TOM70_YEAST
ID TOM70_YEAST Reviewed; 617 AA.
AC P07213; B0KZR5; B0KZS4; B0KZU2; B0KZY7; B0KZZ6; B0L005; B0L023; D6W162;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Mitochondrial import receptor subunit TOM70;
DE AltName: Full=70 kDa mitochondrial outer membrane protein;
DE AltName: Full=Translocase of outer membrane 70 kDa subunit;
GN Name=TOM70; Synonyms=MAS70, OMP1; OrderedLocusNames=YNL121C;
GN ORFNames=N1905;
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].
RX PubMed=6365533; DOI=10.1002/j.1460-2075.1983.tb01718.x;
RA Hase T., Riezman H., Suda K., Schatz G.;
RT "Import of proteins into mitochondria: nucleotide sequence of the gene for
RT a 70-kd protein of the yeast mitochondrial outer membrane.";
RL EMBO J. 2:2169-2172(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-30; SER-68; HIS-277;
RP SER-359; ILE-364; HIS-385 AND GLY-429.
RC STRAIN=ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM 270,
RC YJM 320, YJM 326, YJM 339, YJM 627, and YJM230;
RX PubMed=18780730; DOI=10.1534/genetics.108.092932;
RA Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S.,
RA Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H.,
RA Steinmetz L.M.;
RT "Sequential elimination of major-effect contributors identifies additional
RT quantitative trait loci conditioning high-temperature growth in yeast.";
RL Genetics 180:1661-1670(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9090055;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l;
RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
RA Pallavicini A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces
RT cerevisiae reveals an unusually high number of overlapping open reading
RT frames.";
RL Yeast 13:261-266(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP DOMAINS TPR REPEATS.
RX PubMed=1694969; DOI=10.1038/346114a0;
RA Boguski M.S., Sikorski R.S., Hieter P.A., Goebl M.;
RT "Expanding family.";
RL Nature 346:114-114(1990).
RN [7]
RP CHARACTERIZATION.
RX PubMed=2170106; DOI=10.1002/j.1460-2075.1990.tb07517.x;
RA Hines V., Brandt A., Griffiths G., Horstmann H., Brutsch H., Schatz G.;
RT "Protein import into yeast mitochondria is accelerated by the outer
RT membrane protein MAS70.";
RL EMBO J. 9:3191-3200(1990).
RN [8]
RP CHARACTERIZATION.
RX PubMed=8380165; DOI=10.1016/s0021-9258(18)54172-7;
RA Hines V., Schatz G.;
RT "Precursor binding to yeast mitochondria. A general role for the outer
RT membrane protein Mas70p.";
RL J. Biol. Chem. 268:449-454(1993).
RN [9]
RP IDENTIFICATION IN THE TOM COMPLEX.
RX PubMed=9774667; DOI=10.1128/mcb.18.11.6515;
RA Dekker P.J.T., Ryan M.T., Brix J., Mueller H., Hoenlinger A., Pfanner N.;
RT "Preprotein translocase of the outer mitochondrial membrane: molecular
RT dissection and assembly of the general import pore complex.";
RL Mol. Cell. Biol. 18:6515-6524(1998).
RN [10]
RP INTERACTION WITH TOM22.
RX PubMed=10519552; DOI=10.1038/46802;
RA van Wilpe S., Ryan M.T., Hill K., Maarse A.C., Meisinger C., Brix J.,
RA Dekker P.J.T., Moczko M., Wagner R., Meijer M., Guiard B., Hoenlinger A.,
RA Pfanner N.;
RT "Tom22 is a multifunctional organizer of the mitochondrial preprotein
RT translocase.";
RL Nature 401:485-489(1999).
RN [11]
RP FUNCTION.
RX PubMed=11054285; DOI=10.1006/jmbi.2000.4120;
RA Brix J., Ziegler G.A., Dietmeier K., Schneider-Mergener J., Schulz G.E.,
RA Pfanner N.;
RT "The mitochondrial import receptor Tom70: identification of a 25 kDa core
RT domain with a specific binding site for preproteins.";
RL J. Mol. Biol. 303:479-488(2000).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [16]
RP IDENTIFICATION BY 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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the TOM (translocase of outer membrane) receptor
CC complex responsible for the recognition and translocation of
CC cytosolically synthesized mitochondrial preproteins. Together with
CC TOM20 and TOM22 functions as the transit peptide receptor at the
CC surface of the mitochondrion outer membrane and facilitates the
CC movement of preproteins into the TOM40 translocation pore.
CC {ECO:0000269|PubMed:11054285}.
CC -!- SUBUNIT: Forms part of the TOM (translocase of outer membrane) complex
CC that consists of at least 7 different proteins (TOM5, TOM6, TOM7,
CC TOM20, TOM22, TOM40 and TOM70). In the complex interacts with TOM22.
CC Interacts with TOM37. {ECO:0000269|PubMed:10519552,
CC ECO:0000269|PubMed:9774667}.
CC -!- INTERACTION:
CC P07213; Q07812: BAX; Xeno; NbExp=2; IntAct=EBI-12551, EBI-516580;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:11502169}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11502169}.
CC -!- MISCELLANEOUS: Present with 45300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Tom70 family. {ECO:0000305}.
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DR EMBL; X05585; CAA29085.1; -; Genomic_DNA.
DR EMBL; EF125216; ABN58537.1; -; Genomic_DNA.
DR EMBL; EF125217; ABN58546.1; -; Genomic_DNA.
DR EMBL; EF125218; ABN58555.1; -; Genomic_DNA.
DR EMBL; EF125219; ABN58564.1; -; Genomic_DNA.
DR EMBL; EF125220; ABN58573.1; -; Genomic_DNA.
DR EMBL; EF125221; ABN58582.1; -; Genomic_DNA.
DR EMBL; EF125222; ABN58591.1; -; Genomic_DNA.
DR EMBL; EF125223; ABN58600.1; -; Genomic_DNA.
DR EMBL; EF125224; ABN58609.1; -; Genomic_DNA.
DR EMBL; EF125225; ABN58618.1; -; Genomic_DNA.
DR EMBL; EF125226; ABN58627.1; -; Genomic_DNA.
DR EMBL; EF125228; ABN58645.1; -; Genomic_DNA.
DR EMBL; Z69382; CAA93386.1; -; Genomic_DNA.
DR EMBL; Z71397; CAA96002.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10428.1; -; Genomic_DNA.
DR PIR; S63062; MMBYO.
DR RefSeq; NP_014278.3; NM_001182959.3.
DR PDB; 2GW1; X-ray; 3.00 A; A/B=94-607.
DR PDBsum; 2GW1; -.
DR AlphaFoldDB; P07213; -.
DR SMR; P07213; -.
DR BioGRID; 35706; 300.
DR ComplexPortal; CPX-474; TOM40 mitochondrial outer membrane translocase holocomplex.
DR DIP; DIP-2301N; -.
DR IntAct; P07213; 14.
DR MINT; P07213; -.
DR STRING; 4932.YNL121C; -.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR iPTMnet; P07213; -.
DR MaxQB; P07213; -.
DR PaxDb; P07213; -.
DR PRIDE; P07213; -.
DR EnsemblFungi; YNL121C_mRNA; YNL121C; YNL121C.
DR GeneID; 855602; -.
DR KEGG; sce:YNL121C; -.
DR SGD; S000005065; TOM70.
DR VEuPathDB; FungiDB:YNL121C; -.
DR eggNOG; KOG0547; Eukaryota.
DR GeneTree; ENSGT00940000176538; -.
DR HOGENOM; CLU_017516_1_0_1; -.
DR InParanoid; P07213; -.
DR OMA; HEATKDM; -.
DR BioCyc; YEAST:G3O-33142-MON; -.
DR EvolutionaryTrace; P07213; -.
DR PRO; PR:P07213; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P07213; protein.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:ComplexPortal.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0030943; F:mitochondrion targeting sequence binding; IMP:SGD.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IDA:ComplexPortal.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IGI:SGD.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR005687; Tom70.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR TIGRFAMs; TIGR00990; 3a0801s09; 1.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Reference proteome; Repeat; TPR repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..617
FT /note="Mitochondrial import receptor subunit TOM70"
FT /id="PRO_0000106340"
FT TOPO_DOM 1..10
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..617
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 99..132
FT /note="TPR 1"
FT REPEAT 134..165
FT /note="TPR 2"
FT REPEAT 281..315
FT /note="TPR 3"
FT REPEAT 363..396
FT /note="TPR 4"
FT REPEAT 397..430
FT /note="TPR 5"
FT REPEAT 432..464
FT /note="TPR 6"
FT REPEAT 465..498
FT /note="TPR 7"
FT REPEAT 505..541
FT /note="TPR 8"
FT REPEAT 542..575
FT /note="TPR 9"
FT REGION 36..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT VARIANT 30
FT /note="N -> S (in strain: SK1, V1-09, YJM339 and YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 68
FT /note="P -> S (in strain: V1-09 and YJM627)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 277
FT /note="N -> H (in strain: YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 359
FT /note="L -> S (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 364
FT /note="N -> I (in strain: YJM269 and YJM270)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 385
FT /note="Y -> H (in strain: YJM1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 429
FT /note="E -> G (in strain: V1-09)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT CONFLICT 185
FT /note="A -> R (in Ref. 1; CAA29085)"
FT /evidence="ECO:0000305"
FT HELIX 95..111
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:2GW1"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 204..219
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 254..261
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 278..290
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 297..315
FT /evidence="ECO:0007829|PDB:2GW1"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 323..342
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 346..359
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 385..390
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 398..409
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 415..425
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 432..440
FT /evidence="ECO:0007829|PDB:2GW1"
FT TURN 441..445
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 447..460
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 466..477
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 481..496
FT /evidence="ECO:0007829|PDB:2GW1"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 506..516
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 523..537
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 542..554
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 558..571
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 575..594
FT /evidence="ECO:0007829|PDB:2GW1"
FT HELIX 598..605
FT /evidence="ECO:0007829|PDB:2GW1"
SQ SEQUENCE 617 AA; 70123 MW; 664B8FC32CCE39A2 CRC64;
MKSFITRNKT AILATVAATG TAIGAYYYYN QLQQQQQRGK KNTINKDEKK DTKDSQKETE
GAKKSTAPSN PPIYPVSSNG EPDFSNKANF TAEEKDKYAL ALKDKGNQFF RNKKYDDAIK
YYNWALELKE DPVFYSNLSA CYVSVGDLKK VVEMSTKALE LKPDYSKVLL RRASANEGLG
KFADAMFDLS VLSLNGDFND ASIEPMLERN LNKQAMSKLK EKFGDIDTAT ATPTELSTQP
AKERKDKQEN LPSVTSMASF FGIFKPELTF ANYDESNEAD KELMNGLSNL YKRSPESYDK
ADESFTKAAR LFEEQLDKNN EDEKLKEKLA ISLEHTGIFK FLKNDPLGAH EDIKKAIELF
PRVNSYIYMA LIMADRNDST EYYNYFDKAL KLDSNNSSVY YHRGQMNFIL QNYDQAGKDF
DKAKELDPEN IFPYIQLACL AYRENKFDDC ETLFSEAKRK FPEAPEVPNF FAEILTDKND
FDKALKQYDL AIELENKLDG IYVGIAPLVG KATLLTRNPT VENFIEATNL LEKASKLDPR
SEQAKIGLAQ MKLQQEDIDE AITLFEESAD LARTMEEKLQ AITFAEAAKV QQRIRSDPVL
AKKIQETLAK LREQGLM
