OCH1_SCHPO
ID OCH1_SCHPO Reviewed; 396 AA.
AC Q9UTR6;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Initiation-specific alpha-1,6-mannosyltransferase;
DE EC=2.4.1.232 {ECO:0000269|PubMed:11231017};
GN Name=och1 {ECO:0000303|PubMed:11231017};
GN ORFNames=SPAC1006.05c {ECO:0000312|PomBase:SPAC1006.05c};
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], CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11231017; DOI=10.1016/s0014-5793(01)02082-8;
RA Yoko-o T., Tsukahara K., Watanabe T., Hata-Sugi N., Yoshimatsu K.,
RA Nagasu T., Jigami Y.;
RT "Schizosaccharomyces pombe och1(+) encodes alpha-1,6-mannosyltransferase
RT that is involved in outer chain elongation of N-linked oligosaccharides.";
RL FEBS Lett. 489:75-80(2001).
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=12784644; DOI=10.1271/bbb.67.927;
RA Yamamoto K., Okamoto M., Yoko-o T., Jigami Y.;
RT "Salt stress induces the expression of Schizosaccharomyces pombe och1+,
RT which encodes an initiation-specific alpha-1,6-mannosyltransferase for N-
RT linked outer chain synthesis of cell wall mannoproteins.";
RL Biosci. Biotechnol. Biochem. 67:927-929(2003).
CC -!- FUNCTION: Mannosyltransferase involved in outer chain elongation of
CC asparagine-linked oligosaccharides of the type Man(9)GlcNAc(2). May
CC otherwise add the first alpha-1,6-mannose to the Man(8)GlcNAc(2) core
CC oligosaccharide from the ER. Represents the first enzymatic event
CC required for synthesis of outer chain mannose linkages on yeast
CC secretory proteins. {ECO:0000269|PubMed:11231017,
CC ECO:0000269|PubMed:12784644}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers an alpha-D-mannosyl residue from GDP-mannose into
CC lipid-linked oligosaccharide, forming an alpha-(1->6)-D-mannosyl-D-
CC mannose linkage.; EC=2.4.1.232;
CC Evidence={ECO:0000269|PubMed:11231017};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P31755};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P31755}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P31755}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P31755}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P31755}. Note=Is recycled between the trans-
CC Golgi network and a late compartment of the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:P31755}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:P31755}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAD24818.1; -; Genomic_DNA.
DR PIR; T50453; T50453.
DR RefSeq; NP_594852.1; NM_001020281.2.
DR AlphaFoldDB; Q9UTR6; -.
DR BioGRID; 279579; 5.
DR STRING; 4896.SPAC1006.05c.1; -.
DR CAZy; GT32; Glycosyltransferase Family 32.
DR MaxQB; Q9UTR6; -.
DR PaxDb; Q9UTR6; -.
DR PRIDE; Q9UTR6; -.
DR EnsemblFungi; SPAC1006.05c.1; SPAC1006.05c.1:pep; SPAC1006.05c.
DR GeneID; 2543147; -.
DR KEGG; spo:SPAC1006.05c; -.
DR PomBase; SPAC1006.05c; och1.
DR VEuPathDB; FungiDB:SPAC1006.05c; -.
DR eggNOG; ENOG502QW2I; Eukaryota.
DR HOGENOM; CLU_022381_5_0_1; -.
DR InParanoid; Q9UTR6; -.
DR OMA; HINNWIP; -.
DR PhylomeDB; Q9UTR6; -.
DR BRENDA; 2.4.1.232; 5613.
DR PRO; PR:Q9UTR6; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR GO; GO:0000136; C:mannan polymerase complex; IBA:GO_Central.
DR GO; GO:0140497; C:mannan polymerase II complex; ISO:PomBase.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0033164; F:glycolipid 1,6-alpha-mannosyltransferase activity; IDA:PomBase.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP:PomBase.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IMP:PomBase.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:PomBase.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:PomBase.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039367; Och1-like.
DR PANTHER; PTHR31834; PTHR31834; 1.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..396
FT /note="Initiation-specific alpha-1,6-mannosyltransferase"
FT /id="PRO_0000080562"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P31755"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..396
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P31755"
FT MOTIF 229..231
FT /note="DXD motif"
FT /evidence="ECO:0000250|UniProtKB:P31755"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 396 AA; 45930 MW; 824B8932495642F1 CRC64;
MLRLRLRSIV IGAAIAGSIL LLFNHGSIEG MEDLTEISML EDYTPEAANK DYVGQQEEEE
LLYDQPSYIE EEEDPDLEAY LSDLEREELE HSLEELDEEN NYKLHLRYSF SQLQDFDEEN
EAVHMIVPKD TYEFEVPYHA DIPKLIWQTS KDPFDREVMK YTRFWRINHP SYSHAVLDDE
QSKALVISSF GDSSVSKISQ AYAMMPLPVL KADFFRYLVL LAKGGIYSDI DTAPLKHINN
WIPREYRKRN IRLIVGIEAD PDRPDWNDYY ARRVQFCQWT IAAAPGHPIL WELVRRITDE
TWKLHDSKKL SKNGESVMEW TGPGIWTDAI MDYLNWQYGP FSVENITNLE EPYLVGDVLI
LPITAFSPGV GHMGSKSPND PMAYVQHFFA GSWKDD
