PSB6_MOUSE
ID PSB6_MOUSE Reviewed; 238 AA.
AC Q60692; Q3V240; Q60693; Q8BJX9; Q91VH5;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Proteasome subunit beta type-6;
DE EC=3.4.25.1 {ECO:0000250|UniProtKB:P28072};
DE AltName: Full=Low molecular mass protein 19;
DE AltName: Full=Macropain delta chain;
DE AltName: Full=Multicatalytic endopeptidase complex delta chain;
DE AltName: Full=Proteasome delta chain;
DE AltName: Full=Proteasome subunit Y;
DE Flags: Precursor;
GN Name=Psmb6; Synonyms=Lmp19;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS THR-38 AND THR-89.
RC STRAIN=DBA/2J; TISSUE=Liver;
RX PubMed=7797265; DOI=10.1007/bf00164984;
RA Woodward E.C., Monaco J.J.;
RT "Characterization and mapping of the gene encoding mouse proteasome subunit
RT DELTA (Lmp19).";
RL Immunogenetics 42:28-34(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-238.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 209-229, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP FUNCTION.
RX PubMed=16581775; DOI=10.1128/mcb.26.8.2999-3007.2006;
RA Khor B., Bredemeyer A.L., Huang C.-Y., Turnbull I.R., Evans R.,
RA Maggi L.B. Jr., White J.M., Walker L.M., Carnes K., Hess R.A.,
RA Sleckman B.P.;
RT "Proteasome activator PA200 is required for normal spermatogenesis.";
RL Mol. Cell. Biol. 26:2999-3007(2006).
RN [7]
RP INDUCTION BY DITHIOLETHIONE.
RX PubMed=17521679; DOI=10.1016/j.lfs.2007.04.014;
RA Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.;
RT "Tissue specific increase of the catalytic subunits of the 26S proteasome
RT by indirect antioxidant dithiolethione in mice: enhanced activity for
RT degradation of abnormal protein.";
RL Life Sci. 80:2411-2420(2007).
RN [8]
RP IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT,
RP AND FUNCTION.
RX PubMed=22341445; DOI=10.1016/j.cell.2011.12.030;
RA Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M.,
RA Groll M.;
RT "Immuno- and constitutive proteasome crystal structures reveal differences
RT in substrate and inhibitor specificity.";
RL Cell 148:727-738(2012).
CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC proteolytic degradation of most intracellular proteins. This complex
CC plays numerous essential roles within the cell by associating with
CC different regulatory particles. Associated with two 19S regulatory
CC particles, forms the 26S proteasome and thus participates in the ATP-
CC dependent degradation of ubiquitinated proteins. The 26S proteasome
CC plays a key role in the maintenance of protein homeostasis by removing
CC misfolded or damaged proteins that could impair cellular functions, and
CC by removing proteins whose functions are no longer required. Associated
CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC independent protein degradation. This type of proteolysis is required
CC in several pathways including spermatogenesis (20S-PA200 complex) or
CC generation of a subset of MHC class I-presented antigenic peptides
CC (20S-PA28 complex). Within the 20S core complex, PSMB6 displays a
CC peptidylglutamyl-hydrolyzing activity also termed postacidic or
CC caspase-like activity, meaning that the peptides bond hydrolysis occurs
CC directly after acidic residues. {ECO:0000269|PubMed:16581775,
CC ECO:0000269|PubMed:22341445}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000250|UniProtKB:P28072};
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC complex made of 28 subunits that are arranged in four stacked rings.
CC The two outer rings are each formed by seven alpha subunits, and the
CC two inner rings are formed by seven beta subunits. The proteolytic
CC activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
CC {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28072}. Nucleus
CC {ECO:0000250|UniProtKB:P28072}. Note=Translocated from the cytoplasm
CC into the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000250|UniProtKB:P28072}.
CC -!- INDUCTION: Up-regulated by the antioxidant dithiolethione (D3T) in
CC liver, lung and small intestine (at protein level).
CC {ECO:0000269|PubMed:17521679}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA75375.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA75376.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH13897.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE20959.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U13393; AAA75375.1; ALT_INIT; mRNA.
DR EMBL; U13394; AAA75376.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK078437; BAC37272.1; -; mRNA.
DR EMBL; AK132042; BAE20959.1; ALT_FRAME; mRNA.
DR EMBL; AK167123; BAE39271.1; -; mRNA.
DR EMBL; AK167227; BAE39351.1; -; mRNA.
DR EMBL; AL592547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013897; AAH13897.1; ALT_INIT; mRNA.
DR CCDS; CCDS48836.1; -.
DR RefSeq; NP_032972.3; NM_008946.4.
DR PDB; 3UNB; X-ray; 2.90 A; 4/N/b/p=34-238.
DR PDB; 3UNE; X-ray; 3.20 A; 4/N/b/p=34-238.
DR PDBsum; 3UNB; -.
DR PDBsum; 3UNE; -.
DR AlphaFoldDB; Q60692; -.
DR SMR; Q60692; -.
DR BioGRID; 202423; 47.
DR CORUM; Q60692; -.
DR IntAct; Q60692; 6.
DR MINT; Q60692; -.
DR STRING; 10090.ENSMUSP00000018430; -.
DR ChEMBL; CHEMBL1944493; -.
DR MEROPS; T01.010; -.
DR iPTMnet; Q60692; -.
DR PhosphoSitePlus; Q60692; -.
DR SwissPalm; Q60692; -.
DR REPRODUCTION-2DPAGE; Q60692; -.
DR EPD; Q60692; -.
DR jPOST; Q60692; -.
DR MaxQB; Q60692; -.
DR PaxDb; Q60692; -.
DR PeptideAtlas; Q60692; -.
DR PRIDE; Q60692; -.
DR ProteomicsDB; 291538; -.
DR Antibodypedia; 11325; 154 antibodies from 28 providers.
DR DNASU; 19175; -.
DR Ensembl; ENSMUST00000018430; ENSMUSP00000018430; ENSMUSG00000018286.
DR GeneID; 19175; -.
DR KEGG; mmu:19175; -.
DR UCSC; uc007jve.2; mouse.
DR CTD; 5694; -.
DR MGI; MGI:104880; Psmb6.
DR VEuPathDB; HostDB:ENSMUSG00000018286; -.
DR eggNOG; KOG0174; Eukaryota.
DR GeneTree; ENSGT00940000155114; -.
DR HOGENOM; CLU_035750_5_1_1; -.
DR InParanoid; Q60692; -.
DR OMA; HKQAYAI; -.
DR OrthoDB; 1172133at2759; -.
DR PhylomeDB; Q60692; -.
DR TreeFam; TF106221; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 19175; 31 hits in 72 CRISPR screens.
DR ChiTaRS; Psmb6; mouse.
DR PRO; PR:Q60692; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q60692; protein.
DR Bgee; ENSMUSG00000018286; Expressed in saccule of membranous labyrinth and 271 other tissues.
DR Genevisible; Q60692; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR035140; Proteasome_beta6.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF46; PTHR11599:SF46; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Nucleus; Phosphoprotein; Protease; Proteasome; Reference proteome;
KW Threonine protease; Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT PROPEP 2..33
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026615"
FT CHAIN 34..238
FT /note="Proteasome subunit beta type-6"
FT /id="PRO_0000026616"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT MOD_RES 68
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT VARIANT 38
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:7797265"
FT VARIANT 89
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:7797265"
FT CONFLICT 2
FT /note="A -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 6
FT /note="A -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 82..103
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 182..199
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3UNE"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3UNB"
SQ SEQUENCE 238 AA; 25379 MW; 5A4EB82C4374C6FE CRC64;
MAAALAVRRA GSAPAFGPEA LTPDWENREV STGTTIMAVQ FNGGVVLGAD SRTTTGSYIA
NRVTDKLTPI HDHIFCCRSG SAADTQAVAD AVTYQLGFHS IELNEPPLVH TAASLFKEMC
YRYREDLMAG IIIAGWDPQE GGQVYSVPMG GMMVRQSFAI GGSGSSYIYG YVDATYREGM
TKDECLQFTA NALALAMERD GSSGGVIRLA AIQESGVERQ VLLGDQIPKF TIATLPPP
