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 P53954

Entry ID Method Resolution Chain Position Source
AF-P53954-F1 Predicted AlphaFoldDB

8 variants for P53954

Variant ID(s) Position Change Description Diseaes Association Provenance
s14-538211 13 V>G No SGRP
s14-538250 26 S>F No SGRP
s14-538255 28 V>L No SGRP
s14-538316 48 S>N No SGRP
s14-538531 120 V>I No SGRP
s14-538565 131 A>V No SGRP
s14-539006 278 T>M No SGRP
s14-539026 285 P>S No SGRP

No associated diseases with P53954

2 regional properties for P53954

Type Name Position InterPro Accession
domain Glycosyl transferase, family 1 293 - 466 IPR001296
domain ALG11 mannosyltransferase, N-terminal 72 - 274 IPR031814

Functions

Description
EC Number 2.4.1.131 Hexosyltransferases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

2 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.
GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity Catalysis of the reaction: an alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-D-GlcNAc-diphosphodolichol + 2 GDP + 2 H+. This reaction is the transfer of an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage.

3 GO annotations of biological process

Name Definition
oligosaccharide-lipid intermediate biosynthetic process The chemical reactions and pathways resulting in the formation of an oligosaccharide-lipid intermediate, such as a molecule of dolichol-P-man or dolicol-P-Glc used in N-linked glycosylation.
protein glycosylation A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.
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.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9XEE9 ALG11 GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase Arabidopsis thaliana (Mouse-ear cress) PR
Q6P312 alg11 GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
Q7ZW24 alg11 GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MGSAWTNYNF EEVKSHFGFK KYVVSSLVLV YGLIKVLTWI FRQWVYSSLN PFSKKSSLLN
70 80 90 100 110 120
RAVASCGEKN VKVFGFFHPY CNAGGGGEKV LWKAVDITLR KDAKNVIVIY SGDFVNGENV
130 140 150 160 170 180
TPENILNNVK AKFDYDLDSD RIFFISLKLR YLVDSSTWKH FTLIGQAIGS MILAFESIIQ
190 200 210 220 230 240
CPPDIWIDTM GYPFSYPIIA RFLRRIPIVT YTHYPIMSKD MLNKLFKMPK KGIKVYGKIL
250 260 270 280 290 300
YWKVFMLIYQ SIGSKIDIVI TNSTWTNNHI KQIWQSNTCK IIYPPCSTEK LVDWKQKFGT
310 320 330 340 350 360
AKGERLNQAI VLAQFRPEKR HKLIIESFAT FLKNLPDSVS PIKLIMAGST RSKQDENYVK
370 380 390 400 410 420
SLQDWSENVL KIPKHLISFE KNLPFDKIEI LLNKSTFGVN AMWNEHFGIA VVEYMASGLI
430 440 450 460 470 480
PIVHASAGPL LDIVTPWDAN GNIGKAPPQW ELQKKYFAKL EDDGETTGFF FKEPSDPDYN
490 500 510 520 530 540
TTKDPLRYPN LSDLFLQITK LDYDCLRVMG ARNQQYSLYK FSDLKFDKDW ENFVLNPICK
LLEEEERG