MTC6_LODEL
ID MTC6_LODEL Reviewed; 616 AA.
AC A5DZQ4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Maintenance of telomere capping protein 6;
DE Flags: Precursor;
GN Name=MTC6; ORFNames=LELG_02841;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH981526; EDK44662.1; -; Genomic_DNA.
DR RefSeq; XP_001526283.1; XM_001526233.1.
DR AlphaFoldDB; A5DZQ4; -.
DR STRING; 379508.A5DZQ4; -.
DR EnsemblFungi; EDK44662; EDK44662; LELG_02841.
DR GeneID; 5233371; -.
DR KEGG; lel:LELG_02841; -.
DR VEuPathDB; FungiDB:LELG_02841; -.
DR eggNOG; ENOG502QVFP; Eukaryota.
DR HOGENOM; CLU_033723_0_0_1; -.
DR InParanoid; A5DZQ4; -.
DR OMA; NLNESWY; -.
DR OrthoDB; 618092at2759; -.
DR Proteomes; UP000001996; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..616
FT /note="Maintenance of telomere capping protein 6"
FT /id="PRO_0000407780"
FT TOPO_DOM 21..564
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..616
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 616 AA; 70317 MW; B58CA00BF34F7F1A CRC64;
MFNLIKIFFL VSLLSKWVFC DESNNSNYNT NTSNTTSNTT SSSISASTIN ITESINTDVI
NVAVRTQRDV SKPIPIDQVG VAGISLNSVF DNQGYTADSL AELTNLLQLG TQVVLLTLYW
NEFTSVWQLC PAPFPQNVTY YLNSLVNVTW NNNTYLCEYG FTTNDIMDTI FEYLQSSNTV
FNVYFMHLLL NLKSIHYEKS NKTIDLENIY APNSRTNIIG NTTLYDTVAP LSPYIFTPDV
LESYQNSEAN STQSNYQQFY AQSNYTFPSL DSVLFLEVKR LLVNVVNNDL VDSRRVYSIT
LRDRSNIFFN NTMPSTTLDT AEADAFCDRV LNSANDIETF NNLSLYTHFR YVTDNNKKRF
TMKGVRRYVK CGLSPVFNAS SYQVTNDSFA QTSNQSYYPT ANESLLDVEV AFEAFIPYNF
WSFAPGQPIM NETTRGNVLS SDANVAYKCV AMNPDGWTVE DCYTEYQYAC KNITSPNDWF
ISTRSRRSYF DIDNDACPDG YNFSLPRLSI EMAALYNVIK KENAEYPVWI DLNDITISTC
FVSGGPYAQC PYQKTVTTKK FIRMIAPSSI VALVILFLIF LENLFRKNQL QTNRKKYWKK
VLSEHYAKHE QEGVPS
