RTC1_YEAST
ID RTC1_YEAST Reviewed; 1341 AA.
AC Q08281; D6W1T1; Q92271;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Restriction of telomere capping protein 1;
DE AltName: Full=SEH-associated protein 2;
GN Name=RTC1; Synonyms=SEA2; OrderedLocusNames=YOL138C;
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 96604 / S288c / FY1679;
RX PubMed=8896270;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1053::aid-yea993>3.0.co;2-s;
RA Aldea M., Piedrafita L., Casas C., Casamayor A., Khalid H., Balcells L.,
RA Arino J., Herrero E.;
RT "Sequence analysis of a 12 801 bp fragment of the left arm of yeast
RT chromosome XV containing a putative 6-phosphofructo-2-kinase gene, a gene
RT for a possible glycophospholipid-anchored surface protein and six other
RT open reading frames.";
RL Yeast 12:1053-1058(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 393 AND 548.
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 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 [5]
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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=15161972; DOI=10.1073/pnas.0401263101;
RA Askree S.H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C.,
RA Krauskopf A., Kupiec M., McEachern M.J.;
RT "A genome-wide screen for Saccharomyces cerevisiae deletion mutants that
RT affect telomere length.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8658-8663(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RIBOSOMES.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1036 AND SER-1123, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1036; SER-1080; SER-1087;
RP SER-1089; SER-1123 AND SER-1133, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1036; SER-1080; SER-1089 AND
RP SER-1123, AND 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).
RN [13]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEA COMPLEX, AND FUNCTION.
RX PubMed=21454883; DOI=10.1074/mcp.m110.006478;
RA Dokudovskaya S., Waharte F., Schlessinger A., Pieper U., Devos D.P.,
RA Cristea I.M., Williams R., Salamero J., Chait B.T., Sali A., Field M.C.,
RA Rout M.P., Dargemont C.;
RT "A conserved coatomer-related complex containing Sec13 and Seh1 dynamically
RT associates with the vacuole in Saccharomyces cerevisiae.";
RL Mol. Cell. Proteomics 10:M110.006478.1-M110.006478.17(2011).
CC -!- FUNCTION: Component of the SEA complex which coats the vacuolar
CC membrane and is involved in intracellular trafficking, autophagy,
CC response to nitrogen starvation, and amino acid biogenesis. May be
CC involved in a process influencing telomere capping.
CC {ECO:0000269|PubMed:18845848, ECO:0000269|PubMed:21454883}.
CC -!- SUBUNIT: Component of the SEA complex composed of at least IML1/SEA1,
CC RTC1/SEA2, MTC5/SEA3, NPR2, NPR3, SEA4, SEC13 and SEH1. Interacts with
CC ribosomes. {ECO:0000269|PubMed:16702403, ECO:0000269|PubMed:21454883}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:21454883}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21454883}.
CC -!- DISRUPTION PHENOTYPE: Leads to short telomeres.
CC {ECO:0000269|PubMed:15161972}.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat RTC1 family. {ECO:0000305}.
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DR EMBL; X95465; CAA64732.1; -; Genomic_DNA.
DR EMBL; Z74880; CAA99159.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10647.2; -; Genomic_DNA.
DR PIR; S66835; S66835.
DR RefSeq; NP_014503.2; NM_001183392.2.
DR AlphaFoldDB; Q08281; -.
DR SMR; Q08281; -.
DR BioGRID; 34238; 239.
DR ComplexPortal; CPX-3231; SEA complex.
DR IntAct; Q08281; 42.
DR MINT; Q08281; -.
DR STRING; 4932.YOL138C; -.
DR iPTMnet; Q08281; -.
DR MaxQB; Q08281; -.
DR PaxDb; Q08281; -.
DR PRIDE; Q08281; -.
DR EnsemblFungi; YOL138C_mRNA; YOL138C; YOL138C.
DR GeneID; 853982; -.
DR KEGG; sce:YOL138C; -.
DR SGD; S000005498; RTC1.
DR VEuPathDB; FungiDB:YOL138C; -.
DR eggNOG; KOG0269; Eukaryota.
DR GeneTree; ENSGT00940000159396; -.
DR HOGENOM; CLU_008512_0_0_1; -.
DR InParanoid; Q08281; -.
DR OMA; GGRDGKC; -.
DR BioCyc; YEAST:G3O-33531-MON; -.
DR PRO; PR:Q08281; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08281; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0097042; C:extrinsic component of fungal-type vacuolar membrane; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0061700; C:GATOR2 complex; IBA:GO_Central.
DR GO; GO:0035859; C:Seh1-associated complex; IDA:SGD.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034198; P:cellular response to amino acid starvation; IBA:GO_Central.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; IGI:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903432; P:regulation of TORC1 signaling; IDA:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR037590; WDR24.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46200; PTHR46200; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Membrane; Metal-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Vacuole; WD repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..1341
FT /note="Restriction of telomere capping protein 1"
FT /id="PRO_0000223528"
FT REPEAT 207..248
FT /note="WD 1"
FT REPEAT 256..296
FT /note="WD 2"
FT REPEAT 305..342
FT /note="WD 3"
FT REPEAT 367..406
FT /note="WD 4"
FT REPEAT 439..486
FT /note="WD 5"
FT REPEAT 489..527
FT /note="WD 6"
FT REPEAT 843..883
FT /note="WD 7"
FT REPEAT 1129..1169
FT /note="WD 8"
FT REPEAT 1216..1255
FT /note="WD 9"
FT ZN_FING 1293..1335
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..765
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1080
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1089
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 393
FT /note="C -> S (in Ref. 1; CAA64732 and 2; CAA99159)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="D -> G (in Ref. 1; CAA64732 and 2; CAA99159)"
FT /evidence="ECO:0000305"
FT CONFLICT 1222
FT /note="D -> DV (in Ref. 1; CAA64732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1341 AA; 149344 MW; 45B62E3D341397AA CRC64;
MSLSPHVENA SIPKGSTPIP KNRNVSSIGK GEFLGSSSSN NSSFRMNHYS NSGQPSVLDS
IRRPNLTPTF SYSNGVYMPE SHRTSSFNDS YLPYDKNPYA KTTGSMSNKS NMKIKTKKNA
INTNTRKSSG LIYTTKVDKE LSSIDKVNDP NINGLVCAGK THLGLYKFSP SDRSIKCVHD
FITPNSNTST RGTTSLLPKL SKRTRQNKFS TIADVKTGFN NYKNCIAVCN NSTAISIYDL
NKSSSIDNPL ITSLCEHTRS INSFDFNMVE SNLIISGGQD SCVKIWDLRS NKSKSSNRSD
ISINTASDSI RDVKWMPGYN FASKNDQGSS TYGNLKSGYK FASIHDSGYL LKFDLRQPAQ
YEKKLNAHTG PGLCLNWHPN QEYIATGGRD GKCCLWFVGD NANAAENTVL NYGNSPSLHA
PNTSLNNSGS LAFPKLTINT GYPVTKLKFK PAYSSNIYNS LLGISSMGDE AEVRIYSLAR
KYIPKHVLLS ETPSLGLVWW DENLIFNIDK GTRINGWDIN KEPTVLENLS KNTTTWRDLD
GNGLLSVDQE IGSYEVVEPE LQPTSSTTCK KHPGTIKNPK NGNPENQGII GGIKKGFSHT
GLTSFTPERP PTLKAGPTFS TKSLTLASGA SSFNSSSASL TSLTPQTENR EEIAIEPPCI
ITLDIPQIFN NIRLTKIAHS RKKNVISESS SMKNSPVEKF KYLARQLKFS YIREHNVSDS
ADTAYKNDIE NIDVVKNATE THGDNTTTTN NNDDGDDDDD DDDDDKIIES HLLKKYNFPE
NNTWATLMNE KVNNKKSKRN SSSSREFDEK DVRSSISSIS ASRQSHDRAR KIDKNVEAEL
QEKIQTLVDL ISIATHNASV YLSIDDLTNF KIWILIRDSL LWDLKWMTSS QISSDNASNM
DANESSDFEA GENLKTGKEF PEEDGAGTSG AESLVEERPQ AFRANSDEPS DAEKKPVSKL
KEQLKNTEII PYAQPNEDSD EVLTKLKELQ NQRLESRTKM GETVSDDVII EEDEHEHQEE
EQPHDSPTKS AQFHASPIAK SIPILQKREH RKSFIDTFML HSPNGYNGDT DIGNEDDNIS
PRFTYNSVSP RSKVSSLQSY ATTTSQLETF KKLSSHTAPI IGSPRHAPSR PDSIGREQLS
SSLTKKLAKC KKIIADPPWD TKKLIKQLYN QATETGNVVL TVNILFLFQT IYQITEIDIA
KDAIAHFLLL LHRYELFGIA ADVLKYCPFE DIMGSEGDQS SIRLFCERCG ELITNESSKE
KLRAEAQQTG NKKIMDKFGY WYCDSCKKKN TSCVLCERPL KKLTMVILPC GHEGHFQCIQ
EWFLDENEQE CPGGCPGVAF I
