GPI14_NEUCR
ID GPI14_NEUCR Reviewed; 487 AA.
AC Q7S4Z3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=GPI mannosyltransferase 1;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase I;
DE Short=GPI-MT-I;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 14;
GN Name=gim-1; Synonyms=gpi14; ORFNames=NCU06057;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-
CC acyl-PI during GPI precursor assembly. Required for cell wall integrity
CC (By similarity). {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 PIGM family. {ECO:0000305}.
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DR EMBL; CM002242; EAA30584.1; -; Genomic_DNA.
DR RefSeq; XP_959820.1; XM_954727.2.
DR AlphaFoldDB; Q7S4Z3; -.
DR STRING; 5141.EFNCRP00000005331; -.
DR CAZy; GT50; Glycosyltransferase Family 50.
DR EnsemblFungi; EAA30584; EAA30584; NCU06057.
DR GeneID; 3875967; -.
DR KEGG; ncr:NCU06057; -.
DR VEuPathDB; FungiDB:NCU06057; -.
DR HOGENOM; CLU_024220_1_0_1; -.
DR InParanoid; Q7S4Z3; -.
DR OMA; VTSQYFI; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051751; F:alpha-1,4-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR InterPro; IPR007704; PIG-M.
DR PANTHER; PTHR12886; PTHR12886; 1.
DR Pfam; PF05007; Mannosyl_trans; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum;
KW Glycosyltransferase; GPI-anchor biosynthesis; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..487
FT /note="GPI mannosyltransferase 1"
FT /id="PRO_0000246232"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 147..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 54029 MW; D9F8D05D9C6C98D9 CRC64;
MATTSPAAPR PKSKSSSLLS TLFSRPLPLY VSAFLLRIVL LLYGLWQDAN SPLKYTDIDY
LVFTDAARFV SRGESPYARE TYRYTPILAW LLLPTTWTAG AQWGPWAAKV INVAWFSFGK
VLFAAADLVA GWLIEQVLVM GKDFPSSAAK GKEKDTEKTK EGGKKGPSVT ASTGMDPSRA
RAFAAIWLLN PMVATISTRG SSEGLLGVLV MALLWAVLSR RITLAGLLLG FSVHFKIYPF
IYAPAIVWWM DQERLSGVRA GGGGGGGGQK KTSSSFRKTL TRFLTLPRLL LAFTSLATFL
SLNFLMYRLY GHPFLQETYL HHVTRIDHRH NFSPYNTQLY LSSASVSPSH SAAEPKFKIE
SLAFLPQLVL STILIPLTLA KKDLPTSLLA QTFAFVTFNK VCTSQYFLWY LVLLPLYLPR
SSFWTSKRMG LVALGLWVLG QALWLQQAYE LEFLGRSTFL PGLWMASLGF FVVNCWILGV
IVGDGGR