PSB1_MOUSE
ID PSB1_MOUSE Reviewed; 240 AA.
AC O09061; Q62038; Q62039;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Proteasome subunit beta type-1;
DE AltName: Full=Macropain subunit C5;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C5;
DE AltName: Full=Proteasome component C5;
DE AltName: Full=Proteasome gamma chain;
DE Flags: Precursor;
GN Name=Psmb1;
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 [MRNA].
RC STRAIN=C57BL/10J; TISSUE=Brain, and Testis;
RX PubMed=7579585; DOI=10.3109/10425179509030985;
RA Savioz A., Houghton I., Davies R.W.;
RT "Cloning and sequencing of a murine cDNA encoding the proteasome component
RT C5.";
RL DNA Seq. 5:307-309(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP PROTEIN SEQUENCE OF 77-93; 109-126; 146-159; 164-197 AND 204-212, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH RFPL4A.
RX PubMed=12525704; DOI=10.1073/pnas.0234474100;
RA Suzumori N., Burns K.H., Yan W., Matzuk M.M.;
RT "RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome
RT degradation pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:550-555(2003).
RN [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-149, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
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 GLYCOSYLATION AT SER-57 AND SER-208.
RC TISSUE=Brain, and Spleen;
RX PubMed=22556278; DOI=10.1074/mcp.m111.015966;
RA Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A.,
RA Siele D., Kloetzel P.M., Janek K.;
RT "Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel
RT biotin-cystamine tag.";
RL Mol. Cell. Proteomics 11:467-477(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT,
RP FUNCTION, AND TISSUE SPECIFICITY.
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: Non-catalytic component of the 20S core proteasome complex
CC involved in the proteolytic degradation of most intracellular proteins.
CC This complex plays numerous essential roles within the cell by
CC associating with different regulatory particles. Associated with two
CC 19S regulatory particles, forms the 26S proteasome and thus
CC participates in the ATP-dependent degradation of ubiquitinated
CC proteins. The 26S proteasome plays a key role in the maintenance of
CC protein homeostasis by removing misfolded or damaged proteins that
CC could impair cellular functions, and by removing proteins whose
CC functions are no longer required. Associated with the PA200 or PA28,
CC the 20S proteasome mediates ubiquitin-independent protein degradation.
CC This type of proteolysis is required in several pathways including
CC spermatogenesis (20S-PA200 complex) or generation of a subset of MHC
CC class I-presented antigenic peptides (20S-PA28 complex).
CC {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}.
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 (PubMed:16857966, PubMed:22341445). Interacts with SERPINB2 (By
CC similarity). Interacts with RFPL4A (PubMed:12525704).
CC {ECO:0000250|UniProtKB:P20618, ECO:0000269|PubMed:12525704,
CC ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20618}. Nucleus
CC {ECO:0000250|UniProtKB:P20618}. 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:P20618}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22341445}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA56702.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U60824; AAB37251.1; -; mRNA.
DR EMBL; X80686; CAA56701.1; -; mRNA.
DR EMBL; X80686; CAA56702.1; ALT_INIT; mRNA.
DR EMBL; AK077520; BAC36841.1; -; mRNA.
DR EMBL; BC018351; AAH18351.1; -; mRNA.
DR CCDS; CCDS28411.1; -.
DR RefSeq; NP_035315.1; NM_011185.3.
DR PDB; 3UNB; X-ray; 2.90 A; 2/L/Z/n=28-240.
DR PDB; 3UNE; X-ray; 3.20 A; 2/L/Z/n=28-240.
DR PDB; 3UNF; X-ray; 2.90 A; L/Z=28-240.
DR PDB; 3UNH; X-ray; 3.20 A; L/Z=28-240.
DR PDB; 5L65; X-ray; 2.90 A; L/Z=123-137, L/Z=144-159.
DR PDB; 5L66; X-ray; 2.80 A; L/Z=123-137, L/Z=144-159.
DR PDB; 5L67; X-ray; 2.60 A; L/Z=123-137, L/Z=144-159.
DR PDB; 5L68; X-ray; 2.80 A; L/Z=123-137, L/Z=144-159.
DR PDB; 5L69; X-ray; 2.70 A; L/Z=123-137, L/Z=144-159.
DR PDB; 5L6A; X-ray; 2.80 A; L/Z=123-137, L/Z=144-159.
DR PDB; 5L6B; X-ray; 2.60 A; L/Z=123-137, L/Z=144-159.
DR PDB; 5L6C; X-ray; 2.60 A; L/Z=123-137, L/Z=144-159.
DR PDBsum; 3UNB; -.
DR PDBsum; 3UNE; -.
DR PDBsum; 3UNF; -.
DR PDBsum; 3UNH; -.
DR PDBsum; 5L65; -.
DR PDBsum; 5L66; -.
DR PDBsum; 5L67; -.
DR PDBsum; 5L68; -.
DR PDBsum; 5L69; -.
DR PDBsum; 5L6A; -.
DR PDBsum; 5L6B; -.
DR PDBsum; 5L6C; -.
DR AlphaFoldDB; O09061; -.
DR SMR; O09061; -.
DR BioGRID; 202418; 52.
DR CORUM; O09061; -.
DR IntAct; O09061; 6.
DR MINT; O09061; -.
DR STRING; 10090.ENSMUSP00000014913; -.
DR BindingDB; O09061; -.
DR ChEMBL; CHEMBL4523121; -.
DR GlyGen; O09061; 2 sites.
DR iPTMnet; O09061; -.
DR PhosphoSitePlus; O09061; -.
DR SwissPalm; O09061; -.
DR CPTAC; non-CPTAC-3943; -.
DR EPD; O09061; -.
DR jPOST; O09061; -.
DR PaxDb; O09061; -.
DR PeptideAtlas; O09061; -.
DR PRIDE; O09061; -.
DR ProteomicsDB; 291607; -.
DR Antibodypedia; 33582; 238 antibodies from 32 providers.
DR DNASU; 19170; -.
DR Ensembl; ENSMUST00000014913; ENSMUSP00000014913; ENSMUSG00000014769.
DR GeneID; 19170; -.
DR KEGG; mmu:19170; -.
DR UCSC; uc008aol.1; mouse.
DR CTD; 5689; -.
DR MGI; MGI:104884; Psmb1.
DR VEuPathDB; HostDB:ENSMUSG00000014769; -.
DR eggNOG; KOG0179; Eukaryota.
DR GeneTree; ENSGT00550000075035; -.
DR HOGENOM; CLU_035750_1_1_1; -.
DR InParanoid; O09061; -.
DR OMA; IGFKNMQ; -.
DR OrthoDB; 1092660at2759; -.
DR PhylomeDB; O09061; -.
DR TreeFam; TF106218; -.
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-6798695; Neutrophil degranulation.
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; 19170; 32 hits in 73 CRISPR screens.
DR ChiTaRS; Psmb1; mouse.
DR PRO; PR:O09061; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O09061; protein.
DR Bgee; ENSMUSG00000014769; Expressed in medial ganglionic eminence and 267 other tissues.
DR ExpressionAtlas; O09061; baseline and differential.
DR Genevisible; O09061; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR035202; Proteasome_beta1.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF59; PTHR11599:SF59; 1.
DR Pfam; PF00227; Proteasome; 1.
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;
KW Glycoprotein; Nucleus; Phosphoprotein; Proteasome; Reference proteome.
FT PROPEP 1..27
FT /evidence="ECO:0000250"
FT /id="PRO_0000259624"
FT CHAIN 28..240
FT /note="Proteasome subunit beta type-1"
FT /id="PRO_0000148031"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P20618"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20618"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20618"
FT MOD_RES 149
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20618"
FT MOD_RES 203
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20618"
FT CARBOHYD 57
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:22556278"
FT CARBOHYD 208
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:22556278"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 85..106
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:5L67"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:5L67"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3UNE"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 195..212
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:3UNB"
SQ SEQUENCE 240 AA; 26372 MW; 22ADBC6ACB3A8D31 CRC64;
MLSTAAYRDV ERELGMGPHG SAGPVQLRFS PYAFNGGTVL AIAGEDFSIV ASDTRLSEGF
SIHTRDSPKC YKLTDKTVIG CSGFHGDCLT LTKIIEARLK MYKHSNNKAM TTGAIAAMLS
TILYSRRFFP YYVYNIIGGL DEEGKGAVYS FDPVGSYQRD SFKAGGSASA MLQPLLDNQV
GFKNMQNVEH VPLTLDRAMR LVKDVFISAA ERDVYTGDAL RICIVTKEGI REETVPLRKD
