Full text data of B3GAT2
B3GAT2
(GLCATS, KIAA1963)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2; 2.4.1.135 (Beta-1,3-glucuronyltransferase 2; GlcAT-D; UDP-glucuronosyltransferase S; GlcAT-S; Glucuronosyltransferase S)
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2; 2.4.1.135 (Beta-1,3-glucuronyltransferase 2; GlcAT-D; UDP-glucuronosyltransferase S; GlcAT-S; Glucuronosyltransferase S)
hRBCD
IPI00221205
IPI00221205 Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2 Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a cytoplasmic n/a expected molecular weight found in band between 49 and 62 kDa
IPI00221205 Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2 Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a cytoplasmic n/a expected molecular weight found in band between 49 and 62 kDa
UniProt
Q9NPZ5
ID B3GA2_HUMAN Reviewed; 323 AA.
AC Q9NPZ5; Q5JS09; Q8TF38; Q96NK4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 2.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2;
DE EC=2.4.1.135;
DE AltName: Full=Beta-1,3-glucuronyltransferase 2;
DE AltName: Full=GlcAT-D;
DE AltName: Full=UDP-glucuronosyltransferase S;
DE Short=GlcAT-S;
DE Short=Glucuronosyltransferase S;
GN Name=B3GAT2; Synonyms=GLCATS, KIAA1963;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12522689; DOI=10.1007/s100380200103;
RA Marcos I., Galan J.J., Borrego S., Antinolo G.;
RT "Cloning, characterization, and chromosome mapping of the human GlcAT-
RT S gene.";
RL J. Hum. Genet. 47:677-680(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII.
RT The complete sequences of 50 new cDNA clones which code for large
RT proteins.";
RL DNA Res. 8:319-327(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-323.
RC TISSUE=Fetal brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 78-323.
RX PubMed=16897771; DOI=10.1002/prot.21118;
RA Shiba T., Kakuda S., Ishiguro M., Morita I., Oka S., Kawasaki T.,
RA Wakatsuki S., Kato R.;
RT "Crystal structure of GlcAT-S, a human glucuronyltransferase, involved
RT in the biosynthesis of the HNK-1 carbohydrate epitope.";
RL Proteins 65:499-508(2006).
CC -!- FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate
CC epitope on both glycolipids and glycoproteins (By similarity).
CC -!- CATALYTIC ACTIVITY: UDP-glucuronate + 3-beta-D-galactosyl-4-beta-
CC D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-
CC glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-
CC xylosylprotein.
CC -!- COFACTOR: Manganese.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer (Potential).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC II membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the trachea, retina, spinal cord,
CC hippocampus and other brain regions, and, at lower levels, in
CC testis and ovary.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB70889.1; Type=Erroneous initiation;
CC Sequence=BAB85549.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database;
CC URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/";
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DR EMBL; AY070019; AAL57718.1; -; mRNA.
DR EMBL; AY070110; AAL58977.1; -; Genomic_DNA.
DR EMBL; AY070108; AAL58977.1; JOINED; Genomic_DNA.
DR EMBL; AY070109; AAL58977.1; JOINED; Genomic_DNA.
DR EMBL; AB075843; BAB85549.1; ALT_INIT; mRNA.
DR EMBL; AL121961; CAI42145.1; -; Genomic_DNA.
DR EMBL; AL450320; CAI42145.1; JOINED; Genomic_DNA.
DR EMBL; AL450320; CAI39582.1; -; Genomic_DNA.
DR EMBL; AL121961; CAI39582.1; JOINED; Genomic_DNA.
DR EMBL; AK055248; BAB70889.1; ALT_INIT; mRNA.
DR RefSeq; NP_542780.1; NM_080742.2.
DR UniGene; Hs.713609; -.
DR PDB; 2D0J; X-ray; 2.00 A; A/B/C/D=78-323.
DR PDBsum; 2D0J; -.
DR ProteinModelPortal; Q9NPZ5; -.
DR SMR; Q9NPZ5; 78-323.
DR STRING; 9606.ENSP00000230053; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR DMDM; 14285363; -.
DR PaxDb; Q9NPZ5; -.
DR PRIDE; Q9NPZ5; -.
DR Ensembl; ENST00000230053; ENSP00000230053; ENSG00000112309.
DR GeneID; 135152; -.
DR KEGG; hsa:135152; -.
DR UCSC; uc003pfv.3; human.
DR CTD; 135152; -.
DR GeneCards; GC06M071566; -.
DR HGNC; HGNC:922; B3GAT2.
DR HPA; HPA012059; -.
DR MIM; 607497; gene.
DR neXtProt; NX_Q9NPZ5; -.
DR PharmGKB; PA25216; -.
DR eggNOG; NOG292627; -.
DR HOGENOM; HOG000261693; -.
DR HOVERGEN; HBG050650; -.
DR InParanoid; Q9NPZ5; -.
DR KO; K10157; -.
DR OMA; FILLPWV; -.
DR OrthoDB; EOG7QG44X; -.
DR PhylomeDB; Q9NPZ5; -.
DR BioCyc; MetaCyc:HS03557-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR UniPathway; UPA00378; -.
DR EvolutionaryTrace; Q9NPZ5; -.
DR GeneWiki; B3GAT2; -.
DR GenomeRNAi; 135152; -.
DR NextBio; 83461; -.
DR PRO; PR:Q9NPZ5; -.
DR ArrayExpress; Q9NPZ5; -.
DR Bgee; Q9NPZ5; -.
DR CleanEx; HS_B3GAT2; -.
DR Genevestigator; Q9NPZ5; -.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
DR GO; GO:0030204; P:chondroitin sulfate metabolic process; TAS:Reactome.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005027; Glyco_trans_43.
DR PANTHER; PTHR10896; PTHR10896; 1.
DR Pfam; PF03360; Glyco_transf_43; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Glycoprotein; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 323 Galactosylgalactosylxylosylprotein 3-
FT beta-glucuronosyltransferase 2.
FT /FTId=PRO_0000195172.
FT TOPO_DOM 1 2 Cytoplasmic (Potential).
FT TRANSMEM 3 23 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 24 323 Lumenal (Potential).
FT NP_BIND 87 89 UDP-glucuronate binding (By similarity).
FT NP_BIND 185 187 UDP-glucuronate binding (By similarity).
FT NP_BIND 300 302 UDP-glucuronate binding (By similarity).
FT REGION 234 243 Interaction with galactose moiety of
FT substrate glycoprotein (By similarity).
FT ACT_SITE 273 273 Proton donor/acceptor (By similarity).
FT METAL 187 187 Manganese (By similarity).
FT BINDING 118 118 UDP-glucuronate (By similarity).
FT BINDING 155 155 UDP-glucuronate (By similarity).
FT BINDING 160 160 UDP-glucuronate (By similarity).
FT SITE 218 218 Interaction with galactose moiety of
FT substrate glycoprotein (By similarity).
FT SITE 310 310 Interaction with galactose moiety of
FT substrate glycoprotein (By similarity).
FT CARBOHYD 67 67 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 292 292 N-linked (GlcNAc...) (Potential).
FT STRAND 82 88
FT HELIX 94 105
FT STRAND 111 121
FT HELIX 124 132
FT STRAND 137 141
FT HELIX 157 170
FT STRAND 173 175
FT STRAND 180 183
FT HELIX 193 198
FT STRAND 202 206
FT STRAND 209 212
FT STRAND 215 223
FT STRAND 226 231
FT HELIX 244 246
FT STRAND 247 250
FT HELIX 251 256
FT STRAND 266 268
FT HELIX 269 271
FT HELIX 272 278
FT HELIX 283 285
FT HELIX 290 293
FT STRAND 313 315
SQ SEQUENCE 323 AA; 36919 MW; 85058D52D2D28463 CRC64;
MKSALFTRFF ILLPWILIVI IMLDVDTRRP VPPLTPRPYF SPYAVGRGGA RLPLRRGGPA
HGTQKRNQSR PQPQPEPQLP TIYAITPTYS RPVQKAELTR LANTFRQVAQ LHWILVEDAA
ARSELVSRFL ARAGLPSTHL HVPTPRRYKR PGLPRATEQR NAGLAWLRQR HQHQRAQPGV
LFFADDDNTY SLELFQEMRT TRKVSVWPVG LVGGRRYERP LVENGKVVGW YTGWRADRPF
AIDMAGFAVS LQVILSNPKA VFKRRGSQPG MQESDFLKQI TTVEELEPKA NNCTKVLVWH
TRTEKVNLAN EPKYHLDTVK IEV
//
ID B3GA2_HUMAN Reviewed; 323 AA.
AC Q9NPZ5; Q5JS09; Q8TF38; Q96NK4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 2.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2;
DE EC=2.4.1.135;
DE AltName: Full=Beta-1,3-glucuronyltransferase 2;
DE AltName: Full=GlcAT-D;
DE AltName: Full=UDP-glucuronosyltransferase S;
DE Short=GlcAT-S;
DE Short=Glucuronosyltransferase S;
GN Name=B3GAT2; Synonyms=GLCATS, KIAA1963;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12522689; DOI=10.1007/s100380200103;
RA Marcos I., Galan J.J., Borrego S., Antinolo G.;
RT "Cloning, characterization, and chromosome mapping of the human GlcAT-
RT S gene.";
RL J. Hum. Genet. 47:677-680(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII.
RT The complete sequences of 50 new cDNA clones which code for large
RT proteins.";
RL DNA Res. 8:319-327(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-323.
RC TISSUE=Fetal brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 78-323.
RX PubMed=16897771; DOI=10.1002/prot.21118;
RA Shiba T., Kakuda S., Ishiguro M., Morita I., Oka S., Kawasaki T.,
RA Wakatsuki S., Kato R.;
RT "Crystal structure of GlcAT-S, a human glucuronyltransferase, involved
RT in the biosynthesis of the HNK-1 carbohydrate epitope.";
RL Proteins 65:499-508(2006).
CC -!- FUNCTION: Involved in the biosynthesis of L2/HNK-1 carbohydrate
CC epitope on both glycolipids and glycoproteins (By similarity).
CC -!- CATALYTIC ACTIVITY: UDP-glucuronate + 3-beta-D-galactosyl-4-beta-
CC D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-
CC glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-
CC xylosylprotein.
CC -!- COFACTOR: Manganese.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer (Potential).
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC II membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the trachea, retina, spinal cord,
CC hippocampus and other brain regions, and, at lower levels, in
CC testis and ovary.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 43 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB70889.1; Type=Erroneous initiation;
CC Sequence=BAB85549.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=GGDB; Note=GlycoGene database;
CC URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/";
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DR EMBL; AY070019; AAL57718.1; -; mRNA.
DR EMBL; AY070110; AAL58977.1; -; Genomic_DNA.
DR EMBL; AY070108; AAL58977.1; JOINED; Genomic_DNA.
DR EMBL; AY070109; AAL58977.1; JOINED; Genomic_DNA.
DR EMBL; AB075843; BAB85549.1; ALT_INIT; mRNA.
DR EMBL; AL121961; CAI42145.1; -; Genomic_DNA.
DR EMBL; AL450320; CAI42145.1; JOINED; Genomic_DNA.
DR EMBL; AL450320; CAI39582.1; -; Genomic_DNA.
DR EMBL; AL121961; CAI39582.1; JOINED; Genomic_DNA.
DR EMBL; AK055248; BAB70889.1; ALT_INIT; mRNA.
DR RefSeq; NP_542780.1; NM_080742.2.
DR UniGene; Hs.713609; -.
DR PDB; 2D0J; X-ray; 2.00 A; A/B/C/D=78-323.
DR PDBsum; 2D0J; -.
DR ProteinModelPortal; Q9NPZ5; -.
DR SMR; Q9NPZ5; 78-323.
DR STRING; 9606.ENSP00000230053; -.
DR CAZy; GT43; Glycosyltransferase Family 43.
DR DMDM; 14285363; -.
DR PaxDb; Q9NPZ5; -.
DR PRIDE; Q9NPZ5; -.
DR Ensembl; ENST00000230053; ENSP00000230053; ENSG00000112309.
DR GeneID; 135152; -.
DR KEGG; hsa:135152; -.
DR UCSC; uc003pfv.3; human.
DR CTD; 135152; -.
DR GeneCards; GC06M071566; -.
DR HGNC; HGNC:922; B3GAT2.
DR HPA; HPA012059; -.
DR MIM; 607497; gene.
DR neXtProt; NX_Q9NPZ5; -.
DR PharmGKB; PA25216; -.
DR eggNOG; NOG292627; -.
DR HOGENOM; HOG000261693; -.
DR HOVERGEN; HBG050650; -.
DR InParanoid; Q9NPZ5; -.
DR KO; K10157; -.
DR OMA; FILLPWV; -.
DR OrthoDB; EOG7QG44X; -.
DR PhylomeDB; Q9NPZ5; -.
DR BioCyc; MetaCyc:HS03557-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR UniPathway; UPA00378; -.
DR EvolutionaryTrace; Q9NPZ5; -.
DR GeneWiki; B3GAT2; -.
DR GenomeRNAi; 135152; -.
DR NextBio; 83461; -.
DR PRO; PR:Q9NPZ5; -.
DR ArrayExpress; Q9NPZ5; -.
DR Bgee; Q9NPZ5; -.
DR CleanEx; HS_B3GAT2; -.
DR Genevestigator; Q9NPZ5; -.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015018; F:galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
DR GO; GO:0030204; P:chondroitin sulfate metabolic process; TAS:Reactome.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005027; Glyco_trans_43.
DR PANTHER; PTHR10896; PTHR10896; 1.
DR Pfam; PF03360; Glyco_transf_43; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Glycoprotein; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 323 Galactosylgalactosylxylosylprotein 3-
FT beta-glucuronosyltransferase 2.
FT /FTId=PRO_0000195172.
FT TOPO_DOM 1 2 Cytoplasmic (Potential).
FT TRANSMEM 3 23 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 24 323 Lumenal (Potential).
FT NP_BIND 87 89 UDP-glucuronate binding (By similarity).
FT NP_BIND 185 187 UDP-glucuronate binding (By similarity).
FT NP_BIND 300 302 UDP-glucuronate binding (By similarity).
FT REGION 234 243 Interaction with galactose moiety of
FT substrate glycoprotein (By similarity).
FT ACT_SITE 273 273 Proton donor/acceptor (By similarity).
FT METAL 187 187 Manganese (By similarity).
FT BINDING 118 118 UDP-glucuronate (By similarity).
FT BINDING 155 155 UDP-glucuronate (By similarity).
FT BINDING 160 160 UDP-glucuronate (By similarity).
FT SITE 218 218 Interaction with galactose moiety of
FT substrate glycoprotein (By similarity).
FT SITE 310 310 Interaction with galactose moiety of
FT substrate glycoprotein (By similarity).
FT CARBOHYD 67 67 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 292 292 N-linked (GlcNAc...) (Potential).
FT STRAND 82 88
FT HELIX 94 105
FT STRAND 111 121
FT HELIX 124 132
FT STRAND 137 141
FT HELIX 157 170
FT STRAND 173 175
FT STRAND 180 183
FT HELIX 193 198
FT STRAND 202 206
FT STRAND 209 212
FT STRAND 215 223
FT STRAND 226 231
FT HELIX 244 246
FT STRAND 247 250
FT HELIX 251 256
FT STRAND 266 268
FT HELIX 269 271
FT HELIX 272 278
FT HELIX 283 285
FT HELIX 290 293
FT STRAND 313 315
SQ SEQUENCE 323 AA; 36919 MW; 85058D52D2D28463 CRC64;
MKSALFTRFF ILLPWILIVI IMLDVDTRRP VPPLTPRPYF SPYAVGRGGA RLPLRRGGPA
HGTQKRNQSR PQPQPEPQLP TIYAITPTYS RPVQKAELTR LANTFRQVAQ LHWILVEDAA
ARSELVSRFL ARAGLPSTHL HVPTPRRYKR PGLPRATEQR NAGLAWLRQR HQHQRAQPGV
LFFADDDNTY SLELFQEMRT TRKVSVWPVG LVGGRRYERP LVENGKVVGW YTGWRADRPF
AIDMAGFAVS LQVILSNPKA VFKRRGSQPG MQESDFLKQI TTVEELEPKA NNCTKVLVWH
TRTEKVNLAN EPKYHLDTVK IEV
//
MIM
607497
*RECORD*
*FIELD* NO
607497
*FIELD* TI
*607497 BETA-1,3-GLUCURONYLTRANSFERASE 2; B3GAT2
;;UDP-GLUCURONYLTRANSFERASE S;;
GLUCURONOSYLTRANSFERASE S; GLCATS;;
read moreKIAA1963
*FIELD* TX
DESCRIPTION
GLCATS is involved in the synthesis of the HNK1 (see 151290)
carbohydrate epitope. GLCATS transfers a glucuronic acid in beta-1,3
linkage to a terminal galactose of the Gal-beta-1,4-GlcNAc residue found
in different glycoproteins and glycolipids. The HNK1 epitope has a role
in cell-cell and cell-substratum interactions.
CLONING
By randomly sequencing clones derived from an adult hippocampus cDNA
library, Nagase et al. (2001) cloned GLCATS, which they designated
KIAA1963. The deduced protein contains 488 amino acids. RT-PCR ELISA
revealed moderate expression in adult and fetal brain and low levels in
adult testis and ovary. Within adult neural tissues, GLCATS was highly
expressed in spinal cord and hippocampus, with moderate to high
expression in all other adult brain regions tested.
Using homology with the rat Glcats sequence, Marcos et al. (2002)
identified human ESTs and genomic clones for GLCATS. The deduced
324-amino acid protein contains a transmembrane region, a proline-rich
domain, and a C-terminal catalytic domain, which contains 4 highly
conserved regions (motifs I to IV). GLCATS also has 2 putative
N-glycosylation sites. The human and rat proteins share 89% homology,
with the highest identity in the catalytic domain. Northern blot
analysis detected expression in trachea, but not in any other tissues
examined, including spinal cord. By PCR, the authors detected GLCATS
expression in retina.
Imiya et al. (2002) cloned mouse Glcats. The deduced 324-amino acid
protein has a type II membrane topology. Northern blot analysis detected
Glcats expression in brain, but not in liver or kidney.
GENE FUNCTION
Imiya et al. (2002) found that mouse Glcats, transfected and expressed
in COS-1 cells, exhibited glucuronyltransferase activity toward
glycoproteins.
GENE STRUCTURE
Marcos et al. (2002) determined that the GLCATS gene contains 4 exons
and spans approximately 85 kb.
Imiya et al. (2002) analyzed the proximal 5-prime flanking region of the
mouse Glcats gene. This region was characterized by a high GC content
and did not contain a canonical TATA box or a CCAAT box. Imiya et al.
(2002) identified binding sites for several response elements.
MAPPING
By genomic sequence analysis, Nagase et al. (2001) mapped the GLCATS
gene to chromosome 6. Marcos et al. (2002) mapped the GLCATS gene
between microsatellite markers within chromosome 6q13.
By FISH, Imiya et al. (2002) mapped the mouse Glcats gene to the A4-B
region of chromosome 1.
*FIELD* RF
1. Imiya, K.; Ishizaki, T.; Seiki, T.; Saito, F.; Inazawa, J.; Oka,
S.; Kawasaki, T.: cDNA cloning, genomic structure and chromosomal
mapping of the mouse glucuronyltransferase-S involved in the biosynthesis
of the HNK-1 carbohydrate epitope. Gene 296: 29-36, 2002.
2. Marcos, I.; Galan, J. J.; Borrego, S.; Antinolo, G.: Cloning,
characterization, and chromosome mapping of the human GlcAT-S gene. J.
Hum. Genet. 47: 677-680, 2002.
3. Nagase, T.; Kikuno, R.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. XXII. The complete sequences of 50 new
cDNA clones which code for large proteins. DNA Res. 8: 319-327,
2001.
*FIELD* CD
Patricia A. Hartz: 1/22/2003
*FIELD* ED
alopez: 07/24/2006
mgross: 10/10/2005
terry: 7/20/2004
mgross: 1/22/2003
*RECORD*
*FIELD* NO
607497
*FIELD* TI
*607497 BETA-1,3-GLUCURONYLTRANSFERASE 2; B3GAT2
;;UDP-GLUCURONYLTRANSFERASE S;;
GLUCURONOSYLTRANSFERASE S; GLCATS;;
read moreKIAA1963
*FIELD* TX
DESCRIPTION
GLCATS is involved in the synthesis of the HNK1 (see 151290)
carbohydrate epitope. GLCATS transfers a glucuronic acid in beta-1,3
linkage to a terminal galactose of the Gal-beta-1,4-GlcNAc residue found
in different glycoproteins and glycolipids. The HNK1 epitope has a role
in cell-cell and cell-substratum interactions.
CLONING
By randomly sequencing clones derived from an adult hippocampus cDNA
library, Nagase et al. (2001) cloned GLCATS, which they designated
KIAA1963. The deduced protein contains 488 amino acids. RT-PCR ELISA
revealed moderate expression in adult and fetal brain and low levels in
adult testis and ovary. Within adult neural tissues, GLCATS was highly
expressed in spinal cord and hippocampus, with moderate to high
expression in all other adult brain regions tested.
Using homology with the rat Glcats sequence, Marcos et al. (2002)
identified human ESTs and genomic clones for GLCATS. The deduced
324-amino acid protein contains a transmembrane region, a proline-rich
domain, and a C-terminal catalytic domain, which contains 4 highly
conserved regions (motifs I to IV). GLCATS also has 2 putative
N-glycosylation sites. The human and rat proteins share 89% homology,
with the highest identity in the catalytic domain. Northern blot
analysis detected expression in trachea, but not in any other tissues
examined, including spinal cord. By PCR, the authors detected GLCATS
expression in retina.
Imiya et al. (2002) cloned mouse Glcats. The deduced 324-amino acid
protein has a type II membrane topology. Northern blot analysis detected
Glcats expression in brain, but not in liver or kidney.
GENE FUNCTION
Imiya et al. (2002) found that mouse Glcats, transfected and expressed
in COS-1 cells, exhibited glucuronyltransferase activity toward
glycoproteins.
GENE STRUCTURE
Marcos et al. (2002) determined that the GLCATS gene contains 4 exons
and spans approximately 85 kb.
Imiya et al. (2002) analyzed the proximal 5-prime flanking region of the
mouse Glcats gene. This region was characterized by a high GC content
and did not contain a canonical TATA box or a CCAAT box. Imiya et al.
(2002) identified binding sites for several response elements.
MAPPING
By genomic sequence analysis, Nagase et al. (2001) mapped the GLCATS
gene to chromosome 6. Marcos et al. (2002) mapped the GLCATS gene
between microsatellite markers within chromosome 6q13.
By FISH, Imiya et al. (2002) mapped the mouse Glcats gene to the A4-B
region of chromosome 1.
*FIELD* RF
1. Imiya, K.; Ishizaki, T.; Seiki, T.; Saito, F.; Inazawa, J.; Oka,
S.; Kawasaki, T.: cDNA cloning, genomic structure and chromosomal
mapping of the mouse glucuronyltransferase-S involved in the biosynthesis
of the HNK-1 carbohydrate epitope. Gene 296: 29-36, 2002.
2. Marcos, I.; Galan, J. J.; Borrego, S.; Antinolo, G.: Cloning,
characterization, and chromosome mapping of the human GlcAT-S gene. J.
Hum. Genet. 47: 677-680, 2002.
3. Nagase, T.; Kikuno, R.; Ohara, O.: Prediction of the coding sequences
of unidentified human genes. XXII. The complete sequences of 50 new
cDNA clones which code for large proteins. DNA Res. 8: 319-327,
2001.
*FIELD* CD
Patricia A. Hartz: 1/22/2003
*FIELD* ED
alopez: 07/24/2006
mgross: 10/10/2005
terry: 7/20/2004
mgross: 1/22/2003