ID A0A0V1LJN5_9BILA Unreviewed; 680 AA.
AC A0A0V1LJN5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 Name=Pigm {ECO:0000313|EMBL:KRZ59753.1};
GN ORFNames=T02_13007 {ECO:0000313|EMBL:KRZ59753.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ59753.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ59753.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ59753.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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. {ECO:0000256|ARBA:ARBA00025668,
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: Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004274}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004274}. 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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGM family. {ECO:0000256|ARBA:ARBA00011071,
CC ECO:0000256|RuleBase:RU365064}.
CC -!- SIMILARITY: Belongs to the sarcoglycan beta/delta/gamma/zeta family.
CC {ECO:0000256|ARBA:ARBA00007574}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ59753.1}.
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DR EMBL; JYDW01000038; KRZ59753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LJN5; -.
DR STRING; 6335.A0A0V1LJN5; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016012; C:sarcoglycan complex; IEA:InterPro.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
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 InterPro; IPR006875; Sarcoglycan.
DR PANTHER; PTHR12886:SF0; GPI MANNOSYLTRANSFERASE 1; 1.
DR PANTHER; PTHR12886; PIG-M MANNOSYLTRANSFERASE; 1.
DR Pfam; PF05007; Mannosyl_trans; 1.
DR Pfam; PF04790; Sarcoglycan_1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365064};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU365064,
KW ECO:0000313|EMBL:KRZ59753.1};
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:UP000054721};
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 49..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 392..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 418..437
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 443..467
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 488..513
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 554..575
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 582..609
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
FT TRANSMEM 653..672
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365064"
SQ SEQUENCE 680 AA; 76467 MW; D08D02CC48F8A5D5 CRC64;
MANLSHDYAS NSLGCRFGDK LTTYNHGSSK MTDSTIYRIG IYGWRKRCLY AMILLLIVLI
VANITVTFWI MSIMGFTLDG IGGMRISKAK IEVTGEAEFV NAVYLQRLSS ASKVPMFIES
DRAVLLTARD KTGNISSRLV LKDNQIQAIC DRFEVVNRDG KAVFSATENE VAVRVENLRI
ISEGGSVFDG SIQTSVIRPE ADMPLLLESP TRGMEVRVAQ DIEILSRAGD VKAEALHNIV
FQSANGEIVL SSPNIYVDRL MRGTEKGHMQ YQVCLCENGR LFLAHNGVDC RASSDLSCYS
VQNASYSKQD YFFDVKFTDV DYTVMLDAAK LMARGQSPYE RQTYRYTPTF AWLLLPAVRW
PLYGKLLFNA FDLLAGLTST VLALSSDFGH SSLGPLLALA LFNPFTMIIS SRGNAESFVS
FLVLFSLLLV EIGGLPARLC ASLFHGFCVH VKIYPIIYLP SACFKLYQEK LHQKDDDHVA
SRPVRFARAL GAAAGYAFGV LVGFVAPTAL AYYKYGRQYA DEALLYHLRR TDYKHNFSPF
FLPLYLNADS STNIIAWISY AAFVPQALIV LFLALKFARQ LPICWFISTL AFVAHNKVCT
SQYFVWYLAF LPTVWSGFDC DRGRPVRLLL WWTAGQALWL LPAYCLEFRG FNFFLPVWIA
SVLFFLINVH IIRRAIVSFR
//
