ALG3_SCHPO
ID ALG3_SCHPO Reviewed; 406 AA.
AC Q9Y7I4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase;
DE EC=2.4.1.258;
DE AltName: Full=Asparagine-linked glycosylation protein 3;
DE AltName: Full=Dol-P-Man-dependent alpha(1-3)-mannosyltransferase;
DE AltName: Full=Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase;
DE AltName: Full=Dolichyl-phosphate-mannose--glycolipid alpha-mannosyltransferase;
GN Name=alg3; ORFNames=SPAC7D4.06c;
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).
CC -!- FUNCTION: Adds the first Dol-P-Man derived mannose in an alpha-1,3
CC linkage to Man(5)GlcNAc(2)-PP-Dol. {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->6)]-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a
CC dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+);
CC Xref=Rhea:RHEA:29527, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:12627, Rhea:RHEA-COMP:12628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132515,
CC ChEBI:CHEBI:132516; EC=2.4.1.258;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 58 family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB16723.2; -; Genomic_DNA.
DR PIR; T39084; T39084.
DR RefSeq; NP_593853.1; NM_001019282.2.
DR AlphaFoldDB; Q9Y7I4; -.
DR BioGRID; 279218; 1.
DR STRING; 4896.SPAC7D4.06c.1; -.
DR CAZy; GT58; Glycosyltransferase Family 58.
DR PaxDb; Q9Y7I4; -.
DR EnsemblFungi; SPAC7D4.06c.1; SPAC7D4.06c.1:pep; SPAC7D4.06c.
DR GeneID; 2542768; -.
DR KEGG; spo:SPAC7D4.06c; -.
DR PomBase; SPAC7D4.06c; alg3.
DR VEuPathDB; FungiDB:SPAC7D4.06c; -.
DR eggNOG; KOG2762; Eukaryota.
DR HOGENOM; CLU_035382_3_0_1; -.
DR InParanoid; Q9Y7I4; -.
DR OMA; PERYGIH; -.
DR PhylomeDB; Q9Y7I4; -.
DR BRENDA; 2.4.1.258; 5613.
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:Q9Y7I4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IC:PomBase.
DR GO; GO:0052925; F:dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity; IMP:PomBase.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:PomBase.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:PomBase.
DR InterPro; IPR007873; Glycosyltransferase_ALG3.
DR PANTHER; PTHR12646; PTHR12646; 1.
DR Pfam; PF05208; ALG3; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..406
FT /note="Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-
FT mannosyltransferase"
FT /id="PRO_0000327764"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 406 AA; 46992 MW; 039E40A16A9359C8 CRC64;
MSSVETRNSF NPFRVLFDLG SYGWLHPSRL LLLEIPFVFA IISKVPYTEI DWIAYMEQVN
SFLLGERDYK SLVGCTGPLV YPGGHVFLYT LLYYLTDGGT NIVRAQYIFA FVYWITTAIV
GYLFKIVRAP FYIYVLLILS KRLHSIFILR LFNDGFNSLF SSLFILSSCK KKWVRASILL
SVACSVKMSS LLYVPAYLVL LLQILGPKKT WMHIFVIIIV QILFSIPFLA YFWSYWTQAF
DFGRAFDYKW TVNWRFIPRS IFESTSFSTS ILFLHVALLV AFTCKHWNKL SRATPFAMVN
SMLTLKPLPK LQLATPNFIF TALATSNLIG ILCARSLHYQ FYAWFAWYSP YLCYQASFPA
PIVIGLWMLQ EYAWNVFPST KLSSLIAVCV PLITILKLYT SDYRKP
