SMP3_DEBHA
ID SMP3_DEBHA Reviewed; 535 AA.
AC Q6BJ96; B5RV28;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 82.
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=DEHA2G04114g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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=CAR65907.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR382139; CAR65907.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002770572.1; XM_002770526.1.
DR AlphaFoldDB; Q6BJ96; -.
DR STRING; 4959.XP_002770572.1; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR EnsemblFungi; CAR65907; CAR65907; DEHA2G04114g.
DR GeneID; 8999120; -.
DR KEGG; dha:DEHA2G04114g; -.
DR eggNOG; KOG4123; Eukaryota.
DR HOGENOM; CLU_022957_2_0_1; -.
DR InParanoid; Q6BJ96; -.
DR OrthoDB; 821144at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000599; Chromosome G.
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..535
FT /note="GPI mannosyltransferase 4"
FT /id="PRO_0000246276"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..91
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..181
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..284
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..337
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..535
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 535 AA; 61750 MW; 7CE0BF46B38F0EC0 CRC64;
MSLSLDFNWR YVYLIAIGLK FVLALSNSYI HPDEHFQSFE VLTNKIFSFT TTTPWEFSSD
TPARSFGPLY LFYAPLLYSI KLVGYELSPL QIWYMARLQN VLIGWVITDM CIYRLLPTKP
ERIKGLFYTS TSYITLVYQS HCFSNSIETW LVLICVLVIN DLRFIQESNV PELQSQRQYQ
KLFWFGALVS IGIFNRITFP AFLALPSLYL MKYFRHNKMS AIFSLLGFML PTIAIILLDT
FEFNGSIDDI LKHPLDFNSY VITPLNNLIY NSKVENLSNH GLHPYYTHLL VNLPQILGPG
LFFMVSNFKN QYWKTTPFLA VISGVSVLSL IPHQELRFLI PIVPLVCCCF DLKNISSASK
GERITKAPPM VSVLMNLWYL FNILLAVLMG VYHQGGIVPA LDYFHSNIFQ ENSRQSVQIW
WRTYSPPPWI LGDKLDTLQV LTVTDDSPQF ELDSSKSNYL IDAMGSDYTH VSKLIESFKD
FSGSIYLIAP IASIRKHYDI SMHQVWNYTH HLDLDHIDFS DFQSLKPGLG IYELL
