SMP3_ASPFU
ID SMP3_ASPFU Reviewed; 547 AA.
AC Q4WTT7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=GPI mannosyltransferase 4;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase IV;
DE Short=GPI-MT-IV;
GN Name=smp3; ORFNames=AFUA_5G06050;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Alpha-1,2-mannosyltransferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth
CC mannose to trimannosyl-GPIs during GPI precursor assembly. The presence
CC of a fourth mannose in GPI is essential in fungi (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 -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGZ
CC subfamily. {ECO:0000305}.
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DR EMBL; AAHF01000003; EAL91989.2; -; Genomic_DNA.
DR RefSeq; XP_754027.2; XM_748934.2.
DR AlphaFoldDB; Q4WTT7; -.
DR STRING; 746128.CADAFUBP00005248; -.
DR EnsemblFungi; EAL91989; EAL91989; AFUA_5G06050.
DR GeneID; 3511136; -.
DR KEGG; afm:AFUA_5G06050; -.
DR VEuPathDB; FungiDB:Afu5g06050; -.
DR eggNOG; KOG4123; Eukaryota.
DR HOGENOM; CLU_022957_2_0_1; -.
DR InParanoid; Q4WTT7; -.
DR OMA; VLWWKTY; -.
DR OrthoDB; 821144at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002530; Chromosome 5.
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: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 PANTHER; PTHR22760; PTHR22760; 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..547
FT /note="GPI mannosyltransferase 4"
FT /id="PRO_0000246272"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 547 AA; 61599 MW; 758C3A1FB4F1CC17 CRC64;
MWRRTYLLLL LVRVYFALSP SYLHPDENFQ GPELFAGRTL SYPSKLPWEF TSENPIRSVF
PLWPVYSLPM GLLKWFYVEL EIGNPSPEVA YYSLRAVMFL LSFVLEDWAI YELVPLPRHR
RAAVVLVASS YVTWTYQTHT FSNSLETLLV TWGLVLIRRI AGQKRRSSVF SCVVLALITV
AGVFNRITFP AFLLIPGLQL LPHFWRRPTS LFVFVLWGLF FSCTAIIIDT RFYRPSASVL
DALRSPIITP LNNLLYNTKT SNLALHGLHP HYQHFLINLP QLLGPAFVAM ILSLWNRPAI
PSWLKTTQAV SALSGTAMLS VFPHQEPRFL IPCVPLLLSC FRLRKSRLFI VAWVIFNVAL
GFLMGVYHQG GVVPVQLAIP NIISANTLKS NKSLENQPRV SATVLWWKTY SPPSWLLGNN
TNFPLDIDTR DLMGIPGAEM AQELEQLVPP CSSHSGTHMD DASAGSGRAD RTNFVLVVAP
RSATYLDQYT TAAAGSSGLE LQELYSYPQH INMDDLDVGT DGLLATLKRV FGRRGLNVWL
ARRAGCD
