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SMP3_CANAL
ID   SMP3_CANAL              Reviewed;         498 AA.
AC   Q5A0L9; A0A1D8PGU9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=GPI mannosyltransferase 4;
DE            EC=2.4.1.-;
DE   AltName: Full=CaSMP3;
DE   AltName: Full=GPI mannosyltransferase IV;
DE            Short=GPI-MT-IV;
GN   Name=SMP3; OrderedLocusNames=CAALFM_C203070CA;
GN   ORFNames=CaO19.13214, CaO19.5792;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=15470093; DOI=10.1099/mic.0.27254-0;
RA   Grimme S.J., Colussi P.A., Taron C.H., Orlean P.;
RT   "Deficiencies in the essential Smp3 mannosyltransferase block
RT   glycosylphosphatidylinositol assembly and lead to defects in growth and
RT   cell wall biogenesis in Candida albicans.";
RL   Microbiology 150:3115-3128(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   -!- MISCELLANEOUS: May be used as a target for the development of some new
CC       fungicide, due the fact the presence of a fourth mannose in GPI-anchor
CC       proteins is essential for viability in fungi but not in mammals.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGZ
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CP017624; AOW27344.1; -; Genomic_DNA.
DR   RefSeq; XP_715333.2; XM_710240.2.
DR   AlphaFoldDB; Q5A0L9; -.
DR   STRING; 237561.Q5A0L9; -.
DR   GeneID; 3642980; -.
DR   KEGG; cal:CAALFM_C203070CA; -.
DR   CGD; CAL0000175734; SMP3.
DR   VEuPathDB; FungiDB:C2_03070C_A; -.
DR   HOGENOM; CLU_022957_2_0_1; -.
DR   InParanoid; Q5A0L9; -.
DR   OrthoDB; 821144at2759; -.
DR   UniPathway; UPA00196; -.
DR   PRO; PR:Q5A0L9; -.
DR   Proteomes; UP000000559; Chromosome 2.
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   GO; GO:0006276; P:plasmid maintenance; IEA:EnsemblFungi.
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_0000246274"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   498 AA;  57971 MW;  98A3C4952410BCE5 CRC64;
     MIKINFNWRT FYLLTIVFRF VFTLSDSYIH PDEHFQSLEV LTNRILNYST NIPWEFQDDP
     ARSLAPLYFI YGPLLYFIKF FKLNLTALQI WYIARLQISI LSWIITDFCL YWMLPSKPER
     IKAIFFTSTS YITLVYQNHL FSNSIETLLL LVTILLIDDL RYVQESKDQD VQNLNKNKNL
     FYTGVLISLG IFNRITFPAF LILPGWFVMK YVLKHYVSGL YLVMGFFSTT ALLILVDTIL
     FGNINNVVAE PFNVSSYIIA PLNNLLYNAR YENLAQHGIH PYYTHILVNM PQILGPGLIF
     FVSKSYTKTT PFLTVISGLL FLSVIPHQEL RFLIPLLPLA CCSFDFTLKW VQPWMLYTWY
     IFNIFMSILM GKLHQGGVVP VLDHIKSEAS VQVWWRTYTP PSWILGSNST ETTHLGEKLN
     DNKFINIVDC MGADSKEVQQ ILQTISTNKP VYLITPIASF KHFDESRFSP VWNYTFHLDL
     DHLDFADIQP GLGVYQLL
 
 
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