ALG12_SCHPO
ID ALG12_SCHPO Reviewed; 546 AA.
AC Q9USD4; O74753;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase;
DE EC=2.4.1.260;
DE AltName: Full=Asparagine-linked glycosylation protein 12 homolog;
DE AltName: Full=Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase;
DE AltName: Full=Mannosyltransferase ALG12 homolog;
GN Name=alg12; ORFNames=SPBC1734.12c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 115-311, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
CC -!- FUNCTION: Adds the eighth mannose residue in an alpha-1,6 linkage onto
CC the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2))
CC required for protein glycosylation. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate +
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29535, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12629, Rhea:RHEA-COMP:12630,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:132517, ChEBI:CHEBI:132519; EC=2.4.1.260;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:10759889}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:10759889}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA21306.2; -; Genomic_DNA.
DR EMBL; AB027846; BAA87150.1; -; Genomic_DNA.
DR PIR; T39659; T39659.
DR RefSeq; NP_595429.2; NM_001021337.2.
DR AlphaFoldDB; Q9USD4; -.
DR BioGRID; 276606; 41.
DR STRING; 4896.SPBC1734.12c.1; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR MaxQB; Q9USD4; -.
DR PaxDb; Q9USD4; -.
DR EnsemblFungi; SPBC1734.12c.1; SPBC1734.12c.1:pep; SPBC1734.12c.
DR GeneID; 2540068; -.
DR KEGG; spo:SPBC1734.12c; -.
DR PomBase; SPBC1734.12c; alg12.
DR VEuPathDB; FungiDB:SPBC1734.12c; -.
DR eggNOG; KOG2516; Eukaryota.
DR HOGENOM; CLU_008917_0_0_1; -.
DR InParanoid; Q9USD4; -.
DR PhylomeDB; Q9USD4; -.
DR Reactome; R-SPO-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9USD4; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:InterPro.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0052917; F:dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase; ISO:PomBase.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR039485; ALG12.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR PANTHER; PTHR22760:SF1; PTHR22760:SF1; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..546
FT /note="Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-
FT mannosyltransferase"
FT /id="PRO_0000215785"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 546 AA; 62880 MW; 8F4F1C76B2BD7DA1 CRC64;
MTSKESICWY LANILLVTCI GYYSYKTPFT KVEESFAMQA IHDIQTYRWD LSKYDHLEFP
GAVKRSFIPS LFIAVLSYIP SWFVNPLLAA RWTIGYLSWE SMNSVSCSIS KRFGTLSGAL
FILFSCAQFH LVYYMSRPLS NIFGLIATNH SLSLLLKNNY YGSISILVFA AAIVRSEIAL
LLMCLILPLL LQRRITLSKL LLVGISSSLA AVGASFLIDS YFWGAWCWPE LEAFLFNVVE
GKSSDWGTSP FYYYFVRLPW LFLNPTTLLF LLISFVYIKP ARLLIYVPLF FIFVYSFLGH
KEWRFIIYSI PWFNAASAIG ASLCFNASKF GKKIFEILRL MFFSGIIFGF IGSSFLLYVF
QYAYPGGLAL TRLYEIENHP QVSVHMDVYP CMTGITRFSQ LPSWYYDKTE DPKMLSNSLF
ISQFDYLITE DPESYNDTFD VIESVNSNTK IPILPKWLSN HIPREISIRN PAQPVYILAN
KKARATKPAA VDDYSSFIGH KVDEIKLWPP IYRVVSPDTL LTRDYREDRL NFFIDKDRIL
THITQG
