARIFGLIIIP VCVFLLCFKI
310 320 330 340 350 360
HFDLLSNSGP GDSTMPSLFQ ASLNGTKVGK GPRDVALGSS IISIKNQALG GALLHSHVQP
370 380 390 400 410 420
FPEGSEQQQV TVYGYSDANN EWFFQRIRGV EPWTDAENKT IEFVKGGEMY RLMHRLTGKN
430 440 450 460 470 480
LHTHEVPAPI SKSEYEVSAY GDVDLGDYKD NWIIEIVEQV GEEDPTLLHP LSTSFRIKNS
490 500 510 520 530 540
ILGCYLAQSG KHLPEWGFRQ GEVVCLKHAS KRDKRTWWNI ETHENERLPQ GEDFVYPKTS
550 560 570 580 590 600
FFRNFMQLNS AMMATNNALV PNPEKFDGIA SSAWQWPTLN VGVRLCEWSE KSIKYFLLGS
610 620 630 640 650 660
PASVWPSSIA VCALIIHVIF LTLKWQRQCV ILSDPVERDV FVMAAFYPLL AWLLHYMPFV
670 680 690 700 710 720
VMSRVVYAHH YLPTLYFALM ILSYYFDMIT KRWATRNTGK FLRLGAYIVY GSIVIAGFFY
730 740 750
FSPFSFGMDG PVDDYAYLAW LPTWQIVEDI RNT