ALG1_SCHPO
ID ALG1_SCHPO Reviewed; 424 AA.
AC O13933;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase;
DE EC=2.4.1.142;
DE AltName: Full=Asparagine-linked glycosylation protein 1;
DE AltName: Full=Beta-1,4-mannosyltransferase;
DE AltName: Full=GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase;
DE AltName: Full=GDP-mannose-dolichol diphosphochitobiose mannosyltransferase;
GN Name=alg1; ORFNames=SPAC23C4.14;
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: Participates in the formation of the lipid-linked precursor
CC oligosaccharide for N-glycosylation. Involved in assembling the
CC dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic
CC surface of the ER (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl
CC diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:13865,
CC Rhea:RHEA-COMP:9520, Rhea:RHEA-COMP:11044, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472; EC=2.4.1.142;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 33 subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB16885.2; -; Genomic_DNA.
DR PIR; T38269; T38269.
DR RefSeq; NP_593186.1; NM_001018582.2.
DR AlphaFoldDB; O13933; -.
DR SMR; O13933; -.
DR STRING; 4896.SPAC23C4.14.1; -.
DR CAZy; GT33; Glycosyltransferase Family 33.
DR MaxQB; O13933; -.
DR PaxDb; O13933; -.
DR EnsemblFungi; SPAC23C4.14.1; SPAC23C4.14.1:pep; SPAC23C4.14.
DR GeneID; 2541937; -.
DR KEGG; spo:SPAC23C4.14; -.
DR PomBase; SPAC23C4.14; alg1.
DR VEuPathDB; FungiDB:SPAC23C4.14; -.
DR eggNOG; KOG2941; Eukaryota.
DR HOGENOM; CLU_012079_0_0_1; -.
DR InParanoid; O13933; -.
DR OMA; PLKVLWQ; -.
DR PhylomeDB; O13933; -.
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:O13933; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004578; F:chitobiosyldiphosphodolichol beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IC:PomBase.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR InterPro; IPR026051; ALG1-like.
DR PANTHER; PTHR13036; PTHR13036; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..424
FT /note="Chitobiosyldiphosphodolichol beta-
FT mannosyltransferase"
FT /id="PRO_0000080257"
FT TRANSMEM 1..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..424
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 424 AA; 48726 MW; E652399C61A28579 CRC64;
MLVLKIVLFL SLVIWFNLKK RTDKKRIIVL VLGDIARSPR MQYHAVSFAK LGWKVDLLGY
QHPGSSVGLF ESHENIRFYP IPSLPAYLQP KNRLQFLFLG PLKVLHQFLA LNWALFVRKP
ASFLFIQNPP CIPVFFIAQC LHILRGTKFI IDWHNFGYSI LALKLGKQHT FVKLLKIYEK
YMARGAYAHL TVSKRMKDVL QTWGMNPCYV CYDRPPNHFT PIKNEQKKQM SIKKIPCEYN
PSSTKLLITS TSWTPDEDIY ILWEALNEYD KTLDTPKLLV LITGKGPMKE EFSQYIKKHP
LHKVRFCMPW LSIEDYPQVM ACADLGVCLH TSSSGLDLPM KVVDLFGCGV PVIALSYPTI
SELVHDGENG LIVNDSKALS KKMQYLLTHA NELNSLKLGA LKESEYRWDD EWNKVIPPIV
QGSN
