Q5RBC3

PR
Gene name
EXT1
Protein name
Exostosin-1
Names
Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase, Multiple exostoses protein 1 homolog
Species
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
KEGG Pathway
pon:100172450
EC number
2.4.1.225: Hexosyltransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-119 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q5RBC3

Entry ID Method Resolution Chain Position Source
AF-Q5RBC3-F1 Predicted AlphaFoldDB

No variants for Q5RBC3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5RBC3

No associated diseases with Q5RBC3

1 regional properties for Q5RBC3

Type Name Position InterPro Accession
domain Enkurin domain 243 - 343 IPR027012

Functions

Description
EC Number 2.4.1.225 Hexosyltransferases
Subcellular Localization
  • Golgi apparatus membrane ; Single-pass type II membrane protein
  • Golgi apparatus, cis-Golgi network membrane ; Single-pass type II membrane protein
  • Endoplasmic reticulum membrane ; Single-pass type II membrane protein
  • The active heparan sulfate polymerase complex composed of EXT1 and EXT2 is localized to the Golgi apparatus
  • If both proteins are individually detected in the endoplasmic reticulum, the formation of the complex promotes their transport to the Golgi
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.
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.

3 GO annotations of molecular function

Name Definition
glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity Catalysis of the reaction: beta-D-glucuronosyl-(1,4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan + UDP-N-acetyl-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-(1,4)-beta-D-glucuronosyl-(1,4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan + UDP.
metal ion binding Binding to a metal ion.
N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity Catalysis of the reaction: N-acetyl-alpha-D-glucosaminyl-(1,4)-beta-D-glucuronosyl-proteoglycan + UDP-alpha-D-glucuronate = beta-D-glucuronosyl-(1,4)-N-acetyl-alpha-D-glucosaminyl-(1,4)-beta-D-glucuronosyl-proteoglycan + UDP.

2 GO annotations of biological process

Name Definition
heparan sulfate proteoglycan biosynthetic process The chemical reactions and pathways resulting in the formation of the heparan sulfate proteoglycan, a glycosaminoglycan with repeat unit consisting of alternating alpha-(1->4)-linked hexuronic acid and glucosamine residues; the former are a mixture of sulfated and nonsulfated D-glucuronic acid and L-iduronic acid; the L-iduronic acid is either sulfated or acetylated on its amino group as well as being sulfated on one of its hydroxyl groups; heparan sulfate chains are covalently linked to peptidyl-serine by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylosyl to serine residues.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MQAKKRYFIL LSAGSCLALL FYFGGLQFRA SRSHSRREEH SGRNGLHHPS PDHFWPRFPD
70 80 90 100 110 120
ALRPFVPWDQ LENEDSSVHI SPRQKRDANS SIYKGKKCRM ESCFDFTLCK KNGFKVYAYP
130 140 150 160 170 180
QQKGEKIAES YQNILAAIEG SRFYTSDPSQ ACLFVLSLDT LDRDQLSPQY VHNLRSKVQS
190 200 210 220 230 240
LHLWNNGRNH LIFNLYSGTW PDYTEDVGFD IGQAMLAKAS ISTENFRPNF DVSIPLFSKD
250 260 270 280 290 300
HPRTGGERGF LKFNTIPPLR KYMLVFKGKR YLTGIGSDTR NALYHVHNGE DVVLLTTCKH
310 320 330 340 350 360
GKDWQKHKDS RCDRDNTEYE KYDYREMLHN ATFCLVPRGR RLGSFRFLEA LQAACVPVML
370 380 390 400 410 420
SNGWELPFSE VINWNQAAVI GDERLLLQIP STIRSIHQDK ILALRQQTQF LWEAYFSSVE
430 440 450 460 470 480
KIVLTTLEII QDRIFKHISR NSLIWNKHPG GLFVLPQYSS YLGDFPYYYA NLGLKPPSKF
490 500 510 520 530 540
TAVIHAVTPL VSQSQPVLKL LVAAAKSQYC AQIIVLWNCD KPLPAKHRWP ATAVPVIVIE
550 560 570 580 590 600
GESKVMSSRF LPYDNIITDA VLSLDEDTVL STTEVDFAFT VWRSFPERIV GYPARSHFWD
610 620 630 640 650 660
NSKERWGYTS KWTNDYSMVL TGAAIYHKYY HYLYSHYLPA SLKNMVDQLA NCEDILMNFL
670 680 690 700 710 720
VSAVTKLPPI KVTQKEQYKE TMMGQTSRAS RWADPDHFAQ RQSCMNTFAS WFGYMPLIHS
730 740
QMRLDPVLFK DQVSILRKKY RDIERL