ID A3M062_PICST Unreviewed; 313 AA.
AC A3M062;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PICST_33798 {ECO:0000313|EMBL:ABN68460.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN68460.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN68460.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the PIGC family.
CC {ECO:0000256|ARBA:ARBA00008321}.
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; CP000502; ABN68460.2; -; Genomic_DNA.
DR RefSeq; XP_001386489.2; XM_001386452.1.
DR AlphaFoldDB; A3M062; -.
DR STRING; 322104.A3M062; -.
DR GeneID; 4840808; -.
DR KEGG; pic:PICST_33798; -.
DR eggNOG; KOG3059; Eukaryota.
DR HOGENOM; CLU_024002_2_0_1; -.
DR InParanoid; A3M062; -.
DR OMA; STSYHAF; -.
DR OrthoDB; 205848at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002258; Chromosome 8.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR009450; Plno_GlcNAc_GPI2.
DR PANTHER; PTHR12982; PHOSPHATIDYLINOSITOL GLYCAN, CLASS C; 1.
DR PANTHER; PTHR12982:SF0; PHOSPHATIDYLINOSITOL N-ACETYLGLUCOSAMINYLTRANSFERASE SUBUNIT C; 1.
DR Pfam; PF06432; GPI2; 1.
DR PIRSF; PIRSF016104; GPI2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 63..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 313 AA; 36353 MW; BD2AF06D6764CB61 CRC64;
MPPHSYLLRR NTPIRRTPQV SWKKLLYLKQ PFPDNYTDQS FLSQLKRNTT VAKYSYIKLV
KDFSLIVFYI SVILVVVLMF TGIYLHQWSS MLPTMVTSAL SISGFIILKV FDKSYNTKVG
KIGYYSQRLN MKSFVLIIFI LLILSPVLKS LTKSTASDSI WALSFILCVC NTIFHDYSMN
SSSSDVSELQ YRPIISTNIS LSNSIVLASR LGSTSQVFFF VLFSIQVNIL LPLFDFNARR
AQFYRLHWTV YFIVFNFVNY LIILLLGTKF LFYWFVAVLG IVFLMPAYFL FLQRYKNELQ
GPWDTAKPII NTN
//
