MTC6_ASHGO
ID MTC6_ASHGO Reviewed; 450 AA.
AC Q75AQ7;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Maintenance of telomere capping protein 6;
DE Flags: Precursor;
GN Name=MTC6; OrderedLocusNames=ADL137W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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; AE016817; AAS51783.2; -; Genomic_DNA.
DR RefSeq; NP_983959.2; NM_209312.2.
DR AlphaFoldDB; Q75AQ7; -.
DR STRING; 33169.AAS51783; -.
DR EnsemblFungi; AAS51783; AAS51783; AGOS_ADL137W.
DR GeneID; 4620101; -.
DR KEGG; ago:AGOS_ADL137W; -.
DR eggNOG; ENOG502QVFP; Eukaryota.
DR HOGENOM; CLU_033723_0_0_1; -.
DR InParanoid; Q75AQ7; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR018378; C-type_lectin_CS.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..450
FT /note="Maintenance of telomere capping protein 6"
FT /id="PRO_0000407771"
FT TOPO_DOM 19..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 450 AA; 49856 MW; 39F7A53DA90E1ED0 CRC64;
MGSFLLCLLL VQLQWCLCSN VLDDLLQQTN IAFLSQQDVI GVIPVNQIPL VGVELCSMFE
TVGDGQDTLA AMLQTGVQTL VMDIGYDEDA GGWQMCGRTS LSEGISTVSR QIERLFPTLY
ANLVVLVLRG GAAEAHYEAL RDAIGRVGRW TYSAEKVKAT SPHLNSLLDD QEKRVLVVAL
DDSLCEALGT VAFGPEDVAY VEGNDTIDCS EHTDSWSFIE REFHWTDVRE YVRLGCSPVI
TGKSVANISE LEALVKVAQV WSWGAGEPAL TDANSEMQRC ASLGYDSATE RATWKSTSCR
QNLPVLCQAV NDRYSWLVGT RNLRFDQLNM DSCPSGYKPS VPRTPLEQRE VERYLSEHHP
SDGQYWIYLN SISVEKCWVV GGPETPCPYV ALVSTRNFAA MIVTSSILVL LLLVLIILLD
LVRVPIQDNR RSWKRALGSY SKAETEGVPM