RCC1_YEAST
ID RCC1_YEAST Reviewed; 482 AA.
AC P21827; D6VU48;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Guanine nucleotide exchange factor SRM1;
DE AltName: Full=Pheromone response pathway component SRM1;
DE AltName: Full=Pre-mRNA-processing protein 20;
DE AltName: Full=Regulator of chromosome condensation;
DE AltName: Full=Suppressor of receptor mutations 1;
DE AltName: Full=mRNA transport protein 1;
GN Name=SRM1; Synonyms=MTR1, PRP20; OrderedLocusNames=YGL097W;
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], AND FUNCTION.
RX PubMed=2548085; DOI=10.1128/mcb.9.6.2682-2694.1989;
RA Clark K.L., Sprague G.F. Jr.;
RT "Yeast pheromone response pathway: characterization of a suppressor that
RT restores mating to receptorless mutants.";
RL Mol. Cell. Biol. 9:2682-2694(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2277633; DOI=10.1007/bf00259453;
RA Aebi M., Clark M.W., Vijayraghavan U., Abelson J.;
RT "A yeast mutant, PRP20, altered in mRNA metabolism and maintenance of the
RT nuclear structure, is defective in a gene homologous to the human gene RCC1
RT which is involved in the control of chromosome condensation.";
RL Mol. Gen. Genet. 224:72-80(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
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 [6]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=2022190; DOI=10.1002/j.1460-2075.1991.tb08068.x;
RA Ohtsubo M., Yoshida T., Seino H., Nishitani H., Clark K.L.,
RA Sprague G.F. Jr., Frasch M., Nishimoto T.;
RT "Mutation of the hamster cell cycle gene RCC1 is complemented by the
RT homologous genes of Drosophila and S.cerevisiae.";
RL EMBO J. 10:1265-1273(1991).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1666302; DOI=10.1091/mbc.2.10.781;
RA Clark K.L., Ohtsubo M., Nishimoto T., Goebl M., Sprague G.F. Jr.;
RT "The yeast SRM1 protein and human RCC1 protein share analogous functions.";
RL Cell Regul. 2:781-792(1991).
RN [8]
RP PHOSPHORYLATION.
RX PubMed=8676864; DOI=10.1007/bf02174449;
RA Fleischmann M., Stagljar I., Aebi M.;
RT "Allele-specific suppression of a Saccharomyces cerevisiae prp20 mutation
RT by overexpression of a nuclear serine/threonine protein kinase.";
RL Mol. Gen. Genet. 250:614-625(1996).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1865879; DOI=10.1007/bf00273932;
RA Fleischmann M., Clark M.W., Forrester W., Wickens M., Nishimoto T.,
RA Aebi M.;
RT "Analysis of yeast prp20 mutations and functional complementation by the
RT human homologue RCC1, a protein involved in the control of chromosome
RT condensation.";
RL Mol. Gen. Genet. 227:417-423(1991).
RN [10]
RP FUNCTION.
RX PubMed=1398069; DOI=10.1101/gad.6.10.1914;
RA Forrester W., Stutz F., Rosbash M., Wickens M.;
RT "Defects in mRNA 3'-end formation, transcription initiation, and mRNA
RT transport associated with the yeast mutation prp20: possible coupling of
RT mRNA processing and chromatin structure.";
RL Genes Dev. 6:1914-1926(1992).
RN [11]
RP FUNCTION.
RX PubMed=7679070; DOI=10.1002/j.1460-2075.1993.tb05649.x;
RA Amberg D.C., Fleischmann M., Stagljar I., Cole C.N., Aebi M.;
RT "Nuclear PRP20 protein is required for mRNA export.";
RL EMBO J. 12:233-241(1993).
RN [12]
RP DNA-BINDING, AND SUBUNIT.
RX PubMed=8270631; DOI=10.1242/jcs.106.1.287;
RA Lee A., Tam R., Belhumeur P., DiPaolo T., Clark M.W.;
RT "Prp20, the Saccharomyces cerevisiae homolog of the regulator of chromosome
RT condensation, RCC1, interacts with double-stranded DNA through a multi-
RT component complex containing GTP-binding proteins.";
RL J. Cell Sci. 106:287-298(1993).
RN [13]
RP FUNCTION.
RX PubMed=8070652; DOI=10.1093/genetics/137.2.381;
RA Kirkpatrick D., Solomon F.;
RT "Overexpression of yeast homologs of the mammalian checkpoint gene RCC1
RT suppresses the class of alpha-tubulin mutations that arrest with excess
RT microtubules.";
RL Genetics 137:381-392(1994).
RN [14]
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 [15]
RP INTERACTION WITH YRB2.
RX PubMed=9395535; DOI=10.1074/jbc.272.50.31877;
RA Taura T., Schlenstedt G., Silver P.A.;
RT "Yrb2p is a nuclear protein that interacts with Prp20p, a yeast Rcc1
RT homologue.";
RL J. Biol. Chem. 272:31877-31884(1997).
RN [16]
RP FUNCTION.
RX PubMed=9971735; DOI=10.1083/jcb.144.3.389;
RA Hurt E.C., Hannus S., Schmelzl B., Lau D.M., Tollervey D., Simos G.;
RT "A novel in vivo assay reveals inhibition of ribosomal nuclear export in
RT ran-cycle and nucleoporin mutants.";
RL J. Cell Biol. 144:389-401(1999).
RN [17]
RP FUNCTION.
RX PubMed=11071906; DOI=10.1091/mbc.11.11.3777;
RA Stage-Zimmermann T., Schmidt U., Silver P.A.;
RT "Factors affecting nuclear export of the 60S ribosomal subunit in vivo.";
RL Mol. Biol. Cell 11:3777-3789(2000).
RN [18]
RP FUNCTION.
RX PubMed=11142374; DOI=10.1017/s1355838200001059;
RA Brodsky A.S., Silver P.A.;
RT "Pre-mRNA processing factors are required for nuclear export.";
RL RNA 6:1737-1749(2000).
RN [19]
RP FUNCTION.
RX PubMed=11509570; DOI=10.1074/jbc.m106060200;
RA Baker R.P., Harreman M.T., Eccleston J.F., Corbett A.H., Stewart M.;
RT "Interaction between Ran and Mog1 is required for efficient nuclear protein
RT import.";
RL J. Biol. Chem. 276:41255-41262(2001).
RN [20]
RP INTERACTION WITH NUP60.
RX PubMed=11535617; DOI=10.1083/jcb.200101007;
RA Denning D.P., Mykytka B., Allen N.P., Huang L., Burlingame A., Rexach M.;
RT "The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p
RT at the nuclear pore complex.";
RL J. Cell Biol. 154:937-950(2001).
RN [21]
RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF LYS-19;
RP LYS-20 AND LYS-23, AND INTERACTION WITH GSP1.
RX PubMed=11523802; DOI=10.1007/s004380100480;
RA Akhtar N., Hagan H., Lopilato J.E., Corbett A.H.;
RT "Functional analysis of the yeast Ran exchange factor Prp20p: in vivo
RT evidence for the RanGTP gradient model.";
RL Mol. Genet. Genomics 265:851-864(2001).
RN [22]
RP FUNCTION.
RX PubMed=11589573; DOI=10.1007/s004380100511;
RA Clement M., Lavallee F., Barbes-Morin G., de Repentigny L., Belhumeur P.;
RT "Overexpression of Bud5p can suppress mutations in the Gsp1p guanine
RT nucleotide exchange factor Prp20p in Saccharomyces cerevisiae.";
RL Mol. Genet. Genomics 266:20-27(2001).
RN [23]
RP FUNCTION, AND MUTAGENESIS OF GLY-282.
RX PubMed=12654904; DOI=10.1083/jcb.200209116;
RA Ryan K.J., McCaffery J.M., Wente S.R.;
RT "The Ran GTPase cycle is required for yeast nuclear pore complex
RT assembly.";
RL J. Cell Biol. 160:1041-1053(2003).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND CHROMATIN-BINDING.
RX PubMed=16365162; DOI=10.1083/jcb.200509061;
RA Dilworth D.J., Tackett A.J., Rogers R.S., Yi E.C., Christmas R.H.,
RA Smith J.J., Siegel A.F., Chait B.T., Wozniak R.W., Aitchison J.D.;
RT "The mobile nucleoporin Nup2p and chromatin-bound Prp20p function in
RT endogenous NPC-mediated transcriptional control.";
RL J. Cell Biol. 171:955-965(2005).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-136, 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-136, 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-136, 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 -!- FUNCTION: Guanine nucleotide exchange factor that promotes the exchange
CC of GSP1/GSP2-bound GDP by GTP and controls RNA metabolism and
CC transport. Involved in yeast pheromone response pathway and in mRNA
CC metabolism. Involved in nuclear pore complex (NPC) assembly and
CC required for mRNA and ribosome nuclear export. Binds chromatin and is
CC involved NPC-mediated transcriptional control.
CC {ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11142374,
CC ECO:0000269|PubMed:11509570, ECO:0000269|PubMed:11589573,
CC ECO:0000269|PubMed:12654904, ECO:0000269|PubMed:1398069,
CC ECO:0000269|PubMed:16365162, ECO:0000269|PubMed:1666302,
CC ECO:0000269|PubMed:1865879, ECO:0000269|PubMed:2277633,
CC ECO:0000269|PubMed:2548085, ECO:0000269|PubMed:7679070,
CC ECO:0000269|PubMed:8070652, ECO:0000269|PubMed:9971735}.
CC -!- SUBUNIT: Component of a multicomponent complex composed of six to seven
CC proteins, which has a collective molecular mass greater than 150 kDa.
CC Interacts with GSP1 and YRB2. {ECO:0000269|PubMed:11523802,
CC ECO:0000269|PubMed:11535617, ECO:0000269|PubMed:8270631,
CC ECO:0000269|PubMed:9395535}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11523802,
CC ECO:0000269|PubMed:16365162, ECO:0000269|PubMed:1666302,
CC ECO:0000269|PubMed:1865879, ECO:0000269|PubMed:2022190}.
CC -!- INDUCTION: By pheromone.
CC -!- PTM: Phosphorylated; possibly by KSP1. {ECO:0000269|PubMed:8676864}.
CC -!- MISCELLANEOUS: Present with 12100 molecules/cell in log phase SD
CC medium. {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; M27013; AAA62268.1; -; Genomic_DNA.
DR EMBL; Z72619; CAA96803.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08009.1; -; Genomic_DNA.
DR PIR; A32320; RGBYM1.
DR RefSeq; NP_011418.1; NM_001180962.1.
DR PDB; 3OF7; X-ray; 1.90 A; A=27-482.
DR PDB; 4OIH; X-ray; 2.10 A; B=1-25.
DR PDB; 5HQ2; X-ray; 4.50 A; K=2-482.
DR PDB; 5T94; X-ray; 2.63 A; A=1-482.
DR PDBsum; 3OF7; -.
DR PDBsum; 4OIH; -.
DR PDBsum; 5HQ2; -.
DR PDBsum; 5T94; -.
DR AlphaFoldDB; P21827; -.
DR SMR; P21827; -.
DR BioGRID; 33153; 359.
DR DIP; DIP-2315N; -.
DR IntAct; P21827; 4.
DR MINT; P21827; -.
DR STRING; 4932.YGL097W; -.
DR iPTMnet; P21827; -.
DR MaxQB; P21827; -.
DR PaxDb; P21827; -.
DR PRIDE; P21827; -.
DR DNASU; 852782; -.
DR EnsemblFungi; YGL097W_mRNA; YGL097W; YGL097W.
DR GeneID; 852782; -.
DR KEGG; sce:YGL097W; -.
DR SGD; S000003065; SRM1.
DR VEuPathDB; FungiDB:YGL097W; -.
DR eggNOG; KOG1426; Eukaryota.
DR GeneTree; ENSGT00940000174254; -.
DR HOGENOM; CLU_005210_4_0_1; -.
DR InParanoid; P21827; -.
DR OMA; WSWGTND; -.
DR BioCyc; YEAST:G3O-30597-MON; -.
DR Reactome; R-SCE-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR EvolutionaryTrace; P21827; -.
DR PRO; PR:P21827; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P21827; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006997; P:nucleus organization; IMP:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IMP:SGD.
DR GO; GO:0006407; P:rRNA export from nucleus; IMP:SGD.
DR Gene3D; 2.130.10.30; -; 1.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR Pfam; PF00415; RCC1; 4.
DR PRINTS; PR00633; RCCNDNSATION.
DR SUPFAM; SSF50985; SSF50985; 1.
DR PROSITE; PS00625; RCC1_1; 1.
DR PROSITE; PS00626; RCC1_2; 1.
DR PROSITE; PS50012; RCC1_3; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division;
KW Guanine-nucleotide releasing factor; Mitosis; Nucleus; Pheromone response;
KW Phosphoprotein; Reference proteome; Repeat; Transport.
FT CHAIN 1..482
FT /note="Guanine nucleotide exchange factor SRM1"
FT /id="PRO_0000206634"
FT REPEAT 45..101
FT /note="RCC1 1"
FT REPEAT 103..152
FT /note="RCC1 2"
FT REPEAT 183..238
FT /note="RCC1 3"
FT REPEAT 239..291
FT /note="RCC1 4"
FT REPEAT 292..347
FT /note="RCC1 5"
FT REPEAT 349..411
FT /note="RCC1 6"
FT REPEAT 412..466
FT /note="RCC1 7"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 15..26
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:11523802"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 19
FT /note="K->T: Impairs correct nuclear localization; when
FT associated with T-20 and T-23."
FT /evidence="ECO:0000269|PubMed:11523802"
FT MUTAGEN 20
FT /note="K->A,Q: Impairs activity."
FT /evidence="ECO:0000269|PubMed:11523802"
FT MUTAGEN 20
FT /note="K->T: Impairs correct nuclear localization; when
FT associated with T-19 and T-23."
FT /evidence="ECO:0000269|PubMed:11523802"
FT MUTAGEN 23
FT /note="K->T: Impairs correct nuclear localization; when
FT associated with T-19 and T-20."
FT /evidence="ECO:0000269|PubMed:11523802"
FT MUTAGEN 282
FT /note="G->S: Leads to temperature-dependent mislocalization
FT of nucleoporins (nups) and the pore-membrane protein
FT POM152."
FT /evidence="ECO:0000269|PubMed:12654904"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:3OF7"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:3OF7"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:3OF7"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:3OF7"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:3OF7"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3OF7"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:3OF7"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:5T94"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:3OF7"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:3OF7"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:3OF7"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:5T94"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:3OF7"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:5T94"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 435..440
FT /evidence="ECO:0007829|PDB:3OF7"
FT TURN 444..448
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 449..456
FT /evidence="ECO:0007829|PDB:3OF7"
FT STRAND 458..467
FT /evidence="ECO:0007829|PDB:3OF7"
FT HELIX 470..481
FT /evidence="ECO:0007829|PDB:3OF7"
SQ SEQUENCE 482 AA; 53014 MW; 04FFC7B9DC7DE535 CRC64;
MVKRTVATNG DASGAHRAKK MSKTHASHII NAQEDYKHMY LSVQPLDIFC WGTGSMCELG
LGPLAKNKEV KRPRLNPFLP RDEAKIISFA VGGMHTLALD EESNVWSWGC NDVGALGRDT
SNAKEQLKDM DADDSSDDED GDLNELESTP AKIPRESFPP LAEGHKVVQL AATDNMSCAL
FSNGEVYAWG TFRCNEGILG FYQDKIKIQK TPWKVPTFSK YNIVQLAPGK DHILFLDEEG
MVFAWGNGQQ NQLGRKVMER FRLKTLDPRP FGLRHVKYIA SGENHCFALT KDNKLVSWGL
NQFGQCGVSE DVEDGALVTK PKRLALPDNV VIRSIAAGEH HSLILSQDGD LYSCGRLDMF
EVGIPKDNLP EYTYKDVHGK ARAVPLPTKL NNVPKFKSVA AGSHHSVAVA QNGIAYSWGF
GETYAVGLGP FEDDTEVPTR IKNTATQDHN IILVGCGGQF SVSGGVKLSD EDAEKRADEM
DD
