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BMT3_CANAL
ID   BMT3_CANAL              Reviewed;         549 AA.
AC   Q5A846; A0A1D8PRU1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Beta-mannosyltransferase 3;
DE            EC=2.4.1.-;
DE   AltName: Full=WRY family protein 9;
GN   Name=BMT3; Synonyms=WRY9; OrderedLocusNames=CAALFM_CR00740CA;
GN   ORFNames=CaO19.10792, CaO19.3282;
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, DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=18234669; DOI=10.1074/jbc.m708825200;
RA   Mille C., Bobrowicz P., Trinel P.A., Li H., Maes E., Guerardel Y.,
RA   Fradin C., Martinez-Esparza M., Davidson R.C., Janbon G., Poulain D.,
RA   Wildt S.;
RT   "Identification of a new family of genes involved in beta-1,2-mannosylation
RT   of glycans in Pichia pastoris and Candida albicans.";
RL   J. Biol. Chem. 283:9724-9736(2008).
RN   [5]
RP   INDUCTION.
RX   PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA   Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT   "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT   contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL   J. Biol. Chem. 286:25154-25170(2011).
RN   [6]
RP   INDUCTION.
RX   PubMed=22265407; DOI=10.1016/j.cell.2011.10.048;
RA   Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA   Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT   "A recently evolved transcriptional network controls biofilm development in
RT   Candida albicans.";
RL   Cell 148:126-138(2012).
CC   -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis.
CC       Required for addition of the second beta-mannose residue to acid-stable
CC       fraction of cell wall phosphopeptidomannan, and in elongation of beta-
CC       mannose chains on the phosphopeptidomannan acid-labile fraction.
CC       {ECO:0000269|PubMed:18234669}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Expression is induced in biofilm and by HAP43.
CC       {ECO:0000269|PubMed:21592964, ECO:0000269|PubMed:22265407}.
CC   -!- DISRUPTION PHENOTYPE: Impairs the elongation of beta-mannose chains on
CC       the acid-labile fraction of cell wall phosphopeptidomannan.
CC       {ECO:0000269|PubMed:18234669}.
CC   -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR   EMBL; CP017630; AOW30841.1; -; Genomic_DNA.
DR   RefSeq; XP_717972.1; XM_712879.1.
DR   AlphaFoldDB; Q5A846; -.
DR   CAZy; GT91; Glycosyltransferase Family 91.
DR   PRIDE; Q5A846; -.
DR   GeneID; 3640439; -.
DR   KEGG; cal:CAALFM_CR00740CA; -.
DR   CGD; CAL0000192226; BMT3.
DR   VEuPathDB; FungiDB:CR_00740C_A; -.
DR   HOGENOM; CLU_013841_3_0_1; -.
DR   InParanoid; Q5A846; -.
DR   OMA; VYFMVNR; -.
DR   OrthoDB; 487566at2759; -.
DR   PRO; PR:Q5A846; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000030; F:mannosyltransferase activity; IDA:CGD.
DR   GO; GO:0070136; P:beta-1,2-oligomannoside biosynthetic process; IDA:CGD.
DR   GO; GO:0070135; P:beta-1,2-oligomannoside metabolic process; IMP:CGD.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006688; P:glycosphingolipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IMP:CGD.
DR   InterPro; IPR021988; BMT1.
DR   PANTHER; PTHR37989; PTHR37989; 1.
DR   Pfam; PF12141; DUF3589; 2.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..549
FT                   /note="Beta-mannosyltransferase 3"
FT                   /id="PRO_0000426071"
FT   TOPO_DOM        1..37
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..549
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   549 AA;  62926 MW;  F3AE05283F54271F CRC64;
     MFESDLSFYS ALLILCCPIS IVFFKKFPIK GYTGANKVSL FLQCLIAILN LNILYSFINS
     LTITLGHDGS SANTLTIDPI TTTQQQGHVD YTPIKVSGYT FKNQVATKNL QCDSIVYDQD
     LDLQVSQAVD LNKPEDLKFF RDKLNELRSL NNIYDLFFQD NEDEVEESIL ERKWYKFCGS
     AVWLDKYGVY FMVNRIAYSK KGTRNNPTIS VLAGQVFDKN WIELTGKKFP FSGLEFPTIL
     PHYIDEGKEA EKVILGAEDP RVILHEYTNE NGIRIQEPLI AFNALSTEVD WKRAMHIYRP
     LHDPHRIIRL SIENYAPREK EKNWAPFIDG NNLNFVYNFP LRILRCNINN GDCQKVSGPD
     FNDKSHENAG KLRGGTNLVE IPSQSLPKHL RSRKYWFGIA RSHITDCGCV GELYRPHLIL
     ISRNKKSDQY ELNYVSDLID FNVNPEPWTP GKTTCSDGKS VLIPNSVAFI KDDYMSVTFS
     EADKTNKLIN AKGWLTYITK MLEFTQERLK DESSDPVLES RLLSKCSTFL AQQYCALSKD
     TMGWDKLSR
 
 
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