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SMP3_EMENI
ID   SMP3_EMENI              Reviewed;         546 AA.
AC   Q5BAX7; C8VN51;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, 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=AN2303;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA64414.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000038; EAA64414.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF86568.1; -; Genomic_DNA.
DR   RefSeq; XP_659907.1; XM_654815.1.
DR   AlphaFoldDB; Q5BAX7; -.
DR   STRING; 162425.CADANIAP00008996; -.
DR   CAZy; GT22; Glycosyltransferase Family 22.
DR   EnsemblFungi; CBF86568; CBF86568; ANIA_02303.
DR   EnsemblFungi; EAA64414; EAA64414; AN2303.2.
DR   GeneID; 2874611; -.
DR   KEGG; ani:AN2303.2; -.
DR   VEuPathDB; FungiDB:AN2303; -.
DR   eggNOG; KOG4123; Eukaryota.
DR   HOGENOM; CLU_022957_2_0_1; -.
DR   InParanoid; Q5BAX7; -.
DR   OMA; VLWWKTY; -.
DR   OrthoDB; 821144at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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..546
FT                   /note="GPI mannosyltransferase 4"
FT                   /id="PRO_0000246277"
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        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
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        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   546 AA;  61427 MW;  F47DBBD99B77B528 CRC64;
     MWRRTYLLLL LIRAYFALSP SYIHPDEHFQ GLEVFAGRIL SYPSRLPWEF TSERPIRSVF
     PLYPIYGVPI SLLKWFYTET GTESPPAELV YYVVRGVMFL LSFVLEDWAV HDLVPLPRHR
     RVALVLVASS YVTWTHQTHT FSNSLETLLV AWGLVLINRI IDNKRRSSLF SCAILSFICV
     AGIFNRITFP AFLVLSLGLV VYNFPRRPLS FFSLVGFGLV FFCIAVFADT TFYKPSASFA
     DVLRSPVITP LNNLLYNTDN SNLALHGLHP HYNHFLVNLP QLLGPALVAM VLQAYNRGFI
     ASWFKNLRAA SALSATAMLS IFPHQEPRFL IPCVPLLLSC LQVRKSRIFL GAWVIFNATL
     GFLMGVYHQG GVVSTQLAVP SVISTTTSLW HESLKGTQSL FATVVWWKTY SPPLWLLGDN
     STLNLNIDTR DLMGKPGSEM VKELERLVPT CGSKQKSTEL TSSLEQPDAV FVVAPKSVTF
     LDQFLAPQSP DSSLELLELW SYKKHISLDD LDFGSDGVLP TMKRVIGRRG LGVWLAQRPG
     CRAIDS
 
 
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