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BMT5_CANAL
ID   BMT5_CANAL              Reviewed;         612 AA.
AC   Q5ALW2; A0A1D8PGF2;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Beta-mannosyltransferase 5;
DE            EC=2.4.1.-;
DE   AltName: Full=WRY family protein 6;
GN   Name=BMT5; Synonyms=IFQ4, WRY6; OrderedLocusNames=CAALFM_C201560WA;
GN   ORFNames=CaO19.1464, CaO19.9039;
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=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=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).
RN   [6]
RP   FUNCTION.
RX   PubMed=22745283; DOI=10.1093/glycob/cws097;
RA   Mille C., Fradin C., Delplace F., Trinel P.A., Masset A., Francois N.,
RA   Coddeville B., Bobrowicz P., Jouault T., Guerardel Y., Wildt S., Janbon G.,
RA   Poulain D.;
RT   "Members 5 and 6 of the Candida albicans BMT family encode enzymes acting
RT   specifically on beta-mannosylation of the phospholipomannan cell-wall
RT   glycosphingolipid.";
RL   Glycobiology 22:1332-1342(2012).
CC   -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis.
CC       Required for beta-1,2-mannose transfer on phospholipomannan.
CC       {ECO:0000269|PubMed:22745283}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Expression is induced in biofilm.
CC       {ECO:0000269|PubMed:22265407}.
CC   -!- SIMILARITY: Belongs to the BMT family. {ECO:0000305}.
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DR   EMBL; CP017624; AOW27202.1; -; Genomic_DNA.
DR   RefSeq; XP_722514.1; XM_717421.1.
DR   AlphaFoldDB; Q5ALW2; -.
DR   SMR; Q5ALW2; -.
DR   BioGRID; 1218875; 1.
DR   CAZy; GT91; Glycosyltransferase Family 91.
DR   GeneID; 3635781; -.
DR   KEGG; cal:CAALFM_C201560WA; -.
DR   CGD; CAL0000182482; BMT5.
DR   VEuPathDB; FungiDB:C2_01560W_A; -.
DR   eggNOG; ENOG502QTZG; Eukaryota.
DR   HOGENOM; CLU_013841_1_1_1; -.
DR   InParanoid; Q5ALW2; -.
DR   OMA; KEVWISF; -.
DR   OrthoDB; 487566at2759; -.
DR   PRO; PR:Q5ALW2; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0006688; P:glycosphingolipid biosynthetic process; IMP:CGD.
DR   InterPro; IPR021988; BMT1.
DR   PANTHER; PTHR37989; PTHR37989; 1.
DR   Pfam; PF12141; DUF3589; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..612
FT                   /note="Beta-mannosyltransferase 5"
FT                   /id="PRO_0000426073"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        34..612
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        480
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   612 AA;  70896 MW;  F05BC3888A29A33A CRC64;
     MVQKQYRFAP KSIFTFVFLC FVAIVVIIST SSLVQVEESL DPIEVSDEIK KHDRKVVIFP
     SNFQSANNKL ADFLTEAFGQ RLNKGDIVYK NRDTYELPQT VYTWNTIDLF QSIGEKDNLK
     CEKIPLNFEI SKIYNKNADL YKILRDFKNE NSFYYKEVSV FFPDLGKQLR ERTIEKHWFQ
     LIGSSVWLEQ YGVHLMISRV IYTKTGNKVQ PVISLSYVQA FDRNWTELKN VTLVVPDSGK
     AKFKTVSYPS FIPIPVYHNV NQQRGKFYGV EDPRIMLVKN KEGYEEPLIV YNSFNRSPPN
     ANYLEEIKNL VKLDTYRSIF MAWIWRTQLG KSNVGSSLPD LATTDDHKYV KVKELSLPNK
     KRPKTEKNWT PFVIYEDQKK QGYDSHLYFI YSFQDLSILK CSLWDAGNCI WEYRMNNKKT
     KISELRGGTE LMNVNQLLDK YNFAGLETVK DQFKGKEVWI SFARAALSKC GCGSKMYRPN
     FTVLVKQGGR FQLSFVSSYM DFGVPILPWA KGKGLCNGKN LLIPNGISNW VLAKDEGGGF
     QDYMTLSLSR SDSTVDIIHM KGILKSILSE YLLQTNRDVL NNNAIHCALL ESESYCKSYA
     ENYRAHLKRW QN
 
 
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