MTC6_CANAW
ID MTC6_CANAW Reviewed; 613 AA.
AC C4YQQ4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Maintenance of telomere capping protein 6;
DE Flags: Precursor;
GN Name=MTC6; ORFNames=CAWG_02814;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
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; CM000310; EEQ44543.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YQQ4; -.
DR STRING; 5476.C4YQQ4; -.
DR EnsemblFungi; EEQ44543; EEQ44543; CAWG_02814.
DR VEuPathDB; FungiDB:CAWG_02814; -.
DR HOGENOM; CLU_033723_0_0_1; -.
DR OMA; NLNESWY; -.
DR Proteomes; UP000001429; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..613
FT /note="Maintenance of telomere capping protein 6"
FT /id="PRO_0000407773"
FT TOPO_DOM 18..557
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
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 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
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 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 479
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 613 AA; 69691 MW; 47BC4CF50D9789D3 CRC64;
MTSLLFAFSL FLSFSVGSIF PFSTSNGPAV NDTLQNAIRS QRDVSKPIPI DRVGFSGVSL
SSFFESEGYS SDSLSNLNGL LKENVDGVMI DLYWNEFTSK WQLCPAPFPN NITYTTASNR
IVDVSWNNKT YKCDPNLSTD NIMSILNSFI RDTNTDVEAN FMHVMYNLKS IHYEKSNQTI
SLENIYKEKN SNLNVVGMDT LNDTVSLLSS YIFTPTLLKQ YQSTSNKYTN SSSSIRYIDS
LNETQAIQDF YSQSTILMPS LQTVLLTQYK RLMVHVVTND MAESSRSYQI SSSDKDTIFF
NSDLPASIFH TDNASADELC YELSDAYNRT DVNIAEFNKV SLNATLRLVV DDDKTPFTTK
SLSKYVRCGY CPIFNSTEYS SQKVTEGNSS IISREFASNL FWSWAPGQPS GPDNCINCTR
PTTNNTSKHS DDNGEEEEGN NIAYKCVALT EEGWEVSNCY EKYLFACQNK LSRNEWKLNN
STKRNYFDID DDDCPEGYFF SLPRSNIEML SLMTTVKQEN VNYPIWIDLN DITVENCFVS
GGPYAQCPYQ ETVTTDKFVR MIAPSFVVAM VVLVLIFIEK VFRKTPIQTN RKRYWKKAIQ
EYYAKNDYEG VPS
