GMA12_SCHPO
ID GMA12_SCHPO Reviewed; 375 AA.
AC Q09174;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Alpha-1,2-galactosyltransferase;
DE EC=2.4.1.-;
GN Name=gma12; ORFNames=SPCC736.04c;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 35-42; 160-164;
RP 174-178 AND 361-373, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7522655; DOI=10.1091/mbc.5.5.519;
RA Chappell T.G., Hajibagheri M.A.N., Ayscough K., Pierce M., Warren G.;
RT "Localization of an alpha 1,2 galactosyltransferase activity to the Golgi
RT apparatus of Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 5:519-528(1994).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=9839953; DOI=10.1046/j.1432-1327.1998.2570630.x;
RA Yoko-o T., Roy S.K., Jigami Y.;
RT "Differences in in vivo acceptor specificity of two galactosyltransferases,
RT the gmh3+ and gma12+ gene products from Schizosaccharomyces pombe.";
RL Eur. J. Biochem. 257:630-637(1998).
CC -!- FUNCTION: Involved in the O- and N-linked oligosaccharide modification
CC of proteins transported through the Golgi stack. This occurs in cis
CC Golgi where the enzyme transfers galactose from UDP-galactose to a
CC variety of mannose based acceptors. {ECO:0000269|PubMed:7522655,
CC ECO:0000269|PubMed:9839953}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:7522655}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:7522655}.
CC -!- PTM: O-glycosylated.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 34 family.
CC {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; Z30917; CAA83200.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA19268.1; -; Genomic_DNA.
DR PIR; T41561; T41561.
DR RefSeq; NP_587775.1; NM_001022768.2.
DR AlphaFoldDB; Q09174; -.
DR BioGRID; 275673; 139.
DR STRING; 4896.SPCC736.04c.1; -.
DR CAZy; GT34; Glycosyltransferase Family 34.
DR SwissPalm; Q09174; -.
DR MaxQB; Q09174; -.
DR PaxDb; Q09174; -.
DR EnsemblFungi; SPCC736.04c.1; SPCC736.04c.1:pep; SPCC736.04c.
DR GeneID; 2539101; -.
DR KEGG; spo:SPCC736.04c; -.
DR PomBase; SPCC736.04c; gma12.
DR VEuPathDB; FungiDB:SPCC736.04c; -.
DR eggNOG; KOG4748; Eukaryota.
DR HOGENOM; CLU_045726_0_0_1; -.
DR InParanoid; Q09174; -.
DR OMA; WIWWLDH; -.
DR PhylomeDB; Q09174; -.
DR PRO; PR:Q09174; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IDA:PomBase.
DR GO; GO:0031228; C:intrinsic component of Golgi membrane; IDA:CACAO.
DR GO; GO:0140497; C:mannan polymerase II complex; ISO:PomBase.
DR GO; GO:0031278; F:alpha-1,2-galactosyltransferase activity; IDA:PomBase.
DR GO; GO:0006491; P:N-glycan processing; IMP:PomBase.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:PomBase.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:PomBase.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR008630; Glyco_trans_34.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR31306; PTHR31306; 2.
DR Pfam; PF05637; Glyco_transf_34; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..375
FT /note="Alpha-1,2-galactosyltransferase"
FT /id="PRO_0000215163"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..375
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CONFLICT 161
FT /note="W -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 42621 MW; 05ADA38C352B3B3C CRC64;
MRFAPYLISA VVITTIILGG AWWTSAMDTK LQTKMKEIID QHTSTWTPVV SSVTSTQTDT
LRVTISEVVS VTATLTETFT ATPTVTSVVH ALATTDPHPD NSKIVILMGS NFQNDANSPL
HPFAQSIIKN RREYAERHGY KFEFLDADAY ASRVTGHLMP WVKVPMLQDT MKKYPDAEWI
WWLDHDALVM NKDLNVVDHV LKHDRLNTIL TREAEYKSGA GIPADGFRTP KDQDAKDVHF
IISQDFNGIN AGSLFIRNSE VGRWIVDLWF EPLYLDHIQG YAEQQAFSHM VFYHPQVYKH
VGVVPLKAIN AYDFDDNIWG YDDGDLCIHF AGCNYFKNCP EKFLKYAQIL SSKQGSDWMS
AQEKDHIQNL LKPSS
