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   23-FEB-2022, entry version 144.
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};
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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   SMR; Q9P2E5; -.
DR   BioGRID; 119984; 56.
DR   IntAct; Q9P2E5; 6.
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; 103 antibodies from 21 providers.
DR   DNASU; 54480; -.
DR   Ensembl; ENST00000035307; ENSP00000035307; ENSG00000033100.
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; ENSGT01030000234702; -.
DR   HOGENOM; CLU_016244_1_0_1; -.
DR   InParanoid; Q9P2E5; -.
DR   OMA; PKCEMRG; -.
DR   OrthoDB; 758579at2759; -.
DR   PhylomeDB; Q9P2E5; -.
DR   TreeFam; TF318303; -.
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; 8 hits in 1049 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 adenohypophysis and 119 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
//