PIGC_DICDI
ID PIGC_DICDI Reviewed; 345 AA.
AC Q54M40;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Putative phosphatidylinositol N-acetylglucosaminyltransferase subunit C;
DE EC=2.4.1.198;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class C protein;
DE Short=PIG-C;
GN Name=pigC; ORFNames=DDB_G0286221;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Part of the complex catalyzing the transfer of N-
CC acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol,
CC the first step of GPI biosynthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + UDP-N-
CC acetyl-alpha-D-glucosamine = a 6-(N-acetyl-alpha-D-glucosaminyl)-1-
CC phosphatidyl-1D-myo-inositol + H(+) + UDP; Xref=Rhea:RHEA:14789,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57265, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58223; EC=2.4.1.198;
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Component of the phosphatidylinositol N-
CC acetylglucosaminyltransferase complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGC family. {ECO:0000305}.
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DR EMBL; AAFI02000085; EAL64286.1; -; Genomic_DNA.
DR RefSeq; XP_637791.1; XM_632699.1.
DR AlphaFoldDB; Q54M40; -.
DR STRING; 44689.DDB0233342; -.
DR PaxDb; Q54M40; -.
DR EnsemblProtists; EAL64286; EAL64286; DDB_G0286221.
DR GeneID; 8625505; -.
DR KEGG; ddi:DDB_G0286221; -.
DR dictyBase; DDB_G0286221; pigC.
DR eggNOG; KOG3059; Eukaryota.
DR HOGENOM; CLU_024002_2_0_1; -.
DR InParanoid; Q54M40; -.
DR OMA; HAFVMVT; -.
DR PhylomeDB; Q54M40; -.
DR Reactome; R-DDI-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:Q54M40; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR009450; Plno_GlcNAc_GPI2.
DR PANTHER; PTHR12982; PTHR12982; 1.
DR Pfam; PF06432; GPI2; 1.
DR PIRSF; PIRSF016104; GPI2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; GPI-anchor biosynthesis;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..345
FT /note="Putative phosphatidylinositol N-
FT acetylglucosaminyltransferase subunit C"
FT /id="PRO_0000365732"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 13..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 38730 MW; 01DFEBED78BC6AEF CRC64;
MNDHHLNHRI INNINASSSS SSSSSPVQTN ININSANNTN NNNNNNNNNN NNNNNNNNNI
DNKWKKNLYE KQPYSDNYTD ETFLIGLVQN ANFIKYDFWT VVLDSFTVSQ QITSVILFAI
IFFHSLKHTL TLPFLVAMAG GFLVLGYIAI IIIDPSANFL SIRSSFLHII LLFGTVYGLS
PVLRTLTNSF SDDTIWALTF ILLLAHLFFH DYGYTNNESQ KFSAPVSLNA AIFASVLLGS
RLPSNIHVFV LISYAIETFA LFPIFRHHLK RHSMELHVGL TVILCVTCSL LLLGMSKLLA
LIYIGIIGTI TFVCPLWLIF IQKYKNEING PWDEASVISQ SGGEF
