PREP_MOUSE
ID PREP_MOUSE Reviewed; 1036 AA.
AC Q8K411; Q3THC4; Q3TJI1; Q3TPP0; Q3URQ8; Q4KUG2; Q4KUG3; Q6ZPX6; Q922N1;
AC Q9CV63;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q5JRX3};
DE AltName: Full=Pitrilysin metalloproteinase 1 {ECO:0000250|UniProtKB:Q5JRX3};
DE Flags: Precursor;
GN Name=Pitrm1 {ECO:0000312|MGI:MGI:1916867};
GN Synonyms=Kiaa1104 {ECO:0000312|EMBL:BAC98102.1},
GN Ntup1 {ECO:0000312|EMBL:AAM49783.1};
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] (ISOFORM 1), AND INDUCTION.
RC STRAIN=C57BL/6J;
RX PubMed=12490196; DOI=10.1006/dbio.2002.0870;
RA Suemizu H., Aiba K., Yoshikawa T., Sharov A.A., Shimozawa N., Tamaoki N.,
RA Ko M.S.H.;
RT "Expression profiling of placentomegaly associated with nuclear
RT transplantation of mouse ES cells.";
RL Dev. Biol. 253:36-53(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-15; ILE-17;
RP CYS-19; MET-462; LYS-546 AND VAL-583.
RC STRAIN=LG/J, and SM/J;
RX PubMed=15919810; DOI=10.2337/diabetes.54.6.1863;
RA Ehrich T.H., Hrbek T., Kenney-Hunt J.P., Pletscher L.S., Wang B.,
RA Semenkovich C.F., Cheverud J.M.;
RT "Fine-mapping gene-by-diet interactions on chromosome 13 in a LG/J x SM/J
RT murine model of obesity.";
RL Diabetes 54:1863-1872(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Amnion, and Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-1036 (ISOFORM 1).
RC TISSUE=Embryonic tail;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1036.
RC STRAIN=FVB/N; 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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-759, SUCCINYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-770; LYS-848 AND LYS-945, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-770 AND LYS-883, 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).
CC -!- FUNCTION: Metalloendopeptidase of the mitochondrial matrix that
CC functions in peptide cleavage and degradation rather than in protein
CC processing. Has an ATP-independent activity. Specifically cleaves
CC peptides in the range of 5 to 65 residues. Shows a preference for
CC cleavage after small polar residues and before basic residues, but
CC without any positional preference. Degrades the transit peptides of
CC mitochondrial proteins after their cleavage. Also degrades other
CC unstructured peptides. It is also able to degrade amyloid-beta protein
CC 40, one of the peptides produced by APP processing, when it accumulates
CC in mitochondrion. It is a highly efficient protease, at least toward
CC amyloid-beta protein 40. Cleaves that peptide at a specific position
CC and is probably not processive, releasing digested peptides
CC intermediates that can be further cleaved subsequently. It is also able
CC to degrade amyloid-beta protein 42. {ECO:0000250|UniProtKB:Q5JRX3}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q5JRX3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q5JRX3};
CC -!- ACTIVITY REGULATION: Mainly exists in a closed and catalytically
CC competent conformation but a closed-to-open switch allows substrate
CC entry into the catalytic chamber. Substrate binding induces closure and
CC dimerization. A disulfide bond may lock the enzyme in a closed
CC conformation preventing substrate entry into the catalytic chamber,
CC participating in redox regulation of the enzyme. Inhibited by metal-
CC chelating agents. Inhibited by nickel and zinc excess, and slightly
CC activated by manganese. {ECO:0000250|UniProtKB:Q5JRX3}.
CC -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC of the substrate. {ECO:0000250|UniProtKB:Q5JRX3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q5JRX3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8K411-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K411-2; Sequence=VSP_020598;
CC Name=3;
CC IsoId=Q8K411-3; Sequence=VSP_020598, VSP_020599;
CC -!- INDUCTION: Up-regulated transplantes nuclei derived from embryonic stem
CC (ES) cells. {ECO:0000269|PubMed:12490196}.
CC -!- PTM: A disulfide bond locks the enzyme in the closed conformation
CC preventing substrate entry into the catalytic chamber.
CC {ECO:0000250|UniProtKB:Q5JRX3}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06917.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF513714; AAM49783.1; -; mRNA.
DR EMBL; AY779273; AAX11355.1; -; mRNA.
DR EMBL; AY779274; AAX11356.1; -; mRNA.
DR EMBL; AK009313; BAB26211.1; -; mRNA.
DR EMBL; AK141277; BAE24630.1; -; mRNA.
DR EMBL; AK147837; BAE28172.1; -; mRNA.
DR EMBL; AK164235; BAE37695.1; -; mRNA.
DR EMBL; AK167426; BAE39514.1; -; mRNA.
DR EMBL; AK168335; BAE40273.1; -; mRNA.
DR EMBL; AK129292; BAC98102.1; -; mRNA.
DR EMBL; BC006917; AAH06917.1; ALT_INIT; mRNA.
DR CCDS; CCDS36585.1; -. [Q8K411-1]
DR RefSeq; NP_660113.1; NM_145131.1. [Q8K411-1]
DR RefSeq; XP_006516571.1; XM_006516508.1.
DR AlphaFoldDB; Q8K411; -.
DR SMR; Q8K411; -.
DR BioGRID; 213572; 6.
DR STRING; 10090.ENSMUSP00000021611; -.
DR iPTMnet; Q8K411; -.
DR PhosphoSitePlus; Q8K411; -.
DR SwissPalm; Q8K411; -.
DR EPD; Q8K411; -.
DR jPOST; Q8K411; -.
DR MaxQB; Q8K411; -.
DR PaxDb; Q8K411; -.
DR PeptideAtlas; Q8K411; -.
DR PRIDE; Q8K411; -.
DR ProteomicsDB; 289402; -. [Q8K411-1]
DR ProteomicsDB; 289403; -. [Q8K411-2]
DR ProteomicsDB; 289404; -. [Q8K411-3]
DR Antibodypedia; 1721; 191 antibodies from 30 providers.
DR DNASU; 69617; -.
DR Ensembl; ENSMUST00000021611; ENSMUSP00000021611; ENSMUSG00000021193. [Q8K411-3]
DR Ensembl; ENSMUST00000222485; ENSMUSP00000152229; ENSMUSG00000021193. [Q8K411-1]
DR GeneID; 69617; -.
DR KEGG; mmu:69617; -.
DR UCSC; uc007pjx.1; mouse. [Q8K411-1]
DR UCSC; uc007pjy.1; mouse. [Q8K411-2]
DR UCSC; uc011ywa.1; mouse. [Q8K411-3]
DR CTD; 10531; -.
DR MGI; MGI:1916867; Pitrm1.
DR VEuPathDB; HostDB:ENSMUSG00000021193; -.
DR eggNOG; KOG2019; Eukaryota.
DR GeneTree; ENSGT00390000018381; -.
DR HOGENOM; CLU_009165_0_0_1; -.
DR InParanoid; Q8K411; -.
DR OMA; MTYPDKT; -.
DR OrthoDB; 107079at2759; -.
DR PhylomeDB; Q8K411; -.
DR TreeFam; TF300333; -.
DR BRENDA; 3.4.24.56; 3474.
DR Reactome; R-MMU-1268020; Mitochondrial protein import.
DR BioGRID-ORCS; 69617; 15 hits in 73 CRISPR screens.
DR ChiTaRS; Pitrm1; mouse.
DR PRO; PR:Q8K411; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8K411; protein.
DR Bgee; ENSMUSG00000021193; Expressed in embryonic post-anal tail and 291 other tissues.
DR ExpressionAtlas; Q8K411; baseline and differential.
DR Genevisible; Q8K411; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disulfide bond; Hydrolase;
KW Metal-binding; Metalloprotease; Mitochondrion; Protease;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 16..1036
FT /note="Presequence protease, mitochondrial"
FT /id="PRO_0000249932"
FT REGION 806..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q5JRX3"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q5JRX3"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q5JRX3"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q5JRX3"
FT MOD_RES 759
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 770
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 770
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 848
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 883
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 945
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT DISULFID 119..556
FT /evidence="ECO:0000250|UniProtKB:Q5JRX3"
FT VAR_SEQ 20
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020598"
FT VAR_SEQ 380..417
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020599"
FT VARIANT 15
FT /note="R -> Q (in strain: LG/J and SM/J)"
FT /evidence="ECO:0000269|PubMed:15919810"
FT VARIANT 17
FT /note="S -> I (in strain: LG/J and SM/J)"
FT /evidence="ECO:0000269|PubMed:15919810"
FT VARIANT 19
FT /note="G -> C (in strain: LG/J and SM/J)"
FT /evidence="ECO:0000269|PubMed:15919810"
FT VARIANT 462
FT /note="V -> M (in strain: LG/J and SM/J)"
FT /evidence="ECO:0000269|PubMed:15919810"
FT VARIANT 546
FT /note="T -> K (in strain: LG/J and SM/J)"
FT /evidence="ECO:0000269|PubMed:15919810"
FT VARIANT 583
FT /note="I -> V (in strain: LG/J and SM/J)"
FT /evidence="ECO:0000269|PubMed:15919810"
FT CONFLICT 7
FT /note="R -> G (in Ref. 3; BAE37695)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="E -> D (in Ref. 3; BAE39514)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="Y -> C (in Ref. 3; BAE24630)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="Q -> P (in Ref. 2; AAX11356)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="R -> M (in Ref. 3; BAE40273)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="V -> L (in Ref. 4; BAC98102)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="A -> T (in Ref. 3; BAE40273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1036 AA; 117372 MW; D397879609881BF1 CRC64;
MWRFSGRRGL CAVQRLSCGR VHHRVWREKS DQACERALQY KVGEKIHGFT VNQVTPVPEL
FLTAVKLSHD NTGARYLHLA REDKNNLFSV QFRTTPMDST GVPHVLEHTV LCGSQKYPCR
DPFFKMLNRS LSTFMNAMTA SDYTIYPFST QNPKDFQNLL SVYLDATFFP CLRELDFWQE
GWRLEHENPR DPQTPLIFKG VVFNEMKGAF TDNERIFSQH LQNKLLPDHT YSVVSGGDPL
CIPELTWEQL KQFHATHYHP SNARFFTYGN FQLEGHLKQI HEEALSKFQR LEQSTAVPAQ
PHWDKPREFH ITCGPDSLAT ETAKQTTVSV SFLLPDITDT FEAFTLSLLS SLLIAGPNSP
FYKALIESGL GTDFSPDVGY NGYTREAYFS VGLQGIAEKD VKTVRELVDR TIEEVIEKGF
EDDRIEALLH KIEIQTKHQS ASFGLTLTSY IASCWNHDGD PVELLQIGSQ LTRFRKCLKE
NPKFLQEKVE QYFKNNQHKL TLSMKPDDKY YEKQTQMETE KLEQKVNSLS PADKQQIYEK
GLELQTQQSK HQDASCLPAL KVSDIEPSMP FTKLDIGLAA GDIPVQYCPQ PTNGMVYFRA
FSSLNTLPED LRPIVPLFCS VLTKLGCGIL NYREQAQQIE LKTGGMSVTP HVLPDDSQLD
TYEQGVLFSS LCLERNLPDM MHLWSEIFNN PCFEEEEHFK VLVKMTAQEL SNGISDSGHL
YAALRASKTL TPSGDLQETF SGMDQVKVMK RIAEMTDIKP ILRKLPRIKK YLLNCDNMRC
SVNATPQQMP QAEKEVENFL RNVGRSKKER KPVRPHIVEK PTPSGPSGAA HVSGSQIVRK
LVTDPTFKPC QMKTHFVLPF PVNYIGECVR TVPYADPDHA SLKILARLMT AKFLHTEIRE
KGGAYGGGAK LTHSGIFTLY SYRDPNSIET LQSFGKAVDW AKSGKFTQQD IDEAKLSVFS
TVDSPVAPSD KGMDHFLYGL SDEMKQAYRE QLFAVNHDKL TSVSHKYLGI GKSTHGLAIL
GPENSKIAKD PSWIIK
