BMT4_CANAL
ID BMT4_CANAL Reviewed; 781 AA.
AC Q5ABT8; A0A1D8PQ41; Q5AC62;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Beta-mannosyltransferase 4;
DE EC=2.4.1.-;
DE AltName: Full=WRY family protein 1;
GN Name=BMT4; Synonyms=WRY1; OrderedLocusNames=CAALFM_C603250WA;
GN ORFNames=CaO19.13055, CaO19.5612;
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 INDUCTION.
RX PubMed=16102003; DOI=10.1111/j.1365-2958.2005.04771.x;
RA Urban C., Xiong X., Sohn K., Schroppel K., Brunner H., Rupp S.;
RT "The moonlighting protein Tsa1p is implicated in oxidative stress response
RT and in cell wall biogenesis in Candida albicans.";
RL Mol. Microbiol. 57:1318-1341(2005).
RN [5]
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 [6]
RP INDUCTION.
RX PubMed=21414038; DOI=10.1111/j.1365-2958.2011.07626.x;
RA Bonhomme J., Chauvel M., Goyard S., Roux P., Rossignol T., d'Enfert C.;
RT "Contribution of the glycolytic flux and hypoxia adaptation to efficient
RT biofilm formation by Candida albicans.";
RL Mol. Microbiol. 80:995-1013(2011).
CC -!- FUNCTION: Beta-mannosyltransferase involved in cell wall biosynthesis.
CC Required for the elongation of beta-mannose chains on the acid-labile
CC fraction of cell wall phosphopeptidomannan.
CC {ECO:0000269|PubMed:18234669}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Expression in regulated by TSA1 and repressed in rat
CC catheter biofilm. {ECO:0000269|PubMed:16102003,
CC ECO:0000269|PubMed:21414038}.
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; CP017628; AOW30255.1; -; Genomic_DNA.
DR RefSeq; XP_719173.2; XM_714080.2.
DR AlphaFoldDB; Q5ABT8; -.
DR CAZy; GT91; Glycosyltransferase Family 91.
DR GeneID; 3639182; -.
DR KEGG; cal:CAALFM_C603250WA; -.
DR eggNOG; ENOG502QTZG; Eukaryota.
DR HOGENOM; CLU_013841_1_0_1; -.
DR InParanoid; Q5ABT8; -.
DR OrthoDB; 487566at2759; -.
DR PRO; PR:Q5ABT8; -.
DR Proteomes; UP000000559; Chromosome 6.
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; IBA:GO_Central.
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; Coiled coil; Glycosyltransferase;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..781
FT /note="Beta-mannosyltransferase 4"
FT /id="PRO_0000426072"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..781
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 663..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 640..733
FT /evidence="ECO:0000255"
FT COMPBIAS 663..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..739
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..781
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 90959 MW; 82B47D1C6123C4E2 CRC64;
MTKSYMPLFR SPRQFKKIYF ILIPLILAVI ILHVFFDGFN KISEYSPTFI SNRILNHQDQ
QQKSEKSSDV ISSYFPSLAI YPKNFDNRVE FVNEPKNSKW IQYFGDSKTV LSNYITNQTY
TNHSIGLYSS STVRPPASSC KDILYERSFE ITKYRTLHDD LYKLATTLLY QLENDPAFQD
LSPFFNDRLP HIIMRGELHK HIYKFAGTSV WLEQHGVHLM LSRVIYSQQG KKNDPQLSLL
YAQVYDENWN ELNDIELIVP VINPNGERVY DSVKYPQFLA IPFYHNSEYI KSRWYGPEDT
RLILTKNKFG DDEPVIIFNS YHRQIKDMST EDDNNVHTKF EFYRSMFVGW LFQYQLGKLN
TDGIQDSKFN NVTFNKVKEL RIEGKERTSI EKNWTPFIDP DERNQISYYG NHNLGDNYVY
IVYQWNHLKI LKCELDNFID SSHSTCTMFF KDVETTQEVG PVRGGTELWP IKIDNNNNNN
NLNEDDLSTK QEPQQQRQLW IGFLRAHVKD CGCGGSMYRP NFLILEKLNS KFKLTYLSGS
INFNVSVYGW ANYDVVCAGH EANALIPNGI SMFDQDDDYL TLSMSVADQD NTLVHIHGVK
KLIYSLDHDW NGILKENKQI ECVVNNANDF CKAYADEHYK LGDSEAAIKE VKQKAKEEAE
KAKAEKEKAE KEKAEKEKAE KEKEEKEKEE KEEKEKAEKE KEEKEKAEKE LAEKELAEQK
DEDAKDEDKN EDEDDKEKND ESGLTEKSEV EENGENTNEG GEDDGDGDGE EEKEDDDDIE
V
