CEX1_YEAST
ID CEX1_YEAST Reviewed; 761 AA.
AC Q12453; D6W2H1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cytoplasmic export protein 1;
GN Name=CEX1; OrderedLocusNames=YOR112W; ORFNames=O3240, YOR3240w;
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=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [3]
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 [4]
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 [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 FUNCTION, TRNA-BINDING, ASSOCIATION WITH THE NUCLEAR PORE COMPLEX, AND
RP INTERACTION WITH GSP1; LOS1; MSN5; NUPP116 AND TEF2.
RX PubMed=17203074; DOI=10.1038/sj.emboj.7601493;
RA McGuire A.T., Mangroo D.;
RT "Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae
RT nuclear tRNA export machinery.";
RL EMBO J. 26:288-300(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND IDENTIFICATION BY
RP 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 -!- FUNCTION: Component of the nuclear tRNA export machinery that my
CC collect tRNA from the nuclear tRNA export receptors of the
CC aminoacylation-dependent export and may deliver aminoacylated tRNAs to
CC the translation machinery pathway at the nuclear pore complex.
CC {ECO:0000269|PubMed:17203074}.
CC -!- SUBUNIT: Associates with the nuclear pore complex (NPC). Interacts with
CC GSP1, LOS1, MSN5, NUP116 and TEF2. {ECO:0000269|PubMed:17203074}.
CC -!- INTERACTION:
CC Q12453; P33418: LOS1; NbExp=2; IntAct=EBI-31271, EBI-10188;
CC Q12453; Q02630: NUP116; NbExp=4; IntAct=EBI-31271, EBI-11703;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X94335; CAA64032.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62113.1; -; Genomic_DNA.
DR EMBL; Z75020; CAA99310.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10887.1; -; Genomic_DNA.
DR PIR; S60992; S60992.
DR RefSeq; NP_014755.1; NM_001183531.1.
DR PDB; 3VWA; X-ray; 2.20 A; A/B=9-564.
DR PDBsum; 3VWA; -.
DR AlphaFoldDB; Q12453; -.
DR SMR; Q12453; -.
DR BioGRID; 34508; 93.
DR DIP; DIP-4149N; -.
DR IntAct; Q12453; 8.
DR MINT; Q12453; -.
DR STRING; 4932.YOR112W; -.
DR iPTMnet; Q12453; -.
DR MaxQB; Q12453; -.
DR PaxDb; Q12453; -.
DR PRIDE; Q12453; -.
DR EnsemblFungi; YOR112W_mRNA; YOR112W; YOR112W.
DR GeneID; 854279; -.
DR KEGG; sce:YOR112W; -.
DR SGD; S000005638; CEX1.
DR VEuPathDB; FungiDB:YOR112W; -.
DR eggNOG; KOG1243; Eukaryota.
DR GeneTree; ENSGT00930000151054; -.
DR HOGENOM; CLU_010392_2_0_1; -.
DR InParanoid; Q12453; -.
DR OMA; KFMHEAK; -.
DR BioCyc; YEAST:G3O-33641-MON; -.
DR PRO; PR:Q12453; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12453; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IDA:SGD.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..761
FT /note="Cytoplasmic export protein 1"
FT /id="PRO_0000237655"
FT REPEAT 385..423
FT /note="HEAT 1"
FT REPEAT 498..534
FT /note="HEAT 2"
FT REGION 660..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:3VWA"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:3VWA"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:3VWA"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:3VWA"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:3VWA"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:3VWA"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:3VWA"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3VWA"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 110..126
FT /evidence="ECO:0007829|PDB:3VWA"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3VWA"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:3VWA"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3VWA"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:3VWA"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:3VWA"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 259..275
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 292..307
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 325..339
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 346..355
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 359..372
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 378..384
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 398..411
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 417..421
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 423..431
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 437..450
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:3VWA"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 458..473
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 478..491
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 497..502
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 504..508
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 509..513
FT /evidence="ECO:0007829|PDB:3VWA"
FT HELIX 517..540
FT /evidence="ECO:0007829|PDB:3VWA"
SQ SEQUENCE 761 AA; 84769 MW; 0B0D2DA036F5AE5B CRC64;
MNFSSIFKSI SNFQFPYTIE ETAITETALW QCFDGTRKAD SLPVTVFKAK RSPENESLIL
NAVHKSKILK IPGLCTVLET FDSDPQSTFI VTERVVPFPW DNLGSLSQNK FGVELGISQL
LATLGFLKNF VLGTLSKDSV FINIKGEWVL FGLELCSSKE GLSAFEFASR ARSYYNIIGS
QLPCEDPNTI DSMGLGLLIK SLMAPSCLPK DWIVNVNMIS DGKITIENFR KRLENTETWR
SNPLINFYQE LRELHIKDPQ GKLVVMSNLE NLYLESREIF RNLTPGMIEN FIIPELCEII
KLLMTQSISS AASPIGMNFN ASHKLVPFLA IVLDLTSETN TFPVGFNDLI TQSFKLPDRQ
VRFLLLIYLP KLIGPLSKSE ISSRIYPHFI QGLTDSDATL RLQTLKTIPC IVSCLTERQL
NNELLRFLAK TQVDSDVEIR TWTVIIISKI STILSTSVGN RSNILATAFT KSLKDPQVKP
RLAALYGLEK SIELFDVNTI ANKILTVIAP GLLDKSPIVR GRAKILFEEY LEKLEKEAQL
IQTNDSTADS EDVKDIDFEN YGCDEEDMNK EDNLLAAQFL NNLRLNSPSA TTPSNITESE
IDSAQDGSGW DDLSDTDGFI TNGTTESFDE TTNPVTTAST PKLFGKPIKI NKSWNDELND
DGWIQDESGP SKVPQKHTRP QNSTLAKSIA PSSRLSIKKK KTTILAPRNI ASNSTVTTKS
SLSNKTARSK PISSIRGSVT KKGNVDGWDD DGDSDSWDTN W
