ID   PENK_MOUSE              Reviewed;         268 AA.
AC   P22005; Q68G73;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Proenkephalin-A {ECO:0000305};
DE   Contains:
DE     RecName: Full=Synenkephalin;
DE   Contains:
DE     RecName: Full=Met-enkephalin;
DE     AltName: Full=Opioid growth factor;
DE              Short=OGF;
DE   Contains:
DE     RecName: Full=PENK(114-133) {ECO:0000250|UniProtKB:P04094};
DE   Contains:
DE     RecName: Full=PENK(143-184) {ECO:0000250|UniProtKB:P04094};
DE   Contains:
DE     RecName: Full=Met-enkephalin-Arg-Ser-Leu;
DE   Contains:
DE     RecName: Full=Leu-enkephalin;
DE   Contains:
DE     RecName: Full=PENK(238-259) {ECO:0000250|UniProtKB:P04094};
DE   Contains:
DE     RecName: Full=Met-enkephalin-Arg-Phe {ECO:0000303|PubMed:35201898};
DE   Flags: Precursor;
GN   Name=Penk; Synonyms=Penk1;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Testis;
RX   PubMed=2355920; DOI=10.1128/mcb.10.7.3717-3726.1990;
RA   Kilpatrick D.L., Zinn S.A., Fitzgerald M., Higuchi H., Sabol S.L.,
RA   Meyerhardt J.;
RT   "Transcription of the rat and mouse proenkephalin genes is initiated at
RT   distinct sites in spermatogenic and somatic cells.";
RL   Mol. Cell. Biol. 10:3717-3726(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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 GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-268.
RC   TISSUE=T-cell;
RX   PubMed=2938259; DOI=10.1126/science.2938259;
RA   Zurawski G., Benedik M., Kamb B.J., Abrams J.S., Zurawski S.M., Lee F.D.;
RT   "Activation of mouse T-helper cells induces abundant preproenkephalin mRNA
RT   synthesis.";
RL   Science 232:772-775(1986).
RN   [7]
RP   FUNCTION (MET-ENKEPHALIN-ARG-PHE).
RX   PubMed=6933569; DOI=10.1073/pnas.77.9.5512;
RA   Inturrisi C.E., Umans J.G., Wolff D., Stern A.S., Lewis R.V., Stein S.,
RA   Udenfriend S.;
RT   "Analgesic activity of the naturally occurring heptapeptide
RT   [Met]enkephalin-Arg6-Phe7.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:5512-5514(1980).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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   [9]
RP   FUNCTION (MET-ENKEPHALIN-ARG-PHE), AND PROTEOLYTIC CLEAVAGE
RP   (MET-ENKEPHALIN-ARG-PHE).
RX   PubMed=35201898; DOI=10.1126/science.abl5130;
RA   Trieu B.H., Remmers B.C., Toddes C., Brandner D.D., Lefevre E.M.,
RA   Kocharian A., Retzlaff C.L., Dick R.M., Mashal M.A., Gauthier E.A., Xie W.,
RA   Zhang Y., More S.S., Rothwell P.E.;
RT   "Angiotensin-converting enzyme gates brain circuit-specific plasticity via
RT   an endogenous opioid.";
RL   Science 2022:eabl5130-eabl5130(2022).
CC   -!- FUNCTION: [Met-enkephalin]: Neuropeptide that competes with and mimic
CC       the effects of opiate drugs. They play a role in a number of
CC       physiologic functions, including pain perception and responses to
CC       stress. {ECO:0000250|UniProtKB:P01210}.
CC   -!- FUNCTION: [Leu-enkephalin]: Neuropeptide that competes with and mimic
CC       the effects of opiate drugs. They play a role in a number of
CC       physiologic functions, including pain perception and responses to
CC       stress. {ECO:0000250|UniProtKB:P01210}.
CC   -!- FUNCTION: [Met-enkephalin-Arg-Phe]: Met-enkephalin-Arg-Phe neuropeptide
CC       acts as a strong ligand of Mu-type opioid receptor OPRM1
CC       (PubMed:6933569, PubMed:35201898). Met-enkephalin-Arg-Phe-binding to
CC       OPRM1 in the nucleus accumbens of the brain increases activation of
CC       OPRM1, leading to long-term synaptic depression of glutamate release
CC       (PubMed:35201898). {ECO:0000269|PubMed:35201898,
CC       ECO:0000269|PubMed:6933569}.
CC   -!- FUNCTION: [PENK(114-133)]: Increases glutamate release in the striatum
CC       and decreases GABA concentration in the striatum.
CC       {ECO:0000250|UniProtKB:P04094}.
CC   -!- FUNCTION: [PENK(238-259)]: Increases glutamate release in the striatum.
CC       {ECO:0000250|UniProtKB:P04094}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       chromaffin granule lumen {ECO:0000250|UniProtKB:P01211}. Secreted
CC       {ECO:0000250|UniProtKB:P01211}.
CC   -!- TISSUE SPECIFICITY: Spermatogenic and somatic cells.
CC       {ECO:0000269|PubMed:2355920}.
CC   -!- DEVELOPMENTAL STAGE: Highest expression in late pachytene spermatocytes
CC       and postmeiotic round spermatids. {ECO:0000269|PubMed:2355920}.
CC   -!- PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin.
CC       {ECO:0000250|UniProtKB:P01211}.
CC   -!- PTM: [Met-enkephalin]: Processed and degraded by ACE.
CC       {ECO:0000250|UniProtKB:P01210}.
CC   -!- PTM: [Leu-enkephalin]: Processed and degraded by ACE.
CC       {ECO:0000250|UniProtKB:P01210}.
CC   -!- PTM: [Met-enkephalin-Arg-Ser-Leu]: Probably cleaved by ACE.
CC       {ECO:0000250|UniProtKB:P01210}.
CC   -!- PTM: [Met-enkephalin-Arg-Phe]: Processed by ACE to generate Met-
CC       enkephalin in the nucleus accumbens of the brain.
CC       {ECO:0000269|PubMed:35201898}.
CC   -!- PTM: The N-terminal domain contains 6 conserved cysteines thought to be
CC       involved in disulfide bonding and/or processing.
CC       {ECO:0000250|UniProtKB:P01210}.
CC   -!- SIMILARITY: Belongs to the opioid neuropeptide precursor family.
CC       {ECO:0000305}.
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DR   EMBL; M55181; AAA40128.1; -; mRNA.
DR   EMBL; AK161272; BAE36283.1; -; mRNA.
DR   EMBL; BX004841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466538; EDL05699.1; -; Genomic_DNA.
DR   EMBL; CH466538; EDL05700.1; -; Genomic_DNA.
DR   EMBL; BC049766; AAH49766.1; -; mRNA.
DR   EMBL; M13227; AAA37553.1; -; mRNA.
DR   CCDS; CCDS17946.1; -.
DR   PIR; B35678; B35678.
DR   RefSeq; NP_001002927.1; NM_001002927.3.
DR   RefSeq; NP_001335138.1; NM_001348209.1.
DR   AlphaFoldDB; P22005; -.
DR   BioGRID; 202109; 1.
DR   STRING; 10090.ENSMUSP00000066822; -.
DR   GlyConnect; 2610; 1 N-Linked glycan (1 site).
DR   GlyGen; P22005; 1 site, 1 N-linked glycan (1 site).
DR   iPTMnet; P22005; -.
DR   PhosphoSitePlus; P22005; -.
DR   CPTAC; non-CPTAC-3489; -.
DR   MaxQB; P22005; -.
DR   PaxDb; P22005; -.
DR   PeptideAtlas; P22005; -.
DR   PRIDE; P22005; -.
DR   ProteomicsDB; 288027; -.
DR   Antibodypedia; 2211; 395 antibodies from 36 providers.
DR   DNASU; 18619; -.
DR   Ensembl; ENSMUST00000070375; ENSMUSP00000066822; ENSMUSG00000045573.
DR   GeneID; 18619; -.
DR   KEGG; mmu:18619; -.
DR   UCSC; uc008rwz.1; mouse.
DR   CTD; 5179; -.
DR   MGI; MGI:104629; Penk.
DR   VEuPathDB; HostDB:ENSMUSG00000045573; -.
DR   eggNOG; ENOG502QWWK; Eukaryota.
DR   GeneTree; ENSGT00950000183149; -.
DR   HOGENOM; CLU_070973_0_0_1; -.
DR   InParanoid; P22005; -.
DR   OMA; CAACAYR; -.
DR   OrthoDB; 1149395at2759; -.
DR   PhylomeDB; P22005; -.
DR   TreeFam; TF332620; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR   BioGRID-ORCS; 18619; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Penk; mouse.
DR   PRO; PR:P22005; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P22005; protein.
DR   Bgee; ENSMUSG00000045573; Expressed in caudate-putamen and 255 other tissues.
DR   ExpressionAtlas; P22005; baseline and differential.
DR   Genevisible; P22005; MM.
DR   GO; GO:0030424; C:axon; ISO:MGI.
DR   GO; GO:0043679; C:axon terminus; ISO:MGI.
DR   GO; GO:0070852; C:cell body fiber; ISO:MGI.
DR   GO; GO:0034466; C:chromaffin granule lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0099013; C:neuronal dense core vesicle lumen; ISO:MGI.
DR   GO; GO:0043204; C:perikaryon; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032280; C:symmetric synapse; ISO:MGI.
DR   GO; GO:0034592; C:synaptic vesicle lumen; ISO:MGI.
DR   GO; GO:0001515; F:opioid peptide activity; IDA:UniProtKB.
DR   GO; GO:0031628; F:opioid receptor binding; IDA:UniProtKB.
DR   GO; GO:0002118; P:aggressive behavior; IMP:MGI.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR   GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR   GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0051867; P:general adaptation syndrome, behavioral process; IEA:Ensembl.
DR   GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0035641; P:locomotory exploration behavior; ISO:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR   GO; GO:2000987; P:positive regulation of behavioral fear response; ISO:MGI.
DR   GO; GO:1900452; P:regulation of long-term synaptic depression; IDA:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR   GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR   GO; GO:0071871; P:response to epinephrine; IEA:Ensembl.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0043278; P:response to morphine; IEA:Ensembl.
DR   GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR   GO; GO:0009314; P:response to radiation; IEA:Ensembl.
DR   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR   GO; GO:0007600; P:sensory perception; IBA:GO_Central.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0001964; P:startle response; IMP:MGI.
DR   GO; GO:0099538; P:synaptic signaling via neuropeptide; ISO:MGI.
DR   InterPro; IPR006024; Opioid_neupept.
DR   InterPro; IPR000703; Proenkphlin_A.
DR   PANTHER; PTHR11438; PTHR11438; 1.
DR   PANTHER; PTHR11438:SF3; PTHR11438:SF3; 1.
DR   Pfam; PF01160; Opiods_neuropep; 1.
DR   PRINTS; PR01028; OPIOIDPRCRSR.
DR   PRINTS; PR01029; PENKAPRCRSR.
DR   PROSITE; PS01252; OPIOIDS_PRECURSOR; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Cytoplasmic vesicle; Disulfide bond;
KW   Endorphin; Neuropeptide; Opioid peptide; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT   PEPTIDE         25..97
FT                   /note="Synenkephalin"
FT                   /id="PRO_0000008268"
FT   PEPTIDE         100..104
FT                   /note="Met-enkephalin"
FT                   /id="PRO_0000008269"
FT   PEPTIDE         107..111
FT                   /note="Met-enkephalin"
FT                   /id="PRO_0000008270"
FT   PEPTIDE         114..133
FT                   /note="PENK(114-133)"
FT                   /evidence="ECO:0000250|UniProtKB:P04094"
FT                   /id="PRO_0000377694"
FT   PEPTIDE         136..140
FT                   /note="Met-enkephalin"
FT                   /id="PRO_0000008272"
FT   PEPTIDE         143..184
FT                   /note="PENK(143-184)"
FT                   /evidence="ECO:0000250|UniProtKB:P04094"
FT                   /id="PRO_0000377695"
FT   PEPTIDE         187..194
FT                   /note="Met-enkephalin-Arg-Ser-Leu"
FT                   /id="PRO_0000008274"
FT   PROPEP          197..208
FT                   /id="PRO_0000008275"
FT   PEPTIDE         211..215
FT                   /note="Met-enkephalin"
FT                   /id="PRO_0000008276"
FT   PROPEP          218..228
FT                   /id="PRO_0000008277"
FT   PEPTIDE         231..235
FT                   /note="Leu-enkephalin"
FT                   /id="PRO_0000008278"
FT   PEPTIDE         238..259
FT                   /note="PENK(238-259)"
FT                   /evidence="ECO:0000250|UniProtKB:P04094"
FT                   /id="PRO_0000377696"
FT   PEPTIDE         262..268
FT                   /note="Met-enkephalin-Arg-Phe"
FT                   /evidence="ECO:0000269|PubMed:35201898"
FT                   /id="PRO_0000008280"
FT   REGION          163..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            111..112
FT                   /note="Cleavage; by CTSL"
FT                   /evidence="ECO:0000250|UniProtKB:P01211"
FT   SITE            112..113
FT                   /note="Cleavage; by CTSL"
FT                   /evidence="ECO:0000250|UniProtKB:P01211"
FT   SITE            133..134
FT                   /note="Cleavage; by CTSL"
FT                   /evidence="ECO:0000250|UniProtKB:P01211"
FT   SITE            215..216
FT                   /note="Cleavage; by CTSL"
FT                   /evidence="ECO:0000250|UniProtKB:P01211"
FT   SITE            216..217
FT                   /note="Cleavage; by CTSL"
FT                   /evidence="ECO:0000250|UniProtKB:P01211"
FT   SITE            219..220
FT                   /note="Cleavage; by CTSL"
FT                   /evidence="ECO:0000250|UniProtKB:P01211"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04094"
FT   DISULFID        26..48
FT                   /evidence="ECO:0000250|UniProtKB:P01210"
FT   DISULFID        30..52
FT                   /evidence="ECO:0000250|UniProtKB:P01210"
FT   DISULFID        33..65
FT                   /evidence="ECO:0000250|UniProtKB:P01210"
FT   CONFLICT        34
FT                   /note="S -> T (in Ref. 1; AAA40128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="S -> SS (in Ref. 1; AAA40128)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   268 AA;  31004 MW;  637F848B49F44013 CRC64;
     MARFLRLCTW LLALGSCLLA TVQAECSQDC AKCSYRLVRP GDINFLACTL ECEGQLPSFK
     IWETCKDLLQ VSRPEFPWDN IDMYKDSSKQ DESHLLAKKY GGFMKRYGGF MKKMDELYPM
     EPEEEANGGE ILAKRYGGFM KKDADEGDTL ANSSDLLKEL LGTGDNRAKD SHQQESTNND
     EDMSKRYGGF MRSLKRSPQL EDEAKELQKR YGGFMRRVGR PEWWMDYQKR YGGFLKRFAE
     SLPSDEEGEN YSKEVPEIEK RYGGFMRF
//