PSB4_MOUSE
ID PSB4_MOUSE Reviewed; 264 AA.
AC P99026; Q3THC0; Q3THI3; Q3U0S0; Q3UVQ4; Q62008; Q8BK27; Q91VV7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Proteasome subunit beta type-4;
DE AltName: Full=Low molecular mass protein 3;
DE AltName: Full=Macropain beta chain;
DE AltName: Full=Multicatalytic endopeptidase complex beta chain;
DE AltName: Full=Proteasome beta chain;
DE AltName: Full=Proteasome chain 3;
DE Flags: Precursor;
GN Name=Psmb4; Synonyms=Lmp3;
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=B10.A; TISSUE=Macrophage;
RX PubMed=9197541; DOI=10.1016/s0378-1119(97)00003-6;
RA Cruz M., Nandi D., Hendil K.B., Monaco J.J.;
RT "Cloning and characterization of mouse Lmp3 cDNA, encoding a proteasome
RT beta subunit.";
RL Gene 190:251-256(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD; TISSUE=Spleen;
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=NMRI; 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 [4]
RP PROTEIN SEQUENCE OF 46-80; 110-131 AND 232-240, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 46-51.
RC TISSUE=Liver;
RA Sanchez J.-C., Rouge V., Frutiger S., Hughes G., Yan J.X., Hoogland C.,
RA Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.;
RL Submitted (AUG-1998) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 95-112.
RC STRAIN=C57BL/6J;
RA Wang B., Hunsperger J., Laib J., Fan D.;
RL Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=12874245; DOI=10.4049/jimmunol.171.3.1515;
RA Qureshi N., Perera P.-Y., Shen J., Zhang G., Lenschat A., Splitter G.,
RA Morrison D.C., Vogel S.N.;
RT "The proteasome as a lipopolysaccharide-binding protein in macrophages:
RT differential effects of proteasome inhibition on lipopolysaccharide-induced
RT signaling events.";
RL J. Immunol. 171:1515-1525(2003).
RN [8]
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 [9]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16317774; DOI=10.1002/pmic.200500218;
RA Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X.,
RA Zhang X., Yang X.;
RT "The up-regulation of proteasome subunits and lysosomal proteases in
RT hepatocellular carcinomas of the HBx gene knockin transgenic mice.";
RL Proteomics 6:498-504(2006).
RN [10]
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 [11]
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 [12]
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 SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300
CC repressor SNIP1. {ECO:0000269|PubMed:12874245,
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). Forms a ternary complex with SMAD1
CC and OAZ1 before PSMB4 is incorporated into the 20S proteasome (By
CC similarity). Interacts with PRPF19 (By similarity).
CC {ECO:0000250|UniProtKB:P28070, ECO:0000269|PubMed:16857966,
CC ECO:0000269|PubMed:22341445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28070}. Nucleus
CC {ECO:0000250|UniProtKB:P28070}. 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:P28070}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22341445}.
CC -!- INDUCTION: Up-regulated in liver tumor tissues (at protein level).
CC {ECO:0000269|PubMed:16317774}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; U65636; AAC53263.1; -; mRNA.
DR EMBL; AK077448; BAC36805.1; -; mRNA.
DR EMBL; AK137044; BAE23215.1; -; mRNA.
DR EMBL; AK156624; BAE33781.1; -; mRNA.
DR EMBL; AK168265; BAE40213.1; -; mRNA.
DR EMBL; AK168340; BAE40277.1; -; mRNA.
DR EMBL; BC008241; AAH08241.1; -; mRNA.
DR EMBL; M74556; AAA39863.1; -; mRNA.
DR CCDS; CCDS17597.1; -.
DR RefSeq; NP_032971.2; NM_008945.3.
DR PDB; 3UNB; X-ray; 2.90 A; 3/M/a/o=46-264.
DR PDB; 3UNE; X-ray; 3.20 A; 3/M/a/o=46-264.
DR PDB; 3UNF; X-ray; 2.90 A; M/a=46-264.
DR PDB; 3UNH; X-ray; 3.20 A; M/a=46-264.
DR PDBsum; 3UNB; -.
DR PDBsum; 3UNE; -.
DR PDBsum; 3UNF; -.
DR PDBsum; 3UNH; -.
DR AlphaFoldDB; P99026; -.
DR SMR; P99026; -.
DR BioGRID; 202420; 85.
DR CORUM; P99026; -.
DR DIP; DIP-35152N; -.
DR IntAct; P99026; 45.
DR MINT; P99026; -.
DR STRING; 10090.ENSMUSP00000005923; -.
DR MEROPS; T01.987; -.
DR iPTMnet; P99026; -.
DR PhosphoSitePlus; P99026; -.
DR SwissPalm; P99026; -.
DR REPRODUCTION-2DPAGE; P99026; -.
DR SWISS-2DPAGE; P99026; -.
DR CPTAC; non-CPTAC-5617; -.
DR EPD; P99026; -.
DR jPOST; P99026; -.
DR MaxQB; P99026; -.
DR PaxDb; P99026; -.
DR PeptideAtlas; P99026; -.
DR PRIDE; P99026; -.
DR ProteomicsDB; 291761; -.
DR Antibodypedia; 1673; 459 antibodies from 35 providers.
DR DNASU; 19172; -.
DR Ensembl; ENSMUST00000005923; ENSMUSP00000005923; ENSMUSG00000005779.
DR GeneID; 19172; -.
DR KEGG; mmu:19172; -.
DR UCSC; uc008qhe.2; mouse.
DR CTD; 5692; -.
DR MGI; MGI:1098257; Psmb4.
DR VEuPathDB; HostDB:ENSMUSG00000005779; -.
DR eggNOG; KOG0185; Eukaryota.
DR GeneTree; ENSGT00390000000698; -.
DR HOGENOM; CLU_072435_2_0_1; -.
DR InParanoid; P99026; -.
DR OMA; KGYGTQT; -.
DR OrthoDB; 1228942at2759; -.
DR PhylomeDB; P99026; -.
DR TreeFam; TF106220; -.
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; 19172; 31 hits in 73 CRISPR screens.
DR ChiTaRS; Psmb4; mouse.
DR PRO; PR:P99026; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P99026; protein.
DR Bgee; ENSMUSG00000005779; Expressed in indifferent gonad and 259 other tissues.
DR Genevisible; P99026; MM.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; 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:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IMP:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR CDD; cd03760; proteasome_beta_type_4; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR016295; Proteasome_beta4.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF5; PTHR11599:SF5; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PIRSF; PIRSF001213; Psome_endopept_beta; 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; Nucleus;
KW Phosphoprotein; Proteasome; Reference proteome.
FT PROPEP 1..45
FT /evidence="ECO:0000269|Ref.4, ECO:0000269|Ref.5"
FT /id="PRO_0000026581"
FT CHAIN 46..264
FT /note="Proteasome subunit beta type-4"
FT /id="PRO_0000026582"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P28070"
FT MOD_RES 102
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P28070"
FT CONFLICT 26
FT /note="A -> S (in Ref. 2; BAE33781 and 3; AAH08241)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="T -> A (in Ref. 2; BAE33781)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="P -> H (in Ref. 2; BAE40213)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="E -> G (in Ref. 2; BAE23215)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="R -> K (in Ref. 2; BAC36805)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="I -> V (in Ref. 2; BAE33781)"
FT /evidence="ECO:0000305"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 102..122
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 130..146
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3UNE"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 207..224
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3UNE"
SQ SEQUENCE 264 AA; 29116 MW; 6B6B42B21DFA2B74 CRC64;
MEAFWESRAG HWAGGPAPGQ FYRIPATPSG LMDPASAPCE GPITRTQNPM VTGTSVLGVK
FDGGVVIAAD MLGSYGSLAR FRNISRIMRV NDSTMLGASG DYADFQYLKQ VLGQMVIDEE
LLGDGHSYSP RAIHSWLTRA MYSRRSKMNP LWNTMVIGGY ADGESFLGYV DMLGVAYEAP
SLATGYGAYL AQPLLREVLE KQPVLSQTEA RELVERCMRV LYYRDARSYN RFQIATVTEK
GVEIEGPLSA QTNWDIAHMI SGFE
