ID   MPPB_YEAST              Reviewed;         462 AA.
AC   P10507; D6VYG9;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 215.
DE   RecName: Full=Mitochondrial-processing peptidase subunit beta {ECO:0000303|PubMed:9299349};
DE            EC=3.4.24.64 {ECO:0000269|PubMed:2007593, ECO:0000269|PubMed:9299349, ECO:0000269|PubMed:9654444};
DE   AltName: Full=Beta-MPP;
DE   AltName: Full=Mitochondrial assembly protein 1 {ECO:0000303|PubMed:3044780};
DE   AltName: Full=Processing enhancing protein {ECO:0000303|PubMed:3061797};
DE            Short=PEP;
DE   Flags: Precursor;
GN   Name=MAS1 {ECO:0000303|PubMed:3044780};
GN   Synonyms=MIF1 {ECO:0000303|PubMed:3061797};
GN   OrderedLocusNames=YLR163C {ECO:0000312|SGD:S000004153};
GN   ORFNames=L9632.10;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX   PubMed=3044780; DOI=10.1002/j.1460-2075.1988.tb02961.x;
RA   Witte C., Jensen R.E., Yaffe M.P., Schatz G.;
RT   "MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit
RT   of the mitochondrial processing protease.";
RL   EMBO J. 7:1439-1447(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   PROTEIN SEQUENCE OF 21-32, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=2007593; DOI=10.1016/s0021-9258(18)38134-1;
RA   Yang M., Geli V., Oppliger W., Suda K., James P., Schatz G.;
RT   "The MAS-encoded processing protease of yeast mitochondria. Interaction of
RT   the purified enzyme with signal peptides and a purified precursor
RT   protein.";
RL   J. Biol. Chem. 266:6416-6423(1991).
RN   [6]
RP   FUNCTION.
RX   PubMed=3061797; DOI=10.1002/j.1460-2075.1988.tb03225.x;
RA   Pollock R.A., Hartl F.-U., Cheng M.Y., Ostermann J., Horwich A.,
RA   Neupert W.;
RT   "The processing peptidase of yeast mitochondria: the two co-operating
RT   components MPP and PEP are structurally related.";
RL   EMBO J. 7:3493-3500(1988).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH MAS2,
RP   AND MUTAGENESIS OF GLU-89; SER-133; TYR-198; LYS-234; PRO-249; THR-301;
RP   SER-333; LYS-364 AND ARG-400.
RX   PubMed=9299349; DOI=10.1006/jmbi.1997.1231;
RA   Luciano P., Geoffroy S., Brandt A., Hernandez J.F., Geli V.;
RT   "Functional cooperation of the mitochondrial processing peptidase
RT   subunits.";
RL   J. Mol. Biol. 272:213-225(1997).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP   MUTAGENESIS OF HIS-70.
RX   PubMed=9654444; DOI=10.1006/jmbi.1998.1858;
RA   Luciano P., Tokatlidis K., Chambre I., Germanique J.C., Geli V.;
RT   "The mitochondrial processing peptidase behaves as a zinc-
RT   metallopeptidase.";
RL   J. Mol. Biol. 280:193-199(1998).
RN   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=25176146; DOI=10.1016/j.cmet.2014.07.024;
RA   Mossmann D., Voegtle F.N., Taskin A.A., Teixeira P.F., Ring J.,
RA   Burkhart J.M., Burger N., Pinho C.M., Tadic J., Loreth D., Graff C.,
RA   Metzger F., Sickmann A., Kretz O., Wiedemann N., Zahedi R.P., Madeo F.,
RA   Glaser E., Meisinger C.;
RT   "Amyloid-beta peptide induces mitochondrial dysfunction by inhibition of
RT   preprotein maturation.";
RL   Cell Metab. 20:662-669(2014).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 21-462 IN COMPLEX WITH MAS2; ZINC
RP   AND SUBSTRATES, AND ACTIVE SITE.
RX   PubMed=11470436; DOI=10.1016/s0969-2126(01)00621-9;
RA   Taylor A.B., Smith B.S., Kitada S., Kojima K., Miyaura H., Otwinowski Z.,
RA   Ito A., Deisenhofer J.;
RT   "Crystal structures of mitochondrial processing peptidase reveal the mode
RT   for specific cleavage of import signal sequences.";
RL   Structure 9:615-625(2001).
CC   -!- FUNCTION: Catalytic subunit of the essential mitochondrial processing
CC       protease (MPP), which cleaves the mitochondrial sequence off newly
CC       imported precursors proteins (PubMed:2007593, PubMed:9299349,
CC       PubMed:9654444). Preferentially, cleaves after an arginine at position
CC       P2 (By similarity). {ECO:0000250|UniProtKB:Q03346,
CC       ECO:0000269|PubMed:2007593, ECO:0000269|PubMed:9299349,
CC       ECO:0000269|PubMed:9654444}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal transit peptides from precursor proteins
CC         imported into the mitochondrion, typically with Arg in position P2.;
CC         EC=3.4.24.64; Evidence={ECO:0000269|PubMed:2007593,
CC         ECO:0000269|PubMed:9299349, ECO:0000269|PubMed:9654444};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:9654444};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:11470436,
CC       ECO:0000269|PubMed:9654444};
CC   -!- ACTIVITY REGULATION: Binding to MAS2 is required for catalytic activity
CC       (PubMed:9654444, PubMed:9299349). Inhibited by high levels (> 1uM) of
CC       zinc (PubMed:9654444). Inhibited by metal chelators
CC       ethylenediaminetetraacetic acid (EDTA) and O-phenanthroline
CC       (PubMed:9654444). {ECO:0000269|PubMed:9299349,
CC       ECO:0000269|PubMed:9654444}.
CC   -!- SUBUNIT: Heterodimer of MAS2 (alpha) and MAS1 (beta) subunits, forming
CC       the mitochondrial processing protease (MPP) in which MAS2 is involved
CC       in substrate recognition and binding and MAS1 is the catalytic subunit.
CC       {ECO:0000269|PubMed:11470436, ECO:0000269|PubMed:9299349}.
CC   -!- INTERACTION:
CC       P10507; P11914: MAS2; NbExp=4; IntAct=EBI-11212, EBI-11205;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:3044780}.
CC   -!- DISRUPTION PHENOTYPE: Simultaneous disruption of the mitochondrial
CC       presequence protease CYM1 results in synthetic lethality in respiratory
CC       conditions. {ECO:0000269|PubMed:25176146}.
CC   -!- MISCELLANEOUS: Present with 1360 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; X07649; CAA30489.1; -; Genomic_DNA.
DR   EMBL; U51921; AAB67487.1; -; Genomic_DNA.
DR   EMBL; AY693198; AAT93217.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09485.1; -; Genomic_DNA.
DR   PIR; S00552; S00552.
DR   RefSeq; NP_013264.1; NM_001182050.1.
DR   PDB; 1HR6; X-ray; 2.50 A; B/D/F/H=21-462.
DR   PDB; 1HR7; X-ray; 2.55 A; B/D/F/H=21-462.
DR   PDB; 1HR8; X-ray; 2.70 A; B/D/F/H=21-462.
DR   PDB; 1HR9; X-ray; 3.01 A; B/D/F/H=21-462.
DR   PDBsum; 1HR6; -.
DR   PDBsum; 1HR7; -.
DR   PDBsum; 1HR8; -.
DR   PDBsum; 1HR9; -.
DR   AlphaFoldDB; P10507; -.
DR   SMR; P10507; -.
DR   BioGRID; 31436; 101.
DR   ComplexPortal; CPX-1630; Mitochondrial processing peptidase complex.
DR   DIP; DIP-2402N; -.
DR   IntAct; P10507; 16.
DR   MINT; P10507; -.
DR   STRING; 4932.YLR163C; -.
DR   MEROPS; M16.003; -.
DR   MEROPS; M16.980; -.
DR   iPTMnet; P10507; -.
DR   MaxQB; P10507; -.
DR   PaxDb; 4932-YLR163C; -.
DR   PeptideAtlas; P10507; -.
DR   EnsemblFungi; YLR163C_mRNA; YLR163C; YLR163C.
DR   GeneID; 850860; -.
DR   KEGG; sce:YLR163C; -.
DR   AGR; SGD:S000004153; -.
DR   SGD; S000004153; MAS1.
DR   VEuPathDB; FungiDB:YLR163C; -.
DR   eggNOG; KOG0960; Eukaryota.
DR   GeneTree; ENSGT00940000156608; -.
DR   HOGENOM; CLU_009902_4_0_1; -.
DR   InParanoid; P10507; -.
DR   OMA; IDVVCDM; -.
DR   OrthoDB; 167798at2759; -.
DR   BioCyc; MetaCyc:G3O-32293-MONOMER; -.
DR   BioCyc; YEAST:G3O-32293-MONOMER; -.
DR   BRENDA; 3.4.24.64; 984.
DR   Reactome; R-SCE-611105; Respiratory electron transport.
DR   SABIO-RK; P10507; -.
DR   BioGRID-ORCS; 850860; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P10507; -.
DR   PRO; PR:P10507; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P10507; Protein.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0017087; C:mitochondrial processing peptidase complex; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IDA:SGD.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Metalloprotease; Mitochondrion; Phosphoprotein; Protease;
KW   Reference proteome; Transit peptide; Zinc.
FT   TRANSIT         1..20
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2007593"
FT   CHAIN           21..462
FT                   /note="Mitochondrial-processing peptidase subunit beta"
FT                   /id="PRO_0000026784"
FT   ACT_SITE        73
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000269|PubMed:11470436,
FT                   ECO:0007744|PDB:1HR6"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096,
FT                   ECO:0000269|PubMed:11470436, ECO:0000269|PubMed:9654444,
FT                   ECO:0007744|PDB:1HR6, ECO:0007744|PDB:1HR7,
FT                   ECO:0007744|PDB:1HR8, ECO:0007744|PDB:1HR9"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096,
FT                   ECO:0000269|PubMed:11470436, ECO:0007744|PDB:1HR6,
FT                   ECO:0007744|PDB:1HR7, ECO:0007744|PDB:1HR8,
FT                   ECO:0007744|PDB:1HR9"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096,
FT                   ECO:0000269|PubMed:11470436, ECO:0007744|PDB:1HR6,
FT                   ECO:0007744|PDB:1HR7, ECO:0007744|PDB:1HR8,
FT                   ECO:0007744|PDB:1HR9"
FT   MOD_RES         243
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         70
FT                   /note="H->R: Loss of zinc binding. Loss of catalytic
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:9654444"
FT   MUTAGEN         89
FT                   /note="E->A: Loss of catalytic activity and loss of binding
FT                   to MAS2."
FT                   /evidence="ECO:0000269|PubMed:9299349"
FT   MUTAGEN         133
FT                   /note="S->A: Loss of catalytic activity. No effect on the
FT                   binding to MAS2."
FT                   /evidence="ECO:0000269|PubMed:9299349"
FT   MUTAGEN         198
FT                   /note="Y->A: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:9299349"
FT   MUTAGEN         234
FT                   /note="K->A: Loss of catalytic activity and loss of binding
FT                   to MAS2."
FT                   /evidence="ECO:0000269|PubMed:9299349"
FT   MUTAGEN         249
FT                   /note="P->A: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:9299349"
FT   MUTAGEN         301
FT                   /note="T->A: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:9299349"
FT   MUTAGEN         333
FT                   /note="S->A: Loss of catalytic activity. No effect on the
FT                   binding to MAS2."
FT                   /evidence="ECO:0000269|PubMed:9299349"
FT   MUTAGEN         364
FT                   /note="K->A: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:9299349"
FT   MUTAGEN         400
FT                   /note="R->A: No effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:9299349"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          46..55
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   TURN            63..67
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           68..75
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           85..94
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          98..103
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          105..115
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           119..131
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           137..154
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           158..170
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           184..189
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           192..202
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          208..215
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           218..229
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          254..259
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          264..273
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           282..292
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          294..296
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   TURN            297..299
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          302..305
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           308..314
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          321..329
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          334..343
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   TURN            344..346
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           349..364
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           370..385
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           391..405
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           411..419
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           423..433
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          434..436
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   STRAND          439..445
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           447..449
FT                   /evidence="ECO:0007829|PDB:1HR6"
FT   HELIX           453..461
FT                   /evidence="ECO:0007829|PDB:1HR6"
SQ   SEQUENCE   462 AA;  51084 MW;  084CE63C495EDFC4 CRC64;
     MFSRTASKFR NTRRLLSTIS SQIPGTRTSK LPNGLTIATE YIPNTSSATV GIFVDAGSRA
     ENVKNNGTAH FLEHLAFKGT QNRSQQGIEL EIENIGSHLN AYTSRENTVY YAKSLQEDIP
     KAVDILSDIL TKSVLDNSAI ERERDVIIRE SEEVDKMYDE VVFDHLHEIT YKDQPLGRTI
     LGPIKNIKSI TRTDLKDYIT KNYKGDRMVL AGAGAVDHEK LVQYAQKYFG HVPKSESPVP
     LGSPRGPLPV FCRGERFIKE NTLPTTHIAI ALEGVSWSAP DYFVALATQA IVGNWDRAIG
     TGTNSPSPLA VAASQNGSLA NSYMSFSTSY ADSGLWGMYI VTDSNEHNVQ LIVNEILKEW
     KRIKSGKISD AEVNRAKAQL KAALLLSLDG STAIVEDIGR QVVTTGKRLS PEEVFEQVDK
     ITKDDIIMWA NYRLQNKPVS MVALGNTSTV PNVSYIEEKL NQ
//