ID   SMP3_ASPOR              Reviewed;         543 AA.
AC   Q2UTP0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=AO090009000654;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP007150; BAE55075.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2UTP0; -.
DR   STRING; 510516.Q2UTP0; -.
DR   CAZy; GT22; Glycosyltransferase Family 22.
DR   EnsemblFungi; BAE55075; BAE55075; AO090009000654.
DR   HOGENOM; CLU_022957_2_0_1; -.
DR   OMA; VLWWKTY; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000006564; Chromosome 1.
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:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
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..543
FT                   /note="GPI mannosyltransferase 4"
FT                   /id="PRO_0000246273"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   543 AA;  60694 MW;  200EE14BEE7F5463 CRC64;
     MWRRTYLLLL VIRVYFALSP SYLHPDENFQ GPEVFAGRVL SYPSKLPWEF TADKPIRSVF
     PLWPIYDVPI SLLKWFYAET GAPTPPPPQV IYYVLRGVMF LLGFVLEDWA VYELVPFARH
     RRATVVLVAS SYVTWTYQTH TFSNSLETLL VAWGLVLIRR IVVNKRRSSV FSCAVLAFIA
     VAGVFNRITF PAFLAIPGLQ LLPHFRRKSV SPPVSLFSFV GFGIFFFGIA VLVDTAFYRP
     SATLWDALHS PIITPINNLL YNSDSSNLAL HGLHPHYQHF LVNLPQLLGP AYAMMAISLW
     GLPVIPTWLK NARAVSALSA TVILSIFPHQ EPRFLIPCVP LLLSCFRVSK SRLFLAVWMI
     FNAALGFLMG IYHQGGVVPA QLAMPSIISA SSVESNDALP GEIPVVSATV FWWKTYSPPL
     WLLGTNDNSS LNIETRDLMG VPGPNLIEEL EKLLPPCNVA GSKQAGSVFV VAPKSAAFLD
     RYTFLPSSSS VSSALELHEL WSYRKHINLD DLDFGTEGVY PTLRRVIGRR GLAVWRAKRA
     GCN