PSME4_MOUSE
ID PSME4_MOUSE Reviewed; 1843 AA.
AC Q5SSW2; C4IXU5; Q3TER7; Q3V2B7; Q6ZQJ7; Q7TMY9; Q8K0K0; Q99KM2; Q9ESY1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Proteasome activator complex subunit 4;
DE AltName: Full=Proteasome activator PA200;
DE AltName: Full=Protein TEMO;
GN Name=Psme4; Synonyms=Kiaa0077;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-1843 (ISOFORM 1).
RA Mruk D., Mo M.-Y., Cheng C.Y.;
RT "TEMO is a marker to study sertoli-germ cell interactions: cloning and
RT regulation of a novel testicular molecule.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-1843 (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Brain, Colon, and 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1399-1843 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=12093752; DOI=10.1093/emboj/cdf333;
RA Ustrell V., Hoffman L., Pratt G., Rechsteiner M.;
RT "PA200, a nuclear proteasome activator involved in DNA repair.";
RL EMBO J. 21:3516-3525(2002).
RN [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 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 FUNCTION, IDENTIFICATION IN THE SPERMATOPROTEASOME, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23706739; DOI=10.1016/j.cell.2013.04.032;
RA Qian M.X., Pang Y., Liu C.H., Haratake K., Du B.Y., Ji D.Y., Wang G.F.,
RA Zhu Q.Q., Song W., Yu Y., Zhang X.X., Huang H.T., Miao S., Chen L.B.,
RA Zhang Z.H., Liang Y.N., Liu S., Cha H., Yang D., Zhai Y., Komatsu T.,
RA Tsuruta F., Li H., Cao C., Li W., Li G.H., Cheng Y., Chiba T., Wang L.,
RA Goldberg A.L., Shen Y., Qiu X.B.;
RT "Acetylation-mediated proteasomal degradation of core histones during DNA
RT repair and spermatogenesis.";
RL Cell 153:1012-1024(2013).
CC -!- FUNCTION: Associated component of the proteasome that specifically
CC recognizes acetylated histones and promotes ATP- and ubiquitin-
CC independent degradation of core histones during spermatogenesis and DNA
CC damage response. Recognizes and binds acetylated histones via its
CC bromodomain-like (BRDL) region and activates the proteasome by opening
CC the gated channel for substrate entry. Binds to the core proteasome via
CC its C-terminus, which occupies the same binding sites as the
CC proteasomal ATPases, opening the closed structure of the proteasome via
CC an active gating mechanism. Component of the spermatoproteasome, a form
CC of the proteasome specifically found in testis: binds to acetylated
CC histones and promotes degradation of histones, thereby participating
CC actively to the exchange of histones during spermatogenesis. Also
CC involved in DNA damage response in somatic cells, by promoting
CC degradation of histones following DNA double-strand breaks.
CC {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:23706739}.
CC -!- SUBUNIT: Homodimer. Interacts with the 20S and 26S proteasomes.
CC Component of the spermatoproteasome, a form of the proteasome
CC specifically found in testis. {ECO:0000269|PubMed:23706739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Nucleus speckle
CC {ECO:0000250}. Note=Found in nuclear foci following treatment with
CC ionizing radiation, but not with ultraviolet irradiation or H(2)O(2).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SSW2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SSW2-2; Sequence=VSP_023880;
CC -!- TISSUE SPECIFICITY: Broadly expressed. Present in heart (at protein
CC level). {ECO:0000269|PubMed:12093752, ECO:0000269|PubMed:16857966}.
CC -!- DOMAIN: The bromodomain-like (BRDL) region specifically recognizes and
CC binds acetylated histones. {ECO:0000269|PubMed:23706739}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and show no obvious developmental
CC abnormalities. They have reduced male fertility due to defects in
CC spermatogenesis in meiotic spermatocytes and during the maturation of
CC postmeiotic haploid spermatids. Testes are defective in core histone
CC replacement. {ECO:0000269|PubMed:16581775}.
CC -!- SIMILARITY: Belongs to the BLM10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09060.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC97859.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129049; BAC97859.1; ALT_INIT; mRNA.
DR EMBL; AL662891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF296169; AAG09060.1; ALT_FRAME; mRNA.
DR EMBL; BC004575; AAH04575.1; -; mRNA.
DR EMBL; BC031174; AAH31174.1; -; mRNA.
DR EMBL; BC054364; AAH54364.1; -; mRNA.
DR EMBL; BC141381; AAI41382.1; -; mRNA.
DR EMBL; AK131932; BAE20881.1; -; mRNA.
DR EMBL; AK169447; BAE41181.1; -; mRNA.
DR CCDS; CCDS36124.1; -. [Q5SSW2-1]
DR RefSeq; NP_598774.2; NM_134013.3. [Q5SSW2-1]
DR AlphaFoldDB; Q5SSW2; -.
DR SMR; Q5SSW2; -.
DR BioGRID; 222113; 14.
DR IntAct; Q5SSW2; 5.
DR MINT; Q5SSW2; -.
DR STRING; 10090.ENSMUSP00000045460; -.
DR iPTMnet; Q5SSW2; -.
DR PhosphoSitePlus; Q5SSW2; -.
DR SwissPalm; Q5SSW2; -.
DR EPD; Q5SSW2; -.
DR MaxQB; Q5SSW2; -.
DR PaxDb; Q5SSW2; -.
DR PeptideAtlas; Q5SSW2; -.
DR PRIDE; Q5SSW2; -.
DR ProteomicsDB; 291706; -. [Q5SSW2-1]
DR ProteomicsDB; 291707; -. [Q5SSW2-2]
DR Antibodypedia; 30226; 110 antibodies from 22 providers.
DR DNASU; 103554; -.
DR Ensembl; ENSMUST00000041231; ENSMUSP00000045460; ENSMUSG00000040850. [Q5SSW2-1]
DR GeneID; 103554; -.
DR KEGG; mmu:103554; -.
DR UCSC; uc007ihx.1; mouse. [Q5SSW2-1]
DR UCSC; uc007iia.1; mouse. [Q5SSW2-2]
DR CTD; 23198; -.
DR MGI; MGI:2143994; Psme4.
DR VEuPathDB; HostDB:ENSMUSG00000040850; -.
DR eggNOG; KOG1851; Eukaryota.
DR GeneTree; ENSGT00390000011433; -.
DR HOGENOM; CLU_000772_2_0_1; -.
DR InParanoid; Q5SSW2; -.
DR OMA; GKDWSDE; -.
DR OrthoDB; 83617at2759; -.
DR PhylomeDB; Q5SSW2; -.
DR TreeFam; TF106237; -.
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-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-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-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-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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 103554; 2 hits in 110 CRISPR screens.
DR ChiTaRS; Psme4; mouse.
DR PRO; PR:Q5SSW2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SSW2; protein.
DR Bgee; ENSMUSG00000040850; Expressed in temporalis muscle and 267 other tissues.
DR ExpressionAtlas; Q5SSW2; baseline and differential.
DR Genevisible; Q5SSW2; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; IDA:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0016504; F:peptidase activator activity; IDA:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032430; Blm10_mid.
DR InterPro; IPR035309; PSME4.
DR InterPro; IPR021843; PSME4_C.
DR PANTHER; PTHR32170; PTHR32170; 1.
DR Pfam; PF16507; BLM10_mid; 1.
DR Pfam; PF11919; DUF3437; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW DNA damage; DNA repair; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1..1843
FT /note="Proteasome activator complex subunit 4"
FT /id="PRO_0000280719"
FT REPEAT 475..519
FT /note="HEAT 1"
FT REPEAT 998..1037
FT /note="HEAT 2"
FT REPEAT 1179..1217
FT /note="HEAT 3"
FT REPEAT 1354..1392
FT /note="HEAT 4"
FT REPEAT 1636..1674
FT /note="HEAT 5"
FT REPEAT 1680..1718
FT /note="HEAT 6"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1650..1738
FT /note="Bromodomain-like (BRDL)"
FT /evidence="ECO:0000250"
FT MOD_RES 1121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14997"
FT MOD_RES 1614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14997"
FT MOD_RES 1746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14997"
FT VAR_SEQ 1..1703
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_023880"
FT CONFLICT 52
FT /note="L -> Q (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="T -> A (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="D -> V (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="I -> V (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="G -> R (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="P -> L (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="L -> P (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="E -> G (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="V -> A (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="Y -> C (in Ref. 3; AAG09060 and 4; AAI41382)"
FT /evidence="ECO:0000305"
FT CONFLICT 1163
FT /note="F -> S (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 1181
FT /note="L -> S (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 1234
FT /note="K -> R (in Ref. 3; AAG09060 and 4; AAH31174/
FT AAI41382)"
FT /evidence="ECO:0000305"
FT CONFLICT 1238
FT /note="I -> V (in Ref. 3; AAG09060 and 4; AAH31174/
FT AAI41382)"
FT /evidence="ECO:0000305"
FT CONFLICT 1342
FT /note="F -> S (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 1404
FT /note="L -> V (in Ref. 3; AAG09060 and 4; AAH31174/
FT AAI41382)"
FT /evidence="ECO:0000305"
FT CONFLICT 1545
FT /note="T -> P (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
FT CONFLICT 1782
FT /note="P -> S (in Ref. 3; AAG09060)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1843 AA; 211197 MW; 326FD7B3A070C502 CRC64;
MEAPERAGGG EPPEPGGRPV LGPRAFVPQK EIVYNKLLPY AERLDAESDL QLAQIKSNLG
RAVQLQELWP GGLFWTRKLS TYIRLYGRKF SKEDHVLFIK LLYELVSIPK LEISMMQGFA
RLLINLLKKK ELLSRDDLEL PWRPLYDLVE RILYSKTEHL RLNSFPNSIE NVLKTLVKSC
RPYFPADSTA EMLEEWRPLM CPFDVTMQKA ISYFEIFLPT SLPPELHHKG FKLWFDELIG
LWVSVQNLPQ WEGQLVNLFA RLATDNIGYI DWDPYVPKIF TRILRSLNLP VGSSQVLVPR
FLTNAYDIGH AVIWITAMMG GPSKLVQKHL AGLFNSITSF YHPSNNGRWL NKLMKLLQRL
PNSVVRRLHR ERFKKPSWLT PVPESHKLTD EDVTDFVQCI IQPVLLAMFS KTGSLEAAQA
LQNLALMRPE LVIPPVLERT YPALETLTEP HQLTATLNCV IGVARSLVSG SKWFPEGPTH
MLPLLMRALP GVDPNDFSKC MITFQFIGTF STLVPLVDCS SVLQERNDLT EIEKELCSAT
AEFEDFVLQF MDRCFGLIES STLEQTREET ETEKMTHLES LVELGLSSTF STILTQCSKD
IFMVALQKVF NFSVSHIFET RVAGRMVADM CRAAVKCCPE ESLKLFVPHC YGVITQLTMN
DDVLNEEELD KELLWNLQLL SEITRVDGKK LLLYREQLVK ILQRTLHLTC KQGYTLSCNL
LHHLLRSTTL IYPTEYCSVP GGFNKPPSEY FPVKDWGKPG DLWNLGIQWH VPSSEEVSFA
FYLLDSFLQP ELIKLQCCGD GELEMSRDDI LQSLTIVHSC LIGSGNLLPP LKGEAVTNLV
PSMVSLEETK LYTGLEHDLS RENYREVIAS VIRKLLSHIL DNSEDDTKSL FLIIKIIGDL
LHFQGSHKHE FDSRWKSFNL VKKSMENRLH GKKQHIRALL IDRVMLQHEL RTLTVEGCEY
KKIHQDMIRD LLRLSTSSYS QVRNKAQQTF FAALGAYNFC CRDIIPLVLE FLRPDRKDVT
QQQFKGALYC LLGNHSGVCL ANLHDWDCIV QTWPALVSSG LSQAMSLEKP SIVRLFDDLA
EKIHRQYETI GLDFTIPKSC AAIAELLQQS KNPSISQTLL SPEKIKEGQK RQQDKNADAL
RNYECLVNTL LDGVEQRNLP WKFEHIGIGL LSLLLRDDRV LPLRAIRFFV ENLNHDAIVV
RKMAISAVAG ILKQLKRTHK KLTINPYEIS GCPKPTKILA GDRPDNHWLH YDSKNIPRTK
KEWESSCFVE KTHWGYYNWP KNMVVYAGVE EQPKLGRSRE DMIEAEQIIY DRFSDPKFVE
QLITFLSLED RKGRDKFSPR RFCLFKGIFR NFDDAFLPVL KPHLERLVAD SHESTQRCVA
EIIAGLIRGS KHWTFEKVEK LWELLCPLLR TALSNMTVET YNDWGTCIAT SCESRDPRKL
HWLFELLLES PLSGEGGSFV DACRLYVLQG GLAQQEWRVP ELLHRLLKYL EPKLTQVYKN
VRERIGSVLT YIFMIDVSLP NTAPTTSPCI PEFTARVLEK LKPLTDVDEE IQNHVMEENG
IGEEDERTQG IKLLKTILKW LMASAGRSFS TAVKEQLQLL PLFFKIAPVE NDNSYDELKR
DAKLCLSLMS QGLLYPQQVP LILQVLSQTA RSSSWHARYT VLTYLQTMVF YNLFIFLNNE
DAVKDIRWLI ICLLEDEQLE VREMAATTLS GLLQCNFLTM DSAMQIHFEQ LCKTKLPKKR
KRDPGSVGDT IPSAELVKRH AGVLGLGACV LSSPYDVPTW MPQLLMNLSA HLNDPQPIEM
TVKKTLSNFR RTHHDNWQEH KQQFTDDQLL VLTDLLVSPC YYA
