SMP3_YEAST
ID SMP3_YEAST Reviewed; 516 AA.
AC Q04174; D6W2K6; Q99400;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=GPI mannosyltransferase 4;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase IV;
DE Short=GPI-MT-IV;
GN Name=SMP3; Synonyms=LAS2, SAP2; OrderedLocusNames=YOR149C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBW5;
RX PubMed=2005867; DOI=10.1007/bf00269857;
RA Irie K., Araki H., Oshima Y.;
RT "Mutations in a Saccharomyces cerevisiae host showing increased holding
RT stability of the heterologous plasmid pSR1.";
RL Mol. Gen. Genet. 225:257-265(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1678;
RX PubMed=9046089;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<73::aid-yea52>3.0.co;2-m;
RA Bordonne R., Camasses A., Madania A., Poch O., Tarassov I.A., Winsor B.,
RA Martin R.P.;
RT "Analysis of a 35.6 kb region on the right arm of Saccharomyces cerevisiae
RT chromosome XV.";
RL Yeast 13:73-83(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 122-123.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION.
RX PubMed=11356840; DOI=10.1074/jbc.m101986200;
RA Grimme S.J., Westfall B.A., Wiedman J.M., Taron C.H., Orlean P.;
RT "The essential Smp3 protein is required for addition of the side-branching
RT fourth mannose during assembly of yeast glycosylphosphatidylinositols.";
RL J. Biol. Chem. 276:27731-27739(2001).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Alpha-1,2-mannosyltransferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth
CC mannose to trimannosyl-GPIs during GPI precursor assembly. The presence
CC of a fourth mannose in GPI is essential in fungi. Involved in plasmid
CC maintenance with SMP2. {ECO:0000269|PubMed:11356840}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGZ
CC subfamily. {ECO:0000305}.
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DR EMBL; X58121; CAA41123.1; -; Genomic_DNA.
DR EMBL; U55020; AAC49635.1; -; Genomic_DNA.
DR EMBL; Z75057; CAA99355.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10922.2; -; Genomic_DNA.
DR PIR; S67037; S67037.
DR RefSeq; NP_014792.4; NM_001183568.4.
DR AlphaFoldDB; Q04174; -.
DR BioGRID; 34545; 329.
DR STRING; 4932.YOR149C; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR PaxDb; Q04174; -.
DR PRIDE; Q04174; -.
DR EnsemblFungi; YOR149C_mRNA; YOR149C; YOR149C.
DR GeneID; 854320; -.
DR KEGG; sce:YOR149C; -.
DR SGD; S000005675; SMP3.
DR VEuPathDB; FungiDB:YOR149C; -.
DR eggNOG; KOG4123; Eukaryota.
DR GeneTree; ENSGT00950000183090; -.
DR HOGENOM; CLU_022957_2_0_1; -.
DR InParanoid; Q04174; -.
DR OMA; GIMHQNG; -.
DR BioCyc; YEAST:YOR149C-MON; -.
DR Reactome; R-SCE-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:Q04174; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q04174; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
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:0000026; F:alpha-1,2-mannosyltransferase activity; IMP:SGD.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:SGD.
DR GO; GO:0006276; P:plasmid maintenance; IMP:SGD.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..516
FT /note="GPI mannosyltransferase 4"
FT /id="PRO_0000071977"
FT TOPO_DOM 1..5
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..175
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..270
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..516
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 122..123
FT /note="IK -> MQ (in Ref. 2; AAC49635 and 3; CAA99355)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="E -> G (in Ref. 1; CAA41123)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="S -> R (in Ref. 1; CAA41123)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="V -> L (in Ref. 1; CAA41123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 59883 MW; AB5AFCAA086807D1 CRC64;
MMRYQWWLYL VYAIGLMLCL GPSYIHPDEH FQCIEILAMQ FMKVKGTIPW EFKSKFAARS
YGPLLLVYGP LFTILESFPE IQDNPALILY SMRLQNYVMY LLCYHFLIPK LIRDERKAVQ
FIKKSLLLTS YVTWTYQTHT FSNSIETLAL ISTLTVMEDM VNEKNIQRSN FKNSVILGLI
FSFGVFNRVT FPAFIFLPCL ILFWKFYRVH WKSFSLLLLS FSFSSCLFVL IDTNIYNNGK
GFVITPLNNL KYNLNVQNLQ VHGLHPRYTH LLVNLPQIVG PVLLLAIFSG YKLDKLSTYA
IISGLLFLSF FQHQELRFLV PLVPLLVTNL NWTPLSSTLV NKKIFKGTWL LFNIIMAFIM
GISHQAGIIQ FLGDYFHFRT EQMGVHIWWK TYSPPTWMYM SNNLTVSSLI NTQDGIESID
EVAFSVGNHH VIDLKGCDLP LLTETIRRLR LNGSITPLTL VTPNSMTSEL KKLKRDGTIN
LIPKRNYLFH LDLDHLDFND FTTFKPGLTV YSIELL
