(data stored in SCRATCH zone)

SWISSPROT: C5DCB8_LACTC

ID   C5DCB8_LACTC            Unreviewed;       394 AA.
AC   C5DCB8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 47.
DE   RecName: Full=GPI mannosyltransferase 1 {ECO:0000256|RuleBase:RU365064};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU365064};
DE   AltName: Full=GPI mannosyltransferase I {ECO:0000256|RuleBase:RU365064};
GN   OrderedLocusNames=KLTH0B01760g {ECO:0000313|EMBL:CAR21429.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21429.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21429.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-
CC       acyl-PI during GPI precursor assembly. Required for cell wall
CC       integrity. {ECO:0000256|RuleBase:RU365064}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|RuleBase:RU365064}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU365064}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU365064}.
CC   -!- SIMILARITY: Belongs to the PIGM family.
CC       {ECO:0000256|RuleBase:RU365064}.
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DR   EMBL; CU928166; CAR21429.1; -; Genomic_DNA.
DR   RefSeq; XP_002551867.1; XM_002551821.1.
DR   STRING; 381046.XP_002551867.1; -.
DR   EnsemblFungi; CAR21429; CAR21429; KLTH0B01760g.
DR   GeneID; 8290695; -.
DR   KEGG; lth:KLTH0B01760g; -.
DR   HOGENOM; HOG000186884; -.
DR   InParanoid; C5DCB8; -.
DR   KO; K05284; -.
DR   OMA; IQIISHY; -.
DR   OrthoDB; 1003258at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000002036; Chromosome B.
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:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniRule.
DR   InterPro; IPR007704; PIG-M.
DR   PANTHER; PTHR12886; PTHR12886; 1.
DR   Pfam; PF05007; Mannosyl_trans; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DCB8.
DR   SWISS-2DPAGE; C5DCB8.
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU365064};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU365064};
KW   GPI-anchor biosynthesis {ECO:0000256|RuleBase:RU365064};
KW   Membrane {ECO:0000256|RuleBase:RU365064};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Transferase {ECO:0000256|RuleBase:RU365064};
KW   Transmembrane {ECO:0000256|RuleBase:RU365064};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU365064}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        76..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        152..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        188..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        253..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        305..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        330..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365064"
SQ   SEQUENCE   394 AA;  45876 MW;  E1151031146FB09F CRC64;
     MDTATVSLFL GALALRLGFF FYGIYQDKYF EVKYTDVDYF VFNDAASYVF HGLSPYLRDT
     YRYTPLLSWL LVPNHYLQWI HFGKMMFVLF DLLTGLLILN LLEAQSKRKK LILSSLWLLN
     FMVITISTRG NAESVLCFLI LLSLYFLKAR QFVLSGLFLG FAIHFKIYPI IYSIPIAVYV
     YRQRQGGLFN VFKVGVSAIL ALAGTSYWMY QIYGMEFLDN AYFYHLSRTD HRHNFSVFHM
     LLYFESALPT DSFWAKLAFL PQAAITLGVV PLLLRDPSFN SLLSLLFIQT FAFVTYNKVC
     TSQYFIWYLI FLPFYLARTS ITLKKGLTMA LIWVGTQGAW LFFGYLLEFK GKNVFYPGLF
     LASLSFFLGN VWILGQFIDD FKVKTELSEE KKKR
//

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