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MNT4_CANAL
ID   MNT4_CANAL              Reviewed;         719 AA.
AC   Q59MZ9; A0A1D8PST3;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Putative alpha-1,3-mannosyltransferase MNT4;
DE            EC=2.4.1.-;
GN   Name=MNT4; Synonyms=MNN16; OrderedLocusNames=CAALFM_CR04800WA;
GN   ORFNames=CaO19.13690, CaO19.6313;
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=15387822; DOI=10.1111/j.1365-2958.2004.04214.x;
RA   Lan C.Y., Rodarte G., Murillo L.A., Jones T., Davis R.W., Dungan J.,
RA   Newport G., Agabian N.;
RT   "Regulatory networks affected by iron availability in Candida albicans.";
RL   Mol. Microbiol. 53:1451-1469(2004).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=23886038; DOI=10.1186/1756-0500-6-294;
RA   Bates S., Hall R.A., Cheetham J., Netea M.G., MacCallum D.M., Brown A.J.,
RA   Odds F.C., Gow N.A.;
RT   "Role of the Candida albicans MNN1 gene family in cell wall structure and
RT   virulence.";
RL   BMC Res. Notes 6:294-294(2013).
CC   -!- FUNCTION: Responsible for addition of the terminal mannose residues to
CC       the outer chain of core N-linked polysaccharides and to O-linked
CC       mannotriose. Implicated in late Golgi modifications (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- INDUCTION: induced in low iron conditions.
CC       {ECO:0000269|PubMed:15387822}.
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR   EMBL; CP017630; AOW31213.1; -; Genomic_DNA.
DR   RefSeq; XP_711098.1; XM_706006.1.
DR   AlphaFoldDB; Q59MZ9; -.
DR   STRING; 237561.Q59MZ9; -.
DR   GeneID; 3647300; -.
DR   KEGG; cal:CAALFM_CR04800WA; -.
DR   CGD; CAL0000182375; MNT4.
DR   VEuPathDB; FungiDB:CR_04800W_A; -.
DR   eggNOG; ENOG502T9W7; Eukaryota.
DR   HOGENOM; CLU_028276_0_0_1; -.
DR   InParanoid; Q59MZ9; -.
DR   OrthoDB; 527450at2759; -.
DR   UniPathway; UPA00378; -.
DR   PHI-base; PHI:3695; -.
DR   PRO; PR:Q59MZ9; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000033; F:alpha-1,3-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   InterPro; IPR022751; Alpha_mannosyltransferase.
DR   Pfam; PF11051; Mannosyl_trans3; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..719
FT                   /note="Putative alpha-1,3-mannosyltransferase MNT4"
FT                   /id="PRO_0000424329"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        23..719
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        273
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   719 AA;  83976 MW;  4E37C3A03EA418BE CRC64;
     MKFHLKRYVI VTSILLSFFL LFRRQFLPLT QRQPNPINNE LVSFDLIKQR NKFENPIYAK
     WKLSSSSPLE TDLTTRCNDY FQQLLTQENF QINYHDSGYK TEPFVYKRKK WLKERIRSLR
     KQYKFDKNKD KYDFDQIAKQ EFSIVSKNQS IHELNIYQHF SHTRIFGKCF ATNNNNNNNN
     GVINMENPQS NQLCKSFVQK LYPWMSGNLP IFERNKERSP PQLDDSTDCI IEQIYKNSKG
     KGKGIIIPLM TQDKSNNQIQ NIGRLIKVLR GLNNTLPIEI TFMELITPEA KQQLYDIATS
     DSQMYPTKQD IAFVDLSPTT TNQVKGSISD SSIITLSSIF TSFEEFIILN QHIIPLIELT
     KFFNNERYKL HGTYFFKSPS KLKYRTTKFN IGFHEIASFI KNQLIPNKFD KHYFNLYQKG
     SENGDEVTID RFFNYQFNNL IDSSLIIFNK SKTLSGLLIS GNFEFLYHDD LFNIRINNTP
     TKTKMDYLWL GQYISGINEQ IIFNFNYAIM PGILTPSQNL PKDSIECLEI CSSSWGQLSD
     IDDISLLYIT SHQLQNWLNH QKFFESLLKD KYEFKFNELV DNFLITNTNT NTNTNTNTNG
     NTNDKDSTKL TMGRIDLSIF EKIKTQPLKI ETIIRPPTLI EPINVLGYNE PDQAWVHQDD
     FDRIGQNGQG QGQGQGHPFY CVYSSIGDPL KEGIRGLSIN VEQSLQKKYK KLIEIWLQD
 
 
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