CYPH_YEAST
ID CYPH_YEAST Reviewed; 162 AA.
AC P14832; D6VSD6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Cyclophilin;
DE Short=CPH;
DE AltName: Full=Cyclosporin A-binding protein;
DE AltName: Full=PPI-II;
DE AltName: Full=Rotamase;
GN Name=CPR1; Synonyms=CPH1, CYP1, SCC1; OrderedLocusNames=YDR155C;
GN ORFNames=YD8358.10C;
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 [MRNA].
RX PubMed=2183184; DOI=10.1093/nar/18.2.373;
RA Dietmeier K., Tropschug M.;
RT "Nucleotide sequence of a full-length cDNA coding for cyclophilin
RT (peptidyl-prolyl cis-trans isomerase) of Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 18:373-373(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-112 AND 120-151,
RP ACETYLATION AT SER-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=2687115; DOI=10.1016/0378-1119(89)90401-0;
RA Haendler B., Keller R., Hiestand P.C., Kocher H.P., Wegmann G., Movva N.R.;
RT "Yeast cyclophilin: isolation and characterization of the protein, cDNA and
RT gene.";
RL Gene 83:39-46(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PARTIAL PROTEIN SEQUENCE OF 2-10; 30-37; 75-78; 81-85 AND 159-162,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8431466; DOI=10.1016/0167-4838(93)90209-a;
RA Hasumi H., Nishikawa T.;
RT "Purification and properties of multiple molecular forms of yeast peptidyl
RT prolyl cis-trans isomerase.";
RL Biochim. Biophys. Acta 1161:161-167(1993).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH HOS2; HST1; SNT1; SIF2; YIL112W AND SET3.
RX PubMed=11711434; DOI=10.1101/gad.207401;
RA Pijnappel W.W.M.P., Schaft D., Roguev A., Shevchenko A., Tekotte H.,
RA Wilm M., Rigaut G., Seraphin B., Aasland R., Stewart A.F.;
RT "The S. cerevisiae SET3 complex includes two histone deacetylases, Hos2 and
RT Hst1, and is a meiotic-specific repressor of the sporulation gene
RT program.";
RL Genes Dev. 15:2991-3004(2001).
RN [8]
RP INTERACTION WITH RPD3.
RX PubMed=10899127; DOI=10.1093/emboj/19.14.3739;
RA Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J.;
RT "Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-
RT Rpd3 histone deacetylase.";
RL EMBO J. 19:3739-3749(2000).
RN [9]
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 [10]
RP FUNCTION.
RX PubMed=11641409; DOI=10.1074/jbc.m109222200;
RA Brown C.R., Cui D.-Y., Hung G.G.-C., Chiang H.-L.;
RT "Cyclophilin A mediates Vid22p function in the import of fructose-1,6-
RT bisphosphatase into Vid vesicles.";
RL J. Biol. Chem. 276:48017-48026(2001).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SET3C COMPLEX, AND
RP INTERACTION WITH SNT1 AND SIF2.
RX PubMed=15643056; DOI=10.1128/ec.4.1.17-29.2005;
RA Arevalo-Rodriguez M., Heitman J.;
RT "Cyclophilin A is localized to the nucleus and controls meiosis in
RT Saccharomyces cerevisiae.";
RL Eukaryot. Cell 4:17-29(2005).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71; SER-142 AND SER-145, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, 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).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-29; LYS-42; LYS-123; LYS-139;
RP LYS-151 AND LYS-158, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
RA Kashima A., Yoshikawa-Fujioka S., Hayano T., Takahashi N., Konno M.;
RT "Turns are essential in the folding of the globular beta-barrel structure
RT of yeast cyclophilin A, CPR1.";
RL Submitted (DEC-2001) to the PDB data bank.
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
RA Konno M., Shibano T., Okudaira K., Takahashi N.;
RT "Crystal structure of yeast cyclophilin A complexed with ACE-Ala-Ala-Pro-
RT Ala-7-amino-4-methylcoumarin.";
RL Submitted (MAR-2004) to the PDB data bank.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. Involved in histone deacetylase complexes, suggesting a
CC function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase)
CC into the intermediate vacuole import and degradation (Vid) vesicles.
CC Regulates the meiotic gene program via the Set3C histone deacetylase
CC complex to promote efficient sporulation, and the prolyl-isomerase
CC activity is required for this function. {ECO:0000269|PubMed:11641409,
CC ECO:0000269|PubMed:15643056, ECO:0000269|PubMed:8431466}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:8431466};
CC -!- ACTIVITY REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC its effects via an inhibitory action on PPIase.
CC -!- SUBUNIT: Interacts with a complex composed of SIN3 and RPD3. Identified
CC in the Set3C complex with HOS2, HST1, SNT1, SIF2, HOS4/YIL112W and
CC SET3. {ECO:0000269|PubMed:10899127, ECO:0000269|PubMed:11711434,
CC ECO:0000269|PubMed:15643056}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15643056}. Nucleus
CC {ECO:0000269|PubMed:15643056}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:22984289}.
CC -!- MISCELLANEOUS: Present with 86000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC subfamily. {ECO:0000305}.
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DR EMBL; X17505; CAA35545.1; -; mRNA.
DR EMBL; M30513; AAA34528.1; -; Genomic_DNA.
DR EMBL; Z50046; CAA90376.1; -; Genomic_DNA.
DR EMBL; AY557665; AAS55991.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11996.1; -; Genomic_DNA.
DR PIR; S25443; CSBY.
DR RefSeq; NP_010439.1; NM_001180462.1.
DR PDB; 1IST; X-ray; 1.90 A; A/B=1-162.
DR PDB; 1VDN; X-ray; 1.60 A; A=1-162.
DR PDBsum; 1IST; -.
DR PDBsum; 1VDN; -.
DR AlphaFoldDB; P14832; -.
DR SMR; P14832; -.
DR BioGRID; 32207; 184.
DR ComplexPortal; CPX-1342; SET3C histone deacetylase complex.
DR DIP; DIP-5203N; -.
DR IntAct; P14832; 82.
DR MINT; P14832; -.
DR STRING; 4932.YDR155C; -.
DR iPTMnet; P14832; -.
DR MaxQB; P14832; -.
DR PaxDb; P14832; -.
DR PRIDE; P14832; -.
DR TopDownProteomics; P14832; -.
DR EnsemblFungi; YDR155C_mRNA; YDR155C; YDR155C.
DR GeneID; 851733; -.
DR KEGG; sce:YDR155C; -.
DR SGD; S000002562; CPR1.
DR VEuPathDB; FungiDB:YDR155C; -.
DR eggNOG; KOG0865; Eukaryota.
DR GeneTree; ENSGT00940000176670; -.
DR HOGENOM; CLU_012062_4_3_1; -.
DR InParanoid; P14832; -.
DR OMA; CSIINSG; -.
DR BioCyc; YEAST:YDR155C-MON; -.
DR ChiTaRS; CPR1; yeast.
DR EvolutionaryTrace; P14832; -.
DR PRO; PR:P14832; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P14832; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0034967; C:Set3 complex; IDA:SGD.
DR GO; GO:0016018; F:cyclosporin A binding; IMP:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:SGD.
DR GO; GO:0030437; P:ascospore formation; IMP:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0009267; P:cellular response to starvation; IC:ComplexPortal.
DR GO; GO:0016575; P:histone deacetylation; IDA:ComplexPortal.
DR GO; GO:0045835; P:negative regulation of meiotic nuclear division; IDA:ComplexPortal.
DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0019538; P:protein metabolic process; IMP:SGD.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Isomerase;
KW Isopeptide bond; Mitochondrion; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Rotamase; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2687115,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..162
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000064132"
FT DOMAIN 5..161
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:2687115,
FT ECO:0000269|PubMed:8431466, ECO:0007744|PubMed:22814378"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 158
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:1VDN"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:1VDN"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1VDN"
FT HELIX 28..39
FT /evidence="ECO:0007829|PDB:1VDN"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1VDN"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1VDN"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1VDN"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1VDN"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:1VDN"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1VDN"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1VDN"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1VDN"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:1VDN"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1VDN"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1VDN"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1VDN"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:1VDN"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:1VDN"
SQ SEQUENCE 162 AA; 17391 MW; 012D8E8E4D85B4B7 CRC64;
MSQVYFDVEA DGQPIGRVVF KLYNDIVPKT AENFRALCTG EKGFGYAGSP FHRVIPDFML
QGGDFTAGNG TGGKSIYGGK FPDENFKKHH DRPGLLSMAN AGPNTNGSQF FITTVPCPWL
DGKHVVFGEV VDGYDIVKKV ESLGSPSGAT KARIVVAKSG EL
