PVG3_SCHPO
ID PVG3_SCHPO Reviewed; 378 AA.
AC Q9USX0;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Beta-1,3-galactosyltransferase pvg3;
DE EC=2.4.1.134;
DE AltName: Full=Meiotically up-regulated gene 49 protein;
DE AltName: Full=Pyruvylated Gal-beta-1,3-epitope synthesis protein 3;
DE Short=PvGal synthesis protein 3;
GN Name=pvg3; Synonyms=mug49; ORFNames=SPBC1921.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=15173185; DOI=10.1074/jbc.m403574200;
RA Andreishcheva E.N., Kunkel J.P., Gemmill T.R., Trimble R.B.;
RT "Five genes involved in biosynthesis of the pyruvylated Galbeta1,3-epitope
RT in Schizosaccharomyces pombe N-linked glycans.";
RL J. Biol. Chem. 279:35644-35655(2004).
RN [3]
RP FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Involved in cell wall biogenesis. Has a role in the addition
CC of Gal-beta1,3 moeities to galactomannans and their subsequent
CC pyruvylation. Has a role in meiosis. {ECO:0000269|PubMed:15173185,
CC ECO:0000269|PubMed:16303567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-
CC [protein] + UDP-alpha-D-galactose = 3-O-(beta-D-galactosyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:11780, Rhea:RHEA-COMP:12570, Rhea:RHEA-
CC COMP:12571, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:132088, ChEBI:CHEBI:132090; EC=2.4.1.134;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:16823372}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB58972.1; -; Genomic_DNA.
DR PIR; T39790; T39790.
DR RefSeq; NP_595999.1; NM_001021907.2.
DR AlphaFoldDB; Q9USX0; -.
DR BioGRID; 277345; 4.
DR STRING; 4896.SPBC1921.06c.1; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR MaxQB; Q9USX0; -.
DR PaxDb; Q9USX0; -.
DR EnsemblFungi; SPBC1921.06c.1; SPBC1921.06c.1:pep; SPBC1921.06c.
DR GeneID; 2540827; -.
DR KEGG; spo:SPBC1921.06c; -.
DR PomBase; SPBC1921.06c; pvg3.
DR VEuPathDB; FungiDB:SPBC1921.06c; -.
DR eggNOG; KOG2287; Eukaryota.
DR HOGENOM; CLU_731891_0_0_1; -.
DR InParanoid; Q9USX0; -.
DR OMA; FPYMCGF; -.
DR PhylomeDB; Q9USX0; -.
DR BioCyc; MetaCyc:MON-20447; -.
DR PRO; PR:Q9USX0; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047220; F:galactosylxylosylprotein 3-beta-galactosyltransferase activity; TAS:PomBase.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0051072; P:4,6-pyruvylated galactose residue biosynthetic process; IMP:PomBase.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 2.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Meiosis; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..378
FT /note="Beta-1,3-galactosyltransferase pvg3"
FT /id="PRO_0000076296"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..378
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 378 AA; 43834 MW; 9E621E5866407CA3 CRC64;
MFSNSKKKIF LYVLIAGVAT FSFAFLVLNR LQAEEHSLAY VENLFLDPFI KQNESLAHAN
DRPFKLYLGI FSQAKNVDRR NFLRTDYNEY IKEFAVNDTV DVRFILGLPE NEQELATIRE
EQRTYGDLAV LPIPENVDAG KSIVYFQTFL EGYQPFPLFS ELADNLIMPS TQFHGSFIYN
QSIKTYELPG MKEFQDLGEP KHDYDFIVKA DDDSFLNLPR LFEMLKEHVG KSRFYFGRDC
TRRELPTAVR DFPYMCGFFY IVSPDMAYEV AKRRNIIIPF EDAQTGYSIY LSGNVKNAEF
SKCTLYDLIL PNEGFNYRQS YLRIDAIAVH KLKSIPLLST VSNWFKKMYE HRANCSALIE
TERLSCLQAT IPLPSLDV
