CHPF2_HUMAN
ID CHPF2_HUMAN Reviewed; 772 AA.
AC Q9P2E5; B2DBD8; Q6P2I4; Q6UXD2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Chondroitin sulfate glucuronyltransferase;
DE EC=2.4.1.226;
DE AltName: Full=CSGlcA-T;
DE AltName: Full=Chondroitin glucuronyltransferase;
DE AltName: Full=Chondroitin polymerizing factor 2;
DE Short=ChPF-2;
DE AltName: Full=Chondroitin synthase 3;
DE Short=ChSy-3;
DE AltName: Full=N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase;
GN Name=CHPF2; Synonyms=CHSY3, CSGLCAT, KIAA1402; ORFNames=UNQ299/PRO339;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=18316376; DOI=10.1074/jbc.m707549200;
RA Izumikawa T., Koike T., Shiozawa S., Sugahara K., Tamura J., Kitagawa H.;
RT "Identification of chondroitin sulfate glucuronyltransferase as chondroitin
RT synthase-3 involved in chondroitin polymerization: chondroitin
RT polymerization is achieved by multiple enzyme complexes consisting of
RT chondroitin synthase family members.";
RL J. Biol. Chem. 283:11396-11406(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12145278; DOI=10.1074/jbc.m202601200;
RA Gotoh M., Yada T., Sato T., Akashima T., Iwasaki H., Mochizuki H.,
RA Inaba N., Togayachi A., Kudo T., Watanabe H., Kimata K., Narimatsu H.;
RT "Molecular cloning and characterization of a novel chondroitin sulfate
RT glucuronyltransferase that transfers glucuronic acid to N-
RT acetylgalactosamine.";
RL J. Biol. Chem. 277:38179-38188(2002).
CC -!- FUNCTION: Transfers glucuronic acid (GlcUA) from UDP-GlcUA to N-
CC acetylgalactosamine residues on the non-reducing end of the elongating
CC chondroitin polymer. Has no N-acetylgalactosaminyltransferase activity.
CC {ECO:0000269|PubMed:12145278, ECO:0000269|PubMed:18316376}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-
CC (1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-
CC glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-
CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-
CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:23428, Rhea:RHEA-COMP:12575,
CC Rhea:RHEA-COMP:14058, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132105, ChEBI:CHEBI:138442;
CC EC=2.4.1.226;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-([beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-
CC D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-
CC GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:54996,
CC Rhea:RHEA-COMP:14060, Rhea:RHEA-COMP:14061, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:138444,
CC ChEBI:CHEBI:138445; EC=2.4.1.226;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2E5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2E5-2; Sequence=VSP_012724, VSP_012725;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in placenta, small
CC intestine and pancreas. {ECO:0000269|PubMed:12145278}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92640.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB095812; BAG30817.1; -; mRNA.
DR EMBL; AB037823; BAA92640.1; ALT_INIT; mRNA.
DR EMBL; AY358407; AAQ88773.1; -; mRNA.
DR EMBL; CH471173; EAW54011.1; -; Genomic_DNA.
DR EMBL; BC064509; AAH64509.1; -; mRNA.
DR CCDS; CCDS34779.1; -. [Q9P2E5-1]
DR RefSeq; NP_061888.1; NM_019015.2. [Q9P2E5-1]
DR AlphaFoldDB; Q9P2E5; -.
DR SMR; Q9P2E5; -.
DR BioGRID; 119984; 111.
DR IntAct; Q9P2E5; 7.
DR MINT; Q9P2E5; -.
DR STRING; 9606.ENSP00000035307; -.
DR GlyConnect; 1113; 2 N-Linked glycans (1 site).
DR GlyGen; Q9P2E5; 2 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q9P2E5; -.
DR PhosphoSitePlus; Q9P2E5; -.
DR BioMuta; CHPF2; -.
DR DMDM; 67462204; -.
DR EPD; Q9P2E5; -.
DR jPOST; Q9P2E5; -.
DR MassIVE; Q9P2E5; -.
DR MaxQB; Q9P2E5; -.
DR PaxDb; Q9P2E5; -.
DR PeptideAtlas; Q9P2E5; -.
DR PRIDE; Q9P2E5; -.
DR ProteomicsDB; 83794; -. [Q9P2E5-1]
DR ProteomicsDB; 83795; -. [Q9P2E5-2]
DR Antibodypedia; 18744; 105 antibodies from 22 providers.
DR DNASU; 54480; -.
DR Ensembl; ENST00000035307.7; ENSP00000035307.2; ENSG00000033100.17. [Q9P2E5-1]
DR GeneID; 54480; -.
DR KEGG; hsa:54480; -.
DR MANE-Select; ENST00000035307.7; ENSP00000035307.2; NM_019015.3; NP_061888.1.
DR UCSC; uc003wjr.3; human. [Q9P2E5-1]
DR CTD; 54480; -.
DR DisGeNET; 54480; -.
DR GeneCards; CHPF2; -.
DR HGNC; HGNC:29270; CHPF2.
DR HPA; ENSG00000033100; Low tissue specificity.
DR MIM; 608037; gene.
DR neXtProt; NX_Q9P2E5; -.
DR OpenTargets; ENSG00000033100; -.
DR PharmGKB; PA165617920; -.
DR VEuPathDB; HostDB:ENSG00000033100; -.
DR eggNOG; KOG3708; Eukaryota.
DR GeneTree; ENSGT01050000244857; -.
DR HOGENOM; CLU_016244_1_0_1; -.
DR InParanoid; Q9P2E5; -.
DR OMA; FGSDYDW; -.
DR OrthoDB; 758579at2759; -.
DR PhylomeDB; Q9P2E5; -.
DR TreeFam; TF318303; -.
DR BioCyc; MetaCyc:HS12080-MON; -.
DR BRENDA; 2.4.1.226; 2681.
DR PathwayCommons; Q9P2E5; -.
DR Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
DR SignaLink; Q9P2E5; -.
DR BioGRID-ORCS; 54480; 13 hits in 1082 CRISPR screens.
DR ChiTaRS; CHPF2; human.
DR GenomeRNAi; 54480; -.
DR Pharos; Q9P2E5; Tbio.
DR PRO; PR:Q9P2E5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9P2E5; protein.
DR Bgee; ENSG00000033100; Expressed in stromal cell of endometrium and 100 other tissues.
DR ExpressionAtlas; Q9P2E5; baseline and differential.
DR Genevisible; Q9P2E5; HS.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0050510; F:N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity; TAS:Reactome.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IBA:GO_Central.
DR InterPro; IPR008428; Chond_GalNAc.
DR Pfam; PF05679; CHGN; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..772
FT /note="Chondroitin sulfate glucuronyltransferase"
FT /id="PRO_0000189563"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..772
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 629..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..654
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 638..666
FT /note="GPPGAGPDPPSPPGADPSRGAPIGGRFDR -> NLITFPLSASAPGRARQDG
FT GQIENCCCIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012724"
FT VAR_SEQ 667..772
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012725"
SQ SEQUENCE 772 AA; 85948 MW; A4F6EC591919F4A2 CRC64;
MRLSSLLALL RPALPLILGL SLGCSLSLLR VSWIQGEGED PCVEAVGERG GPQNPDSRAR
LDQSDEDFKP RIVPYYRDPN KPYKKVLRTR YIQTELGSRE RLLVAVLTSR ATLSTLAVAV
NRTVAHHFPR LLYFTGQRGA RAPAGMQVVS HGDERPAWLM SETLRHLHTH FGADYDWFFI
MQDDTYVQAP RLAALAGHLS INQDLYLGRA EEFIGAGEQA RYCHGGFGYL LSRSLLLRLR
PHLDGCRGDI LSARPDEWLG RCLIDSLGVG CVSQHQGQQY RSFELAKNRD PEKEGSSAFL
SAFAVHPVSE GTLMYRLHKR FSALELERAY SEIEQLQAQI RNLTVLTPEG EAGLSWPVGL
PAPFTPHSRF EVLGWDYFTE QHTFSCADGA PKCPLQGASR ADVGDALETA LEQLNRRYQP
RLRFQKQRLL NGYRRFDPAR GMEYTLDLLL ECVTQRGHRR ALARRVSLLR PLSRVEILPM
PYVTEATRVQ LVLPLLVAEA AAAPAFLEAF AANVLEPREH ALLTLLLVYG PREGGRGAPD
PFLGVKAAAA ELERRYPGTR LAWLAVRAEA PSQVRLMDVV SKKHPVDTLF FLTTVWTRPG
PEVLNRCRMN AISGWQAFFP VHFQEFNPAL SPQRSPPGPP GAGPDPPSPP GADPSRGAPI
GGRFDRQASA EGCFYNADYL AARARLAGEL AGQEEEEALE GLEVMDVFLR FSGLHLFRAV
EPGLVQKFSL RDCSPRLSEE LYHRCRLSNL EGLGGRAQLA MALFEQEQAN ST
