ID   PRDX5_MOUSE             Reviewed;         210 AA.
AC   P99029; Q9QX45; Q9QZ75;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2002, sequence version 2.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Peroxiredoxin-5, mitochondrial;
DE            EC=1.11.1.24 {ECO:0000269|PubMed:10679306};
DE   AltName: Full=Antioxidant enzyme B166;
DE            Short=AOEB166;
DE   AltName: Full=Liver tissue 2D-page spot 2D-0014IV;
DE   AltName: Full=PLP;
DE   AltName: Full=Peroxiredoxin V;
DE            Short=Prx-V;
DE   AltName: Full=Peroxisomal antioxidant enzyme;
DE   AltName: Full=Thioredoxin peroxidase PMP20;
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin 5 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=Prdx5 {ECO:0000312|MGI:MGI:1859821}; Synonyms=Prdx6;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10679306; DOI=10.1006/bbrc.2000.2231;
RA   Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M.,
RA   Fung P.C.W., Kung H.-F., Jin D.-Y.;
RT   "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-
RT   induced apoptosis.";
RL   Biochem. Biophys. Res. Commun. 268:921-927(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10514471; DOI=10.1074/jbc.274.42.29897;
RA   Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P.,
RA   Subramani S., Rogers R.A., Avraham H.;
RT   "Characterization of human and murine PMP20 peroxisomal proteins that
RT   exhibit antioxidant activity in vitro.";
RL   J. Biol. Chem. 274:29897-29904(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/HeJ; TISSUE=Lung;
RX   PubMed=10521424; DOI=10.1074/jbc.274.43.30451;
RA   Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C.,
RA   Duconseille E., Falmagne P., Bernard A.;
RT   "Cloning and characterization of AOEB166, a novel mammalian antioxidant
RT   enzyme of the peroxiredoxin family.";
RL   J. Biol. Chem. 274:30451-30458(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10753630; DOI=10.1006/bbrc.2000.2430;
RA   Lee T.H., Kim S.J., Kang S.W., Lee K.K., Rhee S.G., Yu D.Y.;
RT   "Molecular cloning and characterization of the mouse Peroxiredoxin V
RT   gene.";
RL   Biochem. Biophys. Res. Commun. 270:356-362(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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   [7]
RP   PROTEIN SEQUENCE OF 50-61.
RC   TISSUE=Liver;
RA   Sanchez J.-C., Rouge V., Frutiger S., Hughes G.J., Yan J.X., Hoogland C.,
RA   Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.;
RL   Submitted (AUG-1998) to UniProtKB.
RN   [8]
RP   PROTEIN SEQUENCE OF 72-79; 83-112 AND 145-172, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-79 AND LYS-112, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-71 AND LYS-79, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN   [12]
RP   PALMITOYLATION.
RX   PubMed=31740833; DOI=10.1038/s41589-019-0399-y;
RA   Cao Y., Qiu T., Kathayat R.S., Azizi S.A., Thorne A.K., Ahn D., Fukata Y.,
RA   Fukata M., Rice P.A., Dickinson B.C.;
RT   "ABHD10 is an S-depalmitoylase affecting redox homeostasis through
RT   peroxiredoxin-5.";
RL   Nat. Chem. Biol. 15:1232-1240(2019).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC       signaling events. {ECO:0000269|PubMed:10679306}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC         disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC         COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC         ChEBI:CHEBI:50058; EC=1.11.1.24;
CC         Evidence={ECO:0000269|PubMed:10679306};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P30044}.
CC   -!- INTERACTION:
CC       P99029; P08228: Sod1; NbExp=2; IntAct=EBI-2735704, EBI-1635090;
CC   -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion
CC       {ECO:0000250|UniProtKB:P30044}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic+peroxisomal]: Cytoplasm
CC       {ECO:0000250|UniProtKB:P30044}. Peroxisome matrix
CC       {ECO:0000250|UniProtKB:P30044}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Mitochondrial;
CC         IsoId=P99029-1; Sequence=Displayed;
CC       Name=Cytoplasmic+peroxisomal;
CC         IsoId=P99029-2; Sequence=VSP_018830;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- PTM: S-palmitoylated. Palmitoylation occurs on the active site,
CC       inhibiting its reactivity; therefore PRDX5 palmitoylation status
CC       determines its antioxidant capacity. {ECO:0000269|PubMed:31740833}.
CC   -!- PTM: [Isoform Mitochondrial]: S-palmitoylated. Depalmitoylated by
CC       ABHD10. {ECO:0000250|UniProtKB:P30044}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. In this atypical 2-Cys
CC       Prx, C(R) is present in the same subunit to form an intramolecular
CC       disulfide. The disulfide is subsequently reduced by thioredoxin.
CC       {ECO:0000250|UniProtKB:P30044}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF197951; AAF04855.1; -; mRNA.
DR   EMBL; AF124994; AAF27532.1; -; mRNA.
DR   EMBL; AF110733; AAG13450.1; -; mRNA.
DR   EMBL; AF208730; AAF21016.1; -; Genomic_DNA.
DR   EMBL; AF208729; AAF21016.1; JOINED; Genomic_DNA.
DR   EMBL; AK002383; BAB22058.1; -; mRNA.
DR   EMBL; AK003332; BAB22720.1; -; mRNA.
DR   EMBL; BC008174; AAH08174.1; -; mRNA.
DR   CCDS; CCDS29507.1; -. [P99029-1]
DR   PIR; JC7239; JC7239.
DR   RefSeq; NP_036151.1; NM_012021.2. [P99029-1]
DR   AlphaFoldDB; P99029; -.
DR   SMR; P99029; -.
DR   BioGRID; 207718; 20.
DR   IntAct; P99029; 6.
DR   MINT; P99029; -.
DR   STRING; 10090.ENSMUSP00000025904; -.
DR   MoonProt; P99029; -.
DR   PeroxiBase; 4453; MmPrxV.
DR   GlyGen; P99029; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P99029; -.
DR   PhosphoSitePlus; P99029; -.
DR   SwissPalm; P99029; -.
DR   REPRODUCTION-2DPAGE; P99029; -.
DR   EPD; P99029; -.
DR   jPOST; P99029; -.
DR   MaxQB; P99029; -.
DR   PaxDb; 10090-ENSMUSP00000025904; -.
DR   PeptideAtlas; P99029; -.
DR   ProteomicsDB; 289893; -. [P99029-1]
DR   ProteomicsDB; 289894; -. [P99029-2]
DR   Pumba; P99029; -.
DR   Antibodypedia; 3276; 494 antibodies from 39 providers.
DR   DNASU; 54683; -.
DR   Ensembl; ENSMUST00000025904.12; ENSMUSP00000025904.6; ENSMUSG00000024953.18. [P99029-1]
DR   GeneID; 54683; -.
DR   KEGG; mmu:54683; -.
DR   UCSC; uc008gjc.1; mouse. [P99029-1]
DR   AGR; MGI:1859821; -.
DR   CTD; 25824; -.
DR   MGI; MGI:1859821; Prdx5.
DR   VEuPathDB; HostDB:ENSMUSG00000024953; -.
DR   eggNOG; KOG0541; Eukaryota.
DR   GeneTree; ENSGT00390000018173; -.
DR   InParanoid; P99029; -.
DR   OMA; PTCHSAH; -.
DR   OrthoDB; 593245at2759; -.
DR   PhylomeDB; P99029; -.
DR   TreeFam; TF105182; -.
DR   Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR   Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR   BioGRID-ORCS; 54683; 4 hits in 79 CRISPR screens.
DR   ChiTaRS; Prdx5; mouse.
DR   PRO; PR:P99029; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P99029; Protein.
DR   Bgee; ENSMUSG00000024953; Expressed in granulocyte and 273 other cell types or tissues.
DR   ExpressionAtlas; P99029; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; ISO:MGI.
DR   GO; GO:0016209; F:antioxidant activity; ISS:UniProtKB.
DR   GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0004601; F:peroxidase activity; ISO:MGI.
DR   GO; GO:0072541; F:peroxynitrite reductase activity; ISO:MGI.
DR   GO; GO:0001016; F:RNA polymerase III transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; ISO:MGI.
DR   GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IDA:FlyBase.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; ISS:UniProtKB.
DR   GO; GO:0070995; P:NADPH oxidation; ISO:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; ISO:MGI.
DR   GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
DR   GO; GO:2001057; P:reactive nitrogen species metabolic process; ISO:MGI.
DR   GO; GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; ISO:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR   CDD; cd03013; PRX5_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR037944; PRX5-like.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR   PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   SWISS-2DPAGE; P99029; -.
DR   Genevisible; P99029; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative initiation; Antioxidant; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Lipoprotein; Mitochondrion;
KW   Oxidoreductase; Palmitate; Peroxidase; Peroxisome; Phosphoprotein;
KW   Redox-active center; Reference proteome; Transit peptide.
FT   TRANSIT         1..48
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..210
FT                   /note="Peroxiredoxin-5, mitochondrial"
FT                   /id="PRO_0000023795"
FT   DOMAIN          52..210
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   MOTIF           208..210
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000250|UniProtKB:P30044"
FT   ACT_SITE        96
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P30044"
FT   MOD_RES         70
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         70
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         71
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         79
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         79
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         112
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R063"
FT   MOD_RES         178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   LIPID           96
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P30044"
FT   DISULFID        96..200
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   VAR_SEQ         1..48
FT                   /note="Missing (in isoform Cytoplasmic+peroxisomal)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018830"
FT   CONFLICT        55
FT                   /note="G -> D (in Ref. 7; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        83..102
FT                   /note="GVLFGVPGAFTPGCSKTHLP -> VFCLESLGHLHLAVLRPTA (in Ref.
FT                   4; AAF21016)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   210 AA;  21897 MW;  E944104CC468BDD8 CRC64;
     MLQLGLRVLG CKASSVLRAS TCLAGRAGRK EAGWECGGAR SFSSSAVTMA PIKVGDAIPS
     VEVFEGEPGK KVNLAELFKG KKGVLFGVPG AFTPGCSKTH LPGFVEQAGA LKAKGAQVVA
     CLSVNDVFVI EEWGRAHQAE GKVRLLADPT GAFGKATDLL LDDSLVSLFG NRRLKRFSMV
     IDNGIVKALN VEPDGTGLTC SLAPNILSQL
//