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MNN13_CANAL
ID   MNN13_CANAL             Reviewed;         764 AA.
AC   Q5AGA9; A0A1D8PNG3;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Putative alpha-1,3-mannosyltransferase MNN13;
DE            EC=2.4.1.-;
GN   Name=MNN13; OrderedLocusNames=CAALFM_C502570WA;
GN   ORFNames=CaO19.11746, CaO19.4270;
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=21843869; DOI=10.1016/j.chom.2011.07.005;
RA   Chen C., Pande K., French S.D., Tuch B.B., Noble S.M.;
RT   "An iron homeostasis regulatory circuit with reciprocal roles in Candida
RT   albicans commensalism and pathogenesis.";
RL   Cell Host Microbe 10:118-135(2011).
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: Expression is regulated by SEF1, SFU1, and HAP43.
CC       {ECO:0000269|PubMed:21843869}.
CC   -!- SIMILARITY: Belongs to the MNN1/MNT family. {ECO:0000305}.
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DR   EMBL; CP017627; AOW29682.1; -; Genomic_DNA.
DR   RefSeq; XP_720578.2; XM_715485.2.
DR   AlphaFoldDB; Q5AGA9; -.
DR   STRING; 237561.Q5AGA9; -.
DR   GeneID; 3637720; -.
DR   KEGG; cal:CAALFM_C502570WA; -.
DR   CGD; CAL0000185691; MNN13.
DR   VEuPathDB; FungiDB:C5_02570W_A; -.
DR   eggNOG; ENOG502RZ48; Eukaryota.
DR   HOGENOM; CLU_015387_0_0_1; -.
DR   InParanoid; Q5AGA9; -.
DR   OrthoDB; 527450at2759; -.
DR   UniPathway; UPA00378; -.
DR   PHI-base; PHI:3692; -.
DR   PRO; PR:Q5AGA9; -.
DR   Proteomes; UP000000559; Chromosome 5.
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:0046354; P:mannan biosynthetic process; IEA:UniProt.
DR   GO; GO:0035268; P:protein mannosylation; IEA:UniProt.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   InterPro; IPR022751; Alpha_mannosyltransferase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF11051; Mannosyl_trans3; 1.
DR   SUPFAM; SSF53448; SSF53448; 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..764
FT                   /note="Putative alpha-1,3-mannosyltransferase MNN13"
FT                   /id="PRO_0000424326"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..764
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   764 AA;  89676 MW;  09FE536CC6E388F1 CRC64;
     MIKPILGTKK IRRVICIIIG LFCILLLIGI FKHNSTNSVN NEASNFTVDF EEPSYTFPKT
     VLFENNNNLD DLLLAKKNNW KFQSNVYNQL FMDHSIESVL SLSFNQRCEL LIRNIISQKV
     SWIFDPLETF EINYESEDYI QFIQQEGIKL NKKFEKIKNN LKFKTSLNNF IKDEYKIIRS
     KQYEQKIIDQ LTILRIFNKC FIKNGSKDQN DLVDRIIQEQ QKLVTKANSA ANGQSELELE
     LKLKLKLTEN EKMVSELVED YVTLGKRVYP WISQRFPFYE RWNGDSYYYP PNYEEIFKDK
     NEPLKSERST VRDSTSSPSI FLNQFKDASN GKGIVLSITE KHIDDTINLI RLLRALNNKL
     PIQIIYFNDI SQSSKTKIIK AAREEINNFP KSYEKVYHGK QPSVPPSPPP PQEVWFVNIY
     ESINPQHRNL FAKFDFKLLA SLFNSFNEFM LIDADTILMK SPEFFFNHQS YQQTGAFFFK
     DRSPLLKRPI TDGEFLIKMG PSSIDSIMFD IPMMTQYTTH RELFKGLRLY MESGLVMIDK
     QRRRHFNSIL MMNQLKFIHP ISNSMWGDKE LFWLGFAING DENYKFNNHF AAAIGQLTSN
     QYNKDRRTPL KSKEICSSHP GHISDEDDRS LLWFNSGFRF CHEANNIDYQ EETKNNVILK
     FLNGRHPLEF KKYYSDPLRI THAIVPPLNK NFQKMYNYDE EPTDGWTSEP NCNKYMWCAY
     SSIGGRTGPE ETSHKETLDG LLVEYTPEEI AYFNYLGDVW VGKY
 
 
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