ID   MTC6_CANTT              Reviewed;         601 AA.
AC   C5MA32;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Maintenance of telomere capping protein 6;
DE   Flags: Precursor;
GN   Name=MTC6; ORFNames=CTRG_02344;
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: May be involved in telomere capping. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MTC6 family. {ECO:0000305}.
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DR   EMBL; GG692397; EER33526.1; -; Genomic_DNA.
DR   RefSeq; XP_002548047.1; XM_002548001.1.
DR   AlphaFoldDB; C5MA32; -.
DR   STRING; 5482.XP_002548047.1; -.
DR   EnsemblFungi; EER33526; EER33526; CTRG_02344.
DR   GeneID; 8301785; -.
DR   KEGG; ctp:CTRG_02344; -.
DR   VEuPathDB; FungiDB:CTRG_02344; -.
DR   eggNOG; ENOG502QVFP; Eukaryota.
DR   HOGENOM; CLU_033723_0_0_1; -.
DR   OrthoDB; 618092at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..601
FT                   /note="Maintenance of telomere capping protein 6"
FT                   /id="PRO_0000407776"
FT   TOPO_DOM        22..549
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        550..570
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        571..601
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          405..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   601 AA;  67581 MW;  58DAD0D0977372C1 CRC64;
     MKPVYCFSIL ALLQIFTVVV SESNWPTLNF TLEIASRAQR DISKLLPISQ ITTVGISLSS
     IFRNSGYTVD ALSPLYDLLN GGNEAIMIDL YWNEFTSQWQ LCPAPFPSNT TYNMNDVVDL
     SWENNDYQCQ PGLSTENIMG IINSYIRDTN TNIGANFLRI LFNLKSIHYE NSNRTIDLQN
     IYKPSILNPV NIGNDTLNDT IASLGSYIFT PTVLSQYQSD ASHVEKASSG SSINSTQAIS
     YFYNQSNIIV PSLDTVLLSE YKRVSAHISS NELVNSSRVY QFTSYDTDLI FFNDVVPLVV
     ENTTTGVAGR YCNELFNAYN STGVDIETFN NLSLTTRLRF IVDSDENPFT VDTLSKFVRC
     GYSAIFNGTY DVGVNSSSLD FSDEVDEFIP YGFWSWSPGQ PVDLNDTNSD SINNASMSSN
     NTDDSNGNSL AFKCVVLTET GWSVANCYDR HVIACQNSTS RNNWVLQETN KRNYFEIDKG
     DCPEGYTFSI PRSSTEMLSL QATVKQRNVP YPIWLDLNDI TVPNCFVSGG PYAQCPYQRT
     ITTNKFVRMI APSFAVGVVV LVLILIENIF RTNPIQTNRK RYWKKAIQEY YNKNDFEGVP
     S