ID A0A2Y9JT23_ENHLU Unreviewed; 416 AA.
AC A0A2Y9JT23;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit C isoform X1 {ECO:0000313|RefSeq:XP_022363841.1};
GN Name=LOC111150647 {ECO:0000313|RefSeq:XP_022363841.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022363841.1};
RN [1] {ECO:0000313|RefSeq:XP_022363841.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022363841.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR RefSeq; XP_022363841.1; XM_022508133.1.
DR AlphaFoldDB; A0A2Y9JT23; -.
DR STRING; 391180.A0A2Y9JT23; -.
DR KEGG; elk:111150647; -.
DR OrthoDB; 205848at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|RefSeq:XP_022363841.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Transferase {ECO:0000313|RefSeq:XP_022363841.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 167..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 46794 MW; BAC377CBA6A363EE CRC64;
MGKEAATALR EPRSPGKCGR VGPGREPVFP GRSVLRRPPR APGCFHRFTV LLFLGTWFRE
RAHLLEAWPG LLPLKLGTTS ATARHGISRK VLFRNFVENK SHLDSCERGC TGLCLRERIM
CAQPVTNAKE AKWQKVLYER QPFPDNYVDR RFLEELRKNI YARKYQYWAV VFESSVVVQQ
LCSVCVFVVI WWYLDEGLLA PQWLFGTGLA SSLIGYVLFD LLDGGEGRKK SGRTRWADLK
SALVFVTFTY GFSPVLKTLT ESVSTDTIYA MSVFMLLGHL IFFDYGANAA IVSSTLSLNM
AIFASVCLAS RLPRSLHAFI MVTFAIQIFA LWPMLQKKLK ACTPRSYVGV TLLFAFSALG
GLLSISAVGA ILFALLLVSI SCLCPFYLIR LQLFKENIHG PWDEAEIKED LSRFLS
//
