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Chondroitin sulfate glucuronyltransferase (EC 2.4.1.226) (CSGlcA-T) (Chondroitin glucuronyltransferase) (Chondroitin polymerizing factor 2) (ChPF-2) (Chondroitin synthase 3) (ChSy-3) (N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase)

 CHPF2_HUMAN             Reviewed;         772 AA.
Q9P2E5; B2DBD8; Q6P2I4; Q6UXD2;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 2.
12-SEP-2018, entry version 125.
RecName: Full=Chondroitin sulfate glucuronyltransferase;
EC=2.4.1.226;
AltName: Full=CSGlcA-T;
AltName: Full=Chondroitin glucuronyltransferase;
AltName: Full=Chondroitin polymerizing factor 2;
Short=ChPF-2;
AltName: Full=Chondroitin synthase 3;
Short=ChSy-3;
AltName: Full=N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase;
Name=CHPF2; Synonyms=CHSY3, CSGLCAT, KIAA1402; ORFNames=UNQ299/PRO339;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=18316376; DOI=10.1074/jbc.M707549200;
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. 283:11396-11406(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., 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. 7:65-73(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12145278; DOI=10.1074/jbc.M202601200;
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. 277:38179-38188(2002).
-!- 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.
{ECO:0000269|PubMed:12145278, ECO:0000269|PubMed:18316376}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucuronate + [protein]-3-O-(beta-
D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-
(1->4)-beta-D-Xyl)-L-serine = UDP + [protein]-3-O-(beta-D-GlcA-
(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-
beta-D-Gal-(1->4)-beta-D-Xyl)-L-serine.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucuronate + [protein]-3-O-
((beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3))(n)-beta-D-GalNAc-
(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-
beta-D-Xyl)-L-serine = UDP + [protein]-3-O-(beta-D-GlcA-(1->3)-
(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3))(n)-beta-D-GalNAc-(1->4)-
beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-
Xyl)-L-serine.
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
{ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9P2E5-1; Sequence=Displayed;
Name=2;
IsoId=Q9P2E5-2; Sequence=VSP_012724, VSP_012725;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in placenta,
small intestine and pancreas. {ECO:0000269|PubMed:12145278}.
-!- SIMILARITY: Belongs to the chondroitin N-
acetylgalactosaminyltransferase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA92640.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB095812; BAG30817.1; -; mRNA.
EMBL; AB037823; BAA92640.1; ALT_INIT; mRNA.
EMBL; AY358407; AAQ88773.1; -; mRNA.
EMBL; CH471173; EAW54011.1; -; Genomic_DNA.
EMBL; BC064509; AAH64509.1; -; mRNA.
CCDS; CCDS34779.1; -. [Q9P2E5-1]
RefSeq; NP_061888.1; NM_019015.2. [Q9P2E5-1]
UniGene; Hs.647084; -.
ProteinModelPortal; Q9P2E5; -.
SMR; Q9P2E5; -.
BioGrid; 119984; 6.
IntAct; Q9P2E5; 1.
MINT; Q9P2E5; -.
STRING; 9606.ENSP00000035307; -.
iPTMnet; Q9P2E5; -.
PhosphoSitePlus; Q9P2E5; -.
DMDM; 67462204; -.
EPD; Q9P2E5; -.
MaxQB; Q9P2E5; -.
PaxDb; Q9P2E5; -.
PeptideAtlas; Q9P2E5; -.
PRIDE; Q9P2E5; -.
ProteomicsDB; 83794; -.
ProteomicsDB; 83795; -. [Q9P2E5-2]
Ensembl; ENST00000035307; ENSP00000035307; ENSG00000033100. [Q9P2E5-1]
GeneID; 54480; -.
KEGG; hsa:54480; -.
UCSC; uc003wjr.3; human. [Q9P2E5-1]
CTD; 54480; -.
EuPathDB; HostDB:ENSG00000033100.14; -.
GeneCards; CHPF2; -.
H-InvDB; HIX0007230; -.
HGNC; HGNC:29270; CHPF2.
HPA; HPA020992; -.
MIM; 608037; gene.
neXtProt; NX_Q9P2E5; -.
OpenTargets; ENSG00000033100; -.
PharmGKB; PA165617920; -.
eggNOG; KOG3708; Eukaryota.
eggNOG; ENOG410XWZJ; LUCA.
GeneTree; ENSGT00760000119143; -.
HOGENOM; HOG000037934; -.
InParanoid; Q9P2E5; -.
KO; K03419; -.
OMA; ILPMPYV; -.
OrthoDB; EOG091G04Y5; -.
PhylomeDB; Q9P2E5; -.
TreeFam; TF318303; -.
BioCyc; MetaCyc:HS12080-MONOMER; -.
BRENDA; 2.4.1.226; 2681.
Reactome; R-HSA-2022870; Chondroitin sulfate biosynthesis.
ChiTaRS; CHPF2; human.
GenomeRNAi; 54480; -.
PRO; PR:Q9P2E5; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000033100; Expressed in 92 organ(s), highest expression level in adenohypophysis.
ExpressionAtlas; Q9P2E5; baseline and differential.
Genevisible; Q9P2E5; HS.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IEA:InterPro.
GO; GO:0050510; F:N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase activity; TAS:Reactome.
GO; GO:0030206; P:chondroitin sulfate biosynthetic process; TAS:Reactome.
InterPro; IPR008428; Chond_GalNAc.
Pfam; PF05679; CHGN; 1.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Glycoprotein;
Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 772 Chondroitin sulfate
glucuronyltransferase.
/FTId=PRO_0000189563.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 772 Lumenal. {ECO:0000255}.
COMPBIAS 498 505 Poly-Ala.
COMPBIAS 628 659 Gly/Pro-rich.
CARBOHYD 121 121 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 342 342 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 638 666 GPPGAGPDPPSPPGADPSRGAPIGGRFDR -> NLITFPLS
ASAPGRARQDGGQIENCCCIF (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012724.
VAR_SEQ 667 772 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012725.
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


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