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GPI10_TRYB2
ID   GPI10_TRYB2             Reviewed;         558 AA.
AC   P86936; Q38B48; Q9NKZ7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 45.
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;
GN   Name=GPI10; ORFNames=Tb10.70.1440;
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA   Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA   Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA   Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA   Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA   Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA   Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA   Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA   Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA   Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA   Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA   Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA   Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA   Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA   Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA   Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
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 (By similarity).
CC       {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGB
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CM000208; EAN77972.1; -; Genomic_DNA.
DR   RefSeq; XP_822800.1; XM_817707.1.
DR   AlphaFoldDB; P86936; -.
DR   STRING; 5691.EAN77972; -.
DR   PaxDb; P86936; -.
DR   PRIDE; P86936; -.
DR   GeneID; 3662460; -.
DR   KEGG; tbr:Tb10.70.1440; -.
DR   eggNOG; KOG1771; Eukaryota.
DR   InParanoid; P86936; -.
DR   OMA; HHMVFNN; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000008524; Chromosome 10.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..558
FT                   /note="GPI mannosyltransferase 3"
FT                   /id="PRO_0000412122"
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;  64398 MW;  297AC187A17F5C67 CRC64;
     MPWWLISLTF IYRLFLCATI RTVEAPDEWW QSTEVAYNMV FGKGHLPWEW RYGLRSVFFP
     AVVALPFYLL KLLGRDTTWA VWFAPRVLQA LVLTLIDVSV FRMGATLDEL LAKRELELAE
     EMRQSKTKGF SYFREVFVSR SRRGICNSIS YTALLLSLSN WYMAYCGVRL YGNVIEALLV
     LLTLQQRRYV PFLLLTGLAS AIRVTSAVVL SPLVFRHLAN ATREHGFTRG LFRIVLTGLI
     VLVAVLGGVM VLDYCFYGRW VLTPLAFFRF NVLHNLSRFF GEHPWYFYVG PVLVGIVGPH
     VLFTIAAPLV LWRDTASRAV SRPVLGMLGI GAWTLGFYSL IDHKEMRFVF VVIPLSLITA
     AFVLVRWSRT SAVVVKMNRL FVLFNIVMIY LMGYVYRRGP LDVMAEVRDG PRINRLDVIA
     TCYTVPGYSY MHRKVNHLGF VDCSIDLDEK TGLPKVTEDI MFRRYPKEYV LWRYDGKHSF
     NMGDLEESRK ASELQSVVMP KSAPHPDAMV MTRAVAKEIE EPFLKRHGYR LYRTFLHSPL
     TLAPYEDIYI QMWVKVTK
 
 
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