ID A0A0D2ETT0_9EURO Unreviewed; 483 AA.
AC A0A0D2ETT0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 05-FEB-2025, entry version 32.
DE RecName: Full=GPI mannosyltransferase 1 {ECO:0000256|ARBA:ARBA00013797, ECO:0000256|RuleBase:RU365064};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU365064};
DE AltName: Full=GPI mannosyltransferase I {ECO:0000256|RuleBase:RU365064};
GN ORFNames=PV05_09976 {ECO:0000313|EMBL:KIW51234.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW51234.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW51234.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW51234.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00025399,
CC ECO:0000256|RuleBase:RU365064}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687,
CC ECO:0000256|RuleBase:RU365064}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU365064}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU365064}.
CC -!- SIMILARITY: Belongs to the PIGM family. {ECO:0000256|ARBA:ARBA00011071,
CC ECO:0000256|RuleBase:RU365064}.
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DR EMBL; KN847322; KIW51234.1; -; Genomic_DNA.
DR RefSeq; XP_013311818.1; XM_013456364.1.
DR AlphaFoldDB; A0A0D2ETT0; -.
DR STRING; 348802.A0A0D2ETT0; -.
DR GeneID; 25331884; -.
DR HOGENOM; CLU_024220_1_0_1; -.
DR OrthoDB; 1741594at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IEA:TreeGrafter.
DR GO; GO:0051751; F:alpha-1,4-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR007704; PIG-M.
DR PANTHER; PTHR12886:SF0; GPI MANNOSYLTRANSFERASE 1; 1.
DR PANTHER; PTHR12886; PIG-M MANNOSYLTRANSFERASE; 1.
DR Pfam; PF05007; Mannosyl_trans; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365064};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU365064};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW ECO:0000256|RuleBase:RU365064};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365064};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365064};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU365064};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU365064}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 70..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 94..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 215..236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 286..305
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 317..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 384..408
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT REGION 416..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 53914 MW; FAA2417EA079EF2D CRC64;
MSSPNPSLFS SPTFIFLLAF VLRAVLLVYG IYQDSVSALK YTDIDYYVFT DAARAVSRGS
SPYTRATYRY TPLLAWILLP TSWGGLWFHF GKTIFALSDL IAGWLILILL KRRGLHEARA
LGYASVWLLN PMVANISTRG SSEGFLCVLV MALLWAFETR QILLSGVLLG LSVHFKIYPF
IYGASMLWAL GPATKTSPGT AIFQRTLQFM NRDRILLVAT SLITFTVLNI LMYNIYGSPF
LQHTFLHHLT RIDHRHNFSP YNTLLYLSSA QSTSHFTKSS SFSFESFAFV PQLLLSTVLI
PIALAKRDLP RTMLAQTLAF VAFNKVCTSQ YFLWYLVFLP LYLPDSALIR RPGLGTTALA
LWIIGQAAWL QQAYELEFLG KSTFVPGLFA TSLGFFVINC WILGVIVADE RDIANKGSPD
EASKQSAKSE RVLVMPPASE NGSTGFAIKG KEPVRRARAD SHIDTSNLAK VHLGPRDRVL
KSN
//
