MTC6_YEAST
ID MTC6_YEAST Reviewed; 526 AA.
AC P38849; D3DLA0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Maintenance of telomere capping protein 6;
DE Flags: Precursor;
GN Name=MTC6; OrderedLocusNames=YHR151C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=18845848; DOI=10.1534/genetics.108.092577;
RA Addinall S.G., Downey M., Yu M., Zubko M.K., Dewar J., Leake A.,
RA Hallinan J., Shaw O., James K., Wilkinson D.J., Wipat A., Durocher D.,
RA Lydall D.;
RT "A genomewide suppressor and enhancer analysis of cdc13-1 reveals varied
RT cellular processes influencing telomere capping in Saccharomyces
RT cerevisiae.";
RL Genetics 180:2251-2266(2008).
CC -!- FUNCTION: May be involved in telomere capping.
CC {ECO:0000269|PubMed:18845848}.
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; U10397; AAB68988.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06844.1; -; Genomic_DNA.
DR PIR; S46766; S46766.
DR RefSeq; NP_012021.1; NM_001179282.1.
DR AlphaFoldDB; P38849; -.
DR BioGRID; 36585; 144.
DR DIP; DIP-5623N; -.
DR STRING; 4932.YHR151C; -.
DR iPTMnet; P38849; -.
DR PaxDb; P38849; -.
DR PRIDE; P38849; -.
DR EnsemblFungi; YHR151C_mRNA; YHR151C; YHR151C.
DR GeneID; 856556; -.
DR KEGG; sce:YHR151C; -.
DR SGD; S000001194; MTC6.
DR VEuPathDB; FungiDB:YHR151C; -.
DR eggNOG; ENOG502QVFP; Eukaryota.
DR HOGENOM; CLU_033723_0_0_1; -.
DR InParanoid; P38849; -.
DR OMA; NLNESWY; -.
DR BioCyc; YEAST:G3O-31186-MON; -.
DR PRO; PR:P38849; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38849; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
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..526
FT /note="Maintenance of telomere capping protein 6"
FT /id="PRO_0000202926"
FT TOPO_DOM 21..477
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
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 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 526 AA; 59818 MW; 9089E60A15CCA823 CRC64;
MWILIYLFII WSSLRTWVTA VDSTTTVGDD LNETVSASVW PTMSPQMTVA FRSQRDVMGN
LTIDQLPYVG LNLRRVLLNN ETSMVNEGNN TRLLTLFKSM LSSEANAFVL DLEQYNNDLR
VVDTTLLFSD VLTALQSFIF STQNNLYANI IVLLLNISAP ELDSTEYRHQ NQTLNTTYIL
DKNLGNSFIY KPTDLQSDRA KNNTWNIYGK SSIDGWPTLG SVLYEQKKRL VIGELTDFFN
ETTAPYIFPH DVFHYEQGNS TLDCPSTVEG LTDLSSIHWR FLDSLFNSVD IKEYISCGLS
PIISNSAYVN NVTQLADIIH EGSVWSWDSD QPSVTQSTSK SGSSSGTLEA YNCVLLYYFA
NNETVTWRVG NCYNSNIGLC RYENMAFRWL VRSNKATYFD FDSYQGSKCP DQYSFNIPRS
PLEQRSFIAY MRNSSFSDTQ IWIDLNSISV SNCWVSGGPY ASCPYEKVIS RRNFVTMMVP
ASVCSFALLC IVVYLSVLRV PIYDNRKNWR RVINKISKSE LEGVPS
