MTC6_CANAL
ID MTC6_CANAL Reviewed; 614 AA.
AC Q5AND1; A0A1D8PK41;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Maintenance of telomere capping protein 6;
DE Flags: Precursor;
GN Name=MTC6; OrderedLocusNames=CAALFM_C305020WA;
GN ORFNames=CaO19.13392, CaO19.5971;
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).
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; CP017625; AOW28517.1; -; Genomic_DNA.
DR RefSeq; XP_723182.1; XM_718089.1.
DR AlphaFoldDB; Q5AND1; -.
DR STRING; 237561.Q5AND1; -.
DR GeneID; 3635170; -.
DR KEGG; cal:CAALFM_C305020WA; -.
DR CGD; CAL0000178984; orf19.13392.
DR VEuPathDB; FungiDB:C3_05020W_A; -.
DR eggNOG; ENOG502QVFP; Eukaryota.
DR HOGENOM; CLU_033723_0_0_1; -.
DR InParanoid; Q5AND1; -.
DR OMA; NLNESWY; -.
DR OrthoDB; 618092at2759; -.
DR PRO; PR:Q5AND1; -.
DR Proteomes; UP000000559; Chromosome 3.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..614
FT /note="Maintenance of telomere capping protein 6"
FT /id="PRO_0000407772"
FT TOPO_DOM 18..558
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..614
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 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 614 AA; 69768 MW; AD1BD65A2A796A2E CRC64;
MTSLLFAFSL FLSFSVGSIF PFSISNGPAV NDTLQNAIRS QRDVSKPIPI DRVGFSGVSL
SLFFESEGYS 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 YELSDAYNGT DVNIAEFNKV SLNATLRLVV DDDKTPFTTK
SLSKYVRCGY CPIFNSTEYS SQKVTEGNSS IISREFASNL FWSWAPGQPS GPDNCINCTR
PTTNNTSKHS DDNGEEEEEG NNIAYKCVAL TEEGWEVSNC YEKYLFACQN KLSRNEWKLN
NSTKRNYFDI DDDDCPEGYF FSLPRSNIEM LSLMTTVKQE NVNYPIWIDL NDITVENCFV
SGGPYAQCPY QETVTTDKFV RMIAPSFVVA MVVLVLIFIE KVFRKTPIQT NRKRYWKKAI
HEYYAKNDYE GVPS
