MTC4_YEAST
ID MTC4_YEAST Reviewed; 694 AA.
AC P38335; D6VQQ1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Maintenance of telomere capping protein 4;
GN Name=MTC4; OrderedLocusNames=YBR255W; ORFNames=YBR1723;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8465606; DOI=10.1002/yea.320090210;
RA Doignon F., Biteau N., Crouzet M., Aigle M.;
RT "The complete sequence of a 19,482 bp segment located on the right arm of
RT chromosome II from Saccharomyces cerevisiae.";
RL Yeast 9:189-199(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=10206193;
RX DOI=10.1002/(sici)1097-0061(19990315)15:4<351::aid-yea364>3.0.co;2-l;
RA Sanjuan R., Leon M., Zueco J., Sentandreu R.;
RT "Basic phenotypic analysis of six novel yeast genes reveals two essential
RT genes and one which affects the growth rate.";
RL Yeast 15:351-360(1999).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP GENE NAME, AND DISRUPTION PHENOTYPE.
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; THR-263 AND SER-481, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481; SER-491 AND TYR-493, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Note=Punctate pattern.
CC -!- DISRUPTION PHENOTYPE: Shows a slower growth rate on YPD and minimal
CC medium at 15 degrees Celsius. Synthetically sick with temperature-
CC sensitive CDC13-1 mutant. {ECO:0000269|PubMed:10206193,
CC ECO:0000269|PubMed:18845848}.
CC -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; X70529; CAA49919.1; -; Genomic_DNA.
DR EMBL; Z36124; CAA85218.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07371.1; -; Genomic_DNA.
DR PIR; S32958; S32958.
DR RefSeq; NP_009814.3; NM_001178603.3.
DR AlphaFoldDB; P38335; -.
DR SMR; P38335; -.
DR BioGRID; 32950; 223.
DR DIP; DIP-5655N; -.
DR IntAct; P38335; 1.
DR MINT; P38335; -.
DR STRING; 4932.YBR255W; -.
DR iPTMnet; P38335; -.
DR MaxQB; P38335; -.
DR PaxDb; P38335; -.
DR PRIDE; P38335; -.
DR EnsemblFungi; YBR255W_mRNA; YBR255W; YBR255W.
DR GeneID; 852557; -.
DR KEGG; sce:YBR255W; -.
DR SGD; S000000459; MTC4.
DR VEuPathDB; FungiDB:YBR255W; -.
DR eggNOG; ENOG502QXZI; Eukaryota.
DR HOGENOM; CLU_025639_0_0_1; -.
DR InParanoid; P38335; -.
DR OMA; RTSHWDE; -.
DR BioCyc; YEAST:G3O-29180-MON; -.
DR PRO; PR:P38335; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38335; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR InterPro; IPR038769; MTC4.
DR PANTHER; PTHR38426; PTHR38426; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..694
FT /note="Maintenance of telomere capping protein 4"
FT /id="PRO_0000202525"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..243
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 263
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 493
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 694 AA; 79028 MW; 63CB9058F76DD659 CRC64;
MTHTNEHDHK AEQQQNGRGD TTTETVNPQK MKLVTKLLID NKFGLMDDLN FSIPLTASSE
GVPISAKTSE LGTEYLKNQQ ENSVSPILPI SRSTRIKADR VRIYLDYYYN ILERCISIDS
SQNHHEGVEG VYNPLQVIRN RKLKKKHHEL PTREFYTTKH PIIAIKQFSK KPNKKMPWFV
DINEKYMDLT WRTSHWEELV DPQGKLWFQS YSPSNESSGS SSSRRHHGHH IHPRRHLQHH
SRVRTANSVH SNTQSLTPKR VMTNEEDNNN HNNNNMITKI ATTPEAQISR NKKSDLNLSH
IHLEVPITNT VTNTSSDQGS LIIEAKGSSY GGDRRGSSNT SGSGGKRNSK HYRSKSAGPP
ENEKSRMNGL EKIISKTSKG WSRSPKKNTP GLEKQVLLNP TISNGGTSRR SSNNGESIST
NSSKSSMGIT FGNTETYKTP VDNGKDAIIR QSLLSEVPVH TLRGKTSNRS LRAEGEQALE
SDKELPNGAG SIYEGAPREK TTSQGSEPVG LVSDSLQVDE QLQRYWHDTR YIMSTVAMMQ
HRRETHDIVK RREIARRNEI EITQDADTNI RKTADALTQY DNELNKVLKL GNDWTSKLLN
DYSIRVETLI SSSDRILSDI NTTLTLKLKM FQENTERYVT VKVMRAQKMT KTIYRLLEFG
IVLVLWTIWF LFSVLRSIRF TIFLVLKIIK ALLW
