ID   SMP3_ASHGO              Reviewed;         498 AA.
AC   Q753C1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 3.
DT   25-MAY-2022, entry version 92.
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; OrderedLocusNames=AFR395C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 245-264.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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=AAS53766.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE016819; AAS53766.2; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_985942.2; NM_211297.2.
DR   AlphaFoldDB; Q753C1; -.
DR   STRING; 33169.AAS53766; -.
DR   CAZy; GT22; Glycosyltransferase Family 22.
DR   GeneID; 4622214; -.
DR   KEGG; ago:AGOS_AFR395C; -.
DR   eggNOG; KOG4123; Eukaryota.
DR   InParanoid; Q753C1; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000000591; Chromosome VI.
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..498
FT                   /note="GPI mannosyltransferase 4"
FT                   /id="PRO_0000246271"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   498 AA;  55736 MW;  7B3850CE518ED1C7 CRC64;
     MRLAVIRYIW LLVALLVALE PAYVHPDEHM QSVEVMMQKI FGLRGTVPWE FQPEYAARSF
     APLWIFMGPA LVAARLFNAG PRVVLGLLRI QGYFLYVSLT RVAVELVGRT KLRRSMAAFL
     LSTTYVVGAF QSHTFSNSIE TLLAVAAVGL LEVVIADGRA GHRHVRISGV LGFLIALGLF
     NRVTFAGYLG LPCIVAFWQF YRRQWRSLAA LLLCFLLTSG ACIWIDTLSY GTSEWVITPL
     NNLLYNMDEE NLAQHGLHPR YTHILVNLPM LLGPGLLFAL GGIQRLSLPL LSCVSGVATL
     SLFKHQEARF LLPVVPLFLM SVDLTKLRTV SLTLTLKLWL AFNGLMVVIM GVGHQRGVIT
     ALHQLREEPI GVQVWWKTYS PPTWVLMNEA LTVSTTNFVG DDERIDEVPL DVTRNHVIDL
     KGCNIELLNH TLSQFIAAGS KVHLIVPDSV AKKTALLTKR YGFDIHREFR TLVHLDLDHL
     DWSEPSSFTP GLSIYTVT