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Identification
HMDB Protein ID HMDBP02961
Secondary Accession Numbers
  • 8476
Name Chondroitin sulfate glucuronyltransferase
Synonyms
  1. CSGlcA-T
  2. ChPF-2
  3. ChSy-3
  4. Chondroitin glucuronyltransferase
  5. Chondroitin polymerizing factor 2
  6. Chondroitin synthase 3
  7. N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase
Gene Name CHPF2
Protein Type Enzyme
Biological Properties
General Function Involved in transferase activity, transferring hexosyl groups
Specific Function Transfers glucuronic acid (GlcUA) from UDP-GlcUA to N-acetylgalactosamine residues on the non-reducing end of the elongating chondroitin polymer. Has no N-acetylgalactosaminyltransferase activity.
Pathways
  • Glycosaminoglycan biosynthesis - chondroitin sulfate / dermatan sulfate
Reactions
Uridine diphosphate glucuronic acid + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan → Uridine 5'-diphosphate + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan details
UDP-D-glucuronate + → UDP + details
UDP-D-glucuronate + → UDP + details
Uridine diphosphate glucuronic acid + N-Acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosylproteoglycan → Uridine 5'-diphosphate + beta-D-Glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosylproteoglycan details
GO Classification
Biological Process
chondroitin sulfate biosynthetic process
carbohydrate metabolic process
Cellular Component
Golgi cisterna membrane
integral to membrane
Golgi membrane
Component
golgi membrane
membrane
cell part
organelle membrane
golgi cisterna membrane
Function
catalytic activity
transferase activity
transferase activity, transferring hexosyl groups
transferase activity, transferring glycosyl groups
Molecular Function
N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity
Cellular Location
  1. Golgi apparatus
  2. Golgi stack membrane
  3. Single-pass type II membrane protein (Probable)
Gene Properties
Chromosome Location 7
Locus 7q36.1
SNPs CHPF2
Gene Sequence
>2319 bp
ATGCGACTGAGCTCCCTGTTGGCTCTGCTGCGGCCAGCGCTTCCCCTCATCTTAGGGCTG
TCTCTGGGGTGCAGCCTGAGCCTCCTGCGGGTTTCCTGGATCCAGGGGGAGGGAGAAGAT
CCCTGTGTCGAGGCTGTAGGGGAGCGAGGAGGGCCACAGAATCCAGATTCCAGAGCTCGG
CTAGACCAAAGTGATGAAGACTTCAAACCCCGGATTGTCCCCTACTACAGGGACCCCAAC
AAGCCCTACAAGAAGGTGCTCAGGACTCGGTACATCCAGACAGAGCTGGGCTCCCGTGAG
CGGTTGCTGGTGGCTGTCCTGACCTCCCGAGCTACACTGTCCACTTTGGCCGTGGCTGTG
AACCGTACGGTGGCCCATCACTTCCCTCGGTTACTCTACTTCACTGGGCAGCGGGGGGCC
CGGGCTCCAGCAGGGATGCAGGTGGTGTCTCATGGGGATGAGCGGCCCGCCTGGCTCATG
TCAGAGACCCTGCGCCACCTTCACACACACTTTGGGGCCGACTACGACTGGTTCTTCATC
ATGCAGGATGACACATATGTGCAGGCCCCCCGCCTGGCAGCCCTTGCTGGCCACCTCAGC
ATCAACCAAGACCTGTACTTAGGCCGGGCAGAGGAGTTCATTGGCGCAGGCGAGCAGGCC
CGGTACTGTCATGGGGGCTTTGGCTACCTGTTGTCACGGAGTCTCCTGCTTCGTCTGCGG
CCACATCTGGATGGCTGCCGAGGAGACATTCTCAGTGCCCGTCCTGACGAGTGGCTTGGA
CGCTGCCTCATTGACTCTCTGGGCGTCGGCTGTGTCTCACAGCACCAGGGGCAGCAGTAT
CGCTCATTTGAACTGGCCAAAAATAGGGACCCTGAGAAGGAAGGGAGCTCGGCTTTCCTG
AGTGCCTTCGCCGTGCACCCTGTCTCCGAAGGTACCCTCATGTACCGGCTCCACAAACGC
TTCAGCGCTCTGGAGTTGGAGCGGGCTTACAGTGAAATAGAACAACTGCAGGCTCAGATC
CGGAACCTGACCGTGCTGACCCCCGAAGGGGAGGCAGGGCTGAGCTGGCCCGTTGGGCTC
CCTGCTCCTTTCACACCACACTCTCGCTTTGAGGTGCTGGGCTGGGACTACTTCACAGAG
CAGCACACCTTCTCCTGTGCAGATGGGGCTCCCAAGTGCCCACTACAGGGGGCTAGCAGG
GCGGACGTGGGTGATGCGTTGGAGACTGCCCTGGAGCAGCTCAATCGGCGCTATCAGCCC
CGCCTGCGCTTCCAGAAGCAGCGACTGCTCAACGGCTATCGGCGCTTCGACCCAGCACGG
GGCATGGAGTACACCCTGGACCTGCTGTTGGAATGTGTGACACAGCGTGGGCACCGGCGG
GCCCTGGCTCGCAGGGTCAGCCTGCTGCGGCCACTGAGCCGGGTGGAAATCCTACCTATG
CCCTATGTCACTGAGGCCACCCGAGTGCAGCTGGTGCTGCCACTCCTGGTGGCTGAAGCT
GCTGCAGCCCCGGCTTTCCTCGAGGCCTTTGCAGCCAATGTCCTGGAGCCACGAGAACAT
GCATTGCTCACCCTGTTGCTGGTCTACGGGCCACGAGAAGGTGGCCGTGGAGCTCCAGAC
CCATTTCTTGGGGTGAAGGCTGCAGCAGCGGAGTTAGAGCGACGGTACCCTGGGACGAGG
CTGGCCTGGCTCGCTGTGCGAGCAGAGGCCCCTTCCCAGGTGCGACTCATGGACGTGGTC
TCGAAGAAGCACCCTGTGGACACTCTCTTCTTCCTTACCACCGTGTGGACAAGGCCTGGG
CCCGAAGTCCTCAACCGCTGTCGCATGAATGCCATCTCTGGCTGGCAGGCCTTCTTTCCA
GTCCATTTCCAGGAGTTCAATCCTGCCCTGTCACCACAGAGATCACCCCCAGGGCCCCCG
GGGGCTGGCCCTGACCCCCCCTCCCCTCCTGGTGCTGACCCCTCCCGGGGGGCTCCTATA
GGGGGGAGATTTGACCGGCAGGCTTCTGCGGAGGGCTGCTTCTACAACGCTGACTACCTG
GCGGCCCGAGCCCGGCTGGCAGGTGAACTGGCAGGCCAGGAAGAGGAGGAAGCCCTGGAG
GGGCTGGAGGTGATGGATGTTTTCCTCCGGTTCTCAGGGCTCCACCTCTTTCGGGCCGTA
GAGCCAGGGCTGGTGCAGAAGTTCTCCCTGCGAGACTGCAGCCCACGGCTCAGTGAAGAA
CTCTACCACCGCTGCCGCCTCAGCAACCTGGAGGGGCTAGGGGGCCGTGCCCAGCTGGCT
ATGGCTCTCTTTGAGCAGGAGCAGGCCAATAGCACTTAG
Protein Properties
Number of Residues 772
Molecular Weight 85947.205
Theoretical pI 7.773
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Chondroitin sulfate glucuronyltransferase
MRLSSLLALLRPALPLILGLSLGCSLSLLRVSWIQGEGEDPCVEAVGERGGPQNPDSRAR
LDQSDEDFKPRIVPYYRDPNKPYKKVLRTRYIQTELGSRERLLVAVLTSRATLSTLAVAV
NRTVAHHFPRLLYFTGQRGARAPAGMQVVSHGDERPAWLMSETLRHLHTHFGADYDWFFI
MQDDTYVQAPRLAALAGHLSINQDLYLGRAEEFIGAGEQARYCHGGFGYLLSRSLLLRLR
PHLDGCRGDILSARPDEWLGRCLIDSLGVGCVSQHQGQQYRSFELAKNRDPEKEGSSAFL
SAFAVHPVSEGTLMYRLHKRFSALELERAYSEIEQLQAQIRNLTVLTPEGEAGLSWPVGL
PAPFTPHSRFEVLGWDYFTEQHTFSCADGAPKCPLQGASRADVGDALETALEQLNRRYQP
RLRFQKQRLLNGYRRFDPARGMEYTLDLLLECVTQRGHRRALARRVSLLRPLSRVEILPM
PYVTEATRVQLVLPLLVAEAAAAPAFLEAFAANVLEPREHALLTLLLVYGPREGGRGAPD
PFLGVKAAAAELERRYPGTRLAWLAVRAEAPSQVRLMDVVSKKHPVDTLFFLTTVWTRPG
PEVLNRCRMNAISGWQAFFPVHFQEFNPALSPQRSPPGPPGAGPDPPSPPGADPSRGAPI
GGRFDRQASAEGCFYNADYLAARARLAGELAGQEEEEALEGLEVMDVFLRFSGLHLFRAV
EPGLVQKFSLRDCSPRLSEELYHRCRLSNLEGLGGRAQLAMALFEQEQANST
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q9P2E5
UniProtKB/Swiss-Prot Entry Name CHPF2_HUMAN
PDB IDs Not Available
GenBank Gene ID AB095812
GeneCard ID CHPF2
GenAtlas ID CHPF2
HGNC ID HGNC:29270
References
General References
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  3. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed:10718198 ]
  4. Izumikawa T, Koike T, Shiozawa S, Sugahara K, Tamura J, Kitagawa H: Identification of chondroitin sulfate glucuronyltransferase as chondroitin synthase-3 involved in chondroitin polymerization: chondroitin polymerization is achieved by multiple enzyme complexes consisting of chondroitin synthase family members. J Biol Chem. 2008 Apr 25;283(17):11396-406. doi: 10.1074/jbc.M707549200. Epub 2008 Mar 3. [PubMed:18316376 ]
  5. Gotoh M, Yada T, Sato T, Akashima T, Iwasaki H, Mochizuki H, Inaba N, Togayachi A, Kudo T, Watanabe H, Kimata K, Narimatsu H: Molecular cloning and characterization of a novel chondroitin sulfate glucuronyltransferase that transfers glucuronic acid to N-acetylgalactosamine. J Biol Chem. 2002 Oct 11;277(41):38179-88. Epub 2002 Jul 26. [PubMed:12145278 ]