ALG11_SCHPO
ID ALG11_SCHPO Reviewed; 471 AA.
AC O74878;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase;
DE EC=2.4.1.131;
DE AltName: Full=Alpha-1,2-mannosyltransferase alg11;
DE AltName: Full=Asparagine-linked glycosylation protein 11;
DE AltName: Full=Galactomannan deficiency protein 3;
DE AltName: Full=Glycolipid 2-alpha-mannosyltransferase;
GN Name=alg11; Synonyms=gmd3; ORFNames=SPCC330.08;
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], AND FUNCTION.
RX PubMed=11015724;
RX DOI=10.1002/1097-0061(200010)16:14<1261::aid-yea620>3.0.co;2-9;
RA Umeda K., Yoko-o T., Nakayama K., Suzuki T.-O., Jigami Y.;
RT "Schizosaccharomyces pombe gmd3(+)/alg11(+) is a functional homologue of
RT Saccharomyces cerevisiae ALG11 which is involved in N-linked
RT oligosaccharide synthesis.";
RL Yeast 16:1261-1271(2000).
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).
CC -!- FUNCTION: Required for N-linked oligosaccharide assembly. Has a role in
CC the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core
CC oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
CC {ECO:0000269|PubMed:11015724}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=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 + 2 GDP-alpha-
CC D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523,
CC Rhea:RHEA-COMP:12626, Rhea:RHEA-COMP:12627, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511,
CC ChEBI:CHEBI:132515; EC=2.4.1.131;
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 4 subfamily. {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; CU329672; CAA20913.1; -; Genomic_DNA.
DR PIR; T41318; T41318.
DR RefSeq; NP_587708.1; NM_001022703.2.
DR AlphaFoldDB; O74878; -.
DR SMR; O74878; -.
DR BioGRID; 275627; 1.
DR STRING; 4896.SPCC330.08.1; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; O74878; -.
DR MaxQB; O74878; -.
DR PaxDb; O74878; -.
DR PRIDE; O74878; -.
DR EnsemblFungi; SPCC330.08.1; SPCC330.08.1:pep; SPCC330.08.
DR GeneID; 2539054; -.
DR KEGG; spo:SPCC330.08; -.
DR PomBase; SPCC330.08; alg11.
DR VEuPathDB; FungiDB:SPCC330.08; -.
DR eggNOG; KOG1387; Eukaryota.
DR HOGENOM; CLU_017896_1_1_1; -.
DR InParanoid; O74878; -.
DR OMA; RFNIHLH; -.
DR PhylomeDB; O74878; -.
DR BRENDA; 2.4.1.131; 5613.
DR UniPathway; UPA00378; -.
DR PRO; PR:O74878; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IGI:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; ISO:PomBase.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:PomBase.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd03806; GT4_ALG11-like; 1.
DR InterPro; IPR038013; ALG11.
DR InterPro; IPR031814; ALG11_N.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR45919; PTHR45919; 1.
DR Pfam; PF15924; ALG11_N; 1.
DR Pfam; PF00534; Glycos_transf_1; 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..471
FT /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-
FT mannosyltransferase"
FT /id="PRO_0000080278"
FT TRANSMEM 1..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..471
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 471 AA; 53278 MW; 80D30A980D789366 CRC64;
MITTLAIALF IAVVAIHSHI RRKICKEIGI RLIKKIAPVK ASLYKQVGVE PKLARTVGFF
HPYCNAGGGG ERVLWTAVKS VQTEFPNVIS VVYTGDNVSK AEILRRVKNT FEIDLDSSKI
VFVYLKLRFL VSATTWHRFT LLGQSLGSMI LGFEAIYRFA PDIFIDTMGY AFTFCVVKSF
QNIPVGAYVH YPTISTDMLK SLKQVSLLAK VKMAYWRWFA QLYSDAGSHA DYVMTNSSWT
RNHIASLWGK DIQLSVVFPP CNTSELEKID INRKREPTLL YLAQYRPEKN HENVLRSFAL
YFEQHPDSPA KLLLVGSVRG EEDMCFVNHL KTLATELNLQ SKVKFVVDAP WPKVVEYLGT
CSIGVNYMWN EHFGIGVVEY MAAGLIPVVN NSGGPKFDIV IPWIGKPTGF HASTISEYAE
AYHKALTLSP QEQLEMRINA RSACARFGEH VFMRDFGNVF AKLLREDYSR T
