ID   GPI10_TRYBB             Reviewed;         558 AA.
AC   P86935; Q38B48; Q9NKZ7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=GPI mannosyltransferase 3;
DE            EC=2.4.1.-;
DE   AltName: Full=GPI mannosyltransferase III;
DE            Short=GPI-MT-III;
DE   AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 10;
DE   AltName: Full=TbGPI10;
GN   Name=GPI10;
OS   Trypanosoma brucei brucei.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=5702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=427;
RX   PubMed=10954751; DOI=10.1073/pnas.180230697;
RA   Nagamune K., Nozaki T., Maeda Y., Ohishi K., Fukuma T., Hara T.,
RA   Schwarz R.T., Sutterlin C., Brun R., Riezman H., Kinoshita T.;
RT   "Critical roles of glycosylphosphatidylinositol for Trypanosoma brucei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10336-10341(2000).
CC   -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC       anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-
CC       GlcN-acyl-PI during GPI precursor assembly.
CC       {ECO:0000269|PubMed:10954751}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- MISCELLANEOUS: The protozoan parasite evades the immune response of
CC       mammalian hosts and digestion in the gut of the insect vector by means
CC       of its coat proteins tethered to the cell surface via GPI-anchors.
CC       GPI10 is essential for growth of mammalian stage bloodstream form,
CC       while procyclic form (insect stage parasites) are viable but grow
CC       slower, suggesting that inhibition of GPI synthesis may be an effective
CC       chemotherapy against African trypanosomiasis.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB033824; BAA94863.1; -; mRNA.
DR   AlphaFoldDB; P86935; -.
DR   UniPathway; UPA00196; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0000030; F:mannosyltransferase activity; TAS:GeneDB.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR005599; GPI_mannosylTrfase.
DR   InterPro; IPR039521; PIG-B/GPI10.
DR   PANTHER; PTHR22760; PTHR22760; 1.
DR   PANTHER; PTHR22760:SF4; PTHR22760:SF4; 1.
DR   Pfam; PF03901; Glyco_transf_22; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   GPI-anchor biosynthesis; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..558
FT                   /note="GPI mannosyltransferase 3"
FT                   /id="PRO_0000246256"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   558 AA;  64182 MW;  672E51B7E055FE8F CRC64;
     MPWWLISLTF IYRLFLCATI RTVEAPDEWW QSTEVAYNMV FGKGHLPWEW RYGLRSVLFP
     AVVALPFYLL KLLGRDTTWA VWFAPRVLQA LVLTLIDVSV FCMGATLDEL LAKRELELAE
     ETRQSKTKGF SYFCEVSVSR SRRGICNSIS YTALLLSLSN WYMAYCGVRL YGNVIEALLV
     LLTLQQRRYV PFLLLTGLAS AIRVTSAVVL SPLVFRHLAN ATREHGFIRG LFRIVLTGLI
     VLVAVLGGVM VLDYCFYGRW VLTPLAFFRF NVLHNLSRFF GEHPWYFYVG PVLVGIVGPH
     VLFTIAAPLV LWRDTASRAV SRPVLGMLGI GAWTLGFYSL IDHKEMRFVF VVIPLSLITA
     AFVLVRWSRT SAVVVKMNRL FVLFNIVMIY LMGYVYRRGP LDVMAEVRDG PRINRLDVIA
     TCYTVPGYSY MHKKVNHLGF VDCSIDLDEK TGLPKVTEDI MFRRYPKEYV LWRYDGKHSF
     NMSDLEESRK ASELQSVVMP KSAPHPDAMV MTRAVAKEIE EPFLKRHGYR LYRTFLHSPL
     TLAPYEDIYI QMWVKVTK