KEX1_YEAST
ID KEX1_YEAST Reviewed; 729 AA.
AC P09620; D6VTV1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Pheromone-processing carboxypeptidase KEX1;
DE EC=3.4.16.6;
DE AltName: Full=Carboxypeptidase D;
DE AltName: Full=Killer expression defective protein 1;
DE Flags: Precursor;
GN Name=KEX1; OrderedLocusNames=YGL203C;
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], FUNCTION, AND MUTAGENESIS OF SER-198.
RX PubMed=3301004; DOI=10.1016/0092-8674(87)90030-4;
RA Dmochowska A., Dignard D., Henning D., Thomas D.Y., Bussey H.;
RT "Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like
RT function involved in killer toxin and alpha-factor precursor processing.";
RL Cell 50:573-584(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 FUNCTION.
RX PubMed=4364866; DOI=10.1093/genetics/76.3.423;
RA Wickner R.B.;
RT "Chromosomal and nonchromosomal mutations affecting the 'killer character'
RT of Saccharomyces cerevisiae.";
RL Genetics 76:423-432(1974).
RN [5]
RP FUNCTION.
RX PubMed=773743; DOI=10.1093/genetics/82.3.429;
RA Wickner R.B., Leibowitz M.J.;
RT "Two chromosomal genes required for killing expression in killer strains of
RT Saccharomyces cerevisiae.";
RL Genetics 82:429-442(1976).
RN [6]
RP FUNCTION.
RX PubMed=3305079; DOI=10.1016/0014-5793(87)80967-5;
RA Wagner J.C., Wolf D.H.;
RT "Hormone (pheromone) processing enzymes in yeast. The carboxy-terminal
RT processing enzyme of the mating pheromone alpha-factor, carboxypeptidase
RT ysc alpha, is absent in alpha-factor maturation-defective kex1 mutant
RT cells.";
RL FEBS Lett. 221:423-426(1987).
RN [7]
RP FUNCTION.
RX PubMed=3301840; DOI=10.1016/s0021-9258(18)61024-5;
RA Zhu H., Bussey H., Thomas D.Y., Gagnon J., Bell A.W.;
RT "Determination of the carboxyl termini of the alpha and beta subunits of
RT yeast K1 killer toxin. Requirement of a carboxypeptidase B-like activity
RT for maturation.";
RL J. Biol. Chem. 262:10728-10732(1987).
RN [8]
RP CHARACTERIZATION.
RX PubMed=2668738; DOI=10.1128/mcb.9.6.2706-2714.1989;
RA Cooper A., Bussey H.;
RT "Characterization of the yeast KEX1 gene product: a carboxypeptidase
RT involved in processing secreted precursor proteins.";
RL Mol. Cell. Biol. 9:2706-2714(1989).
RN [9]
RP GLYCOSYLATION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1469044; DOI=10.1083/jcb.119.6.1459;
RA Cooper A., Bussey H.;
RT "Yeast Kex1p is a Golgi-associated membrane protein: deletions in a
RT cytoplasmic targeting domain result in mislocalization to the vacuolar
RT membrane.";
RL J. Cell Biol. 119:1459-1468(1992).
RN [10]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8416959; DOI=10.1016/s0021-9258(18)54184-3;
RA Latchinian-Sadek L., Thomas D.Y.;
RT "Expression, purification, and characterization of the yeast KEX1 gene
RT product, a polypeptide precursor processing carboxypeptidase.";
RL J. Biol. Chem. 268:534-540(1993).
RN [11]
RP FUNCTION.
RX PubMed=10972812; DOI=10.1046/j.1365-2958.2000.02063.x;
RA Eisfeld K., Riffer F., Mentges J., Schmitt M.J.;
RT "Endocytotic uptake and retrograde transport of a virally encoded killer
RT toxin in yeast.";
RL Mol. Microbiol. 37:926-940(2000).
RN [12]
RP FUNCTION.
RX PubMed=11988505; DOI=10.1099/00221287-148-5-1317;
RA Riffer F., Eisfeld K., Breinig F., Schmitt M.J.;
RT "Mutational analysis of K28 preprotoxin processing in the yeast
RT Saccharomyces cerevisiae.";
RL Microbiology 148:1317-1328(2002).
RN [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [14]
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 [15]
RP FUNCTION.
RX PubMed=17210951; DOI=10.1083/jcb.200609182;
RA Heiman M.G., Engel A., Walter P.;
RT "The Golgi-resident protease Kex2 acts in conjunction with Prm1 to
RT facilitate cell fusion during yeast mating.";
RL J. Cell Biol. 176:209-222(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660, 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 [17]
RP FUNCTION.
RX PubMed=18474590; DOI=10.1074/jbc.m801303200;
RA Hauptmann P., Lehle L.;
RT "Kex1 protease is involved in yeast cell death induced by defective N-
RT glycosylation, acetic acid, and chronological aging.";
RL J. Biol. Chem. 283:19151-19163(2008).
RN [18]
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 [19]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8745419; DOI=10.1002/pro.5560050225;
RA Shilton B.H., Li Y., Tessier D., Thomas D.Y., Cygler M.;
RT "Crystallization of a soluble form of the Kex1p serine carboxypeptidase
RT from Saccharomyces cerevisiae.";
RL Protein Sci. 5:395-397(1996).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 23-505.
RX PubMed=9220988; DOI=10.1021/bi970433n;
RA Shilton B.H., Thomas D.Y., Cygler M.;
RT "Crystal structure of Kex1deltap, a prohormone-processing carboxypeptidase
RT from Saccharomyces cerevisiae.";
RL Biochemistry 36:9002-9012(1997).
CC -!- FUNCTION: Protease with a carboxypeptidase B-like function involved in
CC the C-terminal processing of the lysine and arginine residues from the
CC precursors of K1, K2 and K28 killer toxins and a-factor (mating
CC pheromone). Involved in the programmed cell death caused by defective
CC N-glycosylation and contributes also to the active cell death program
CC induced by acetic acid stress or during chronological aging. Promotes
CC cell fusion by proteolytically processing substrates that act in
CC parallel to PRM1 as an alternative fusion machine, as cell wall
CC components, or both. {ECO:0000269|PubMed:10972812,
CC ECO:0000269|PubMed:11988505, ECO:0000269|PubMed:1469044,
CC ECO:0000269|PubMed:17210951, ECO:0000269|PubMed:18474590,
CC ECO:0000269|PubMed:3301004, ECO:0000269|PubMed:3301840,
CC ECO:0000269|PubMed:3305079, ECO:0000269|PubMed:4364866,
CC ECO:0000269|PubMed:773743, ECO:0000269|PubMed:8416959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential release of a C-terminal arginine or lysine
CC residue.; EC=3.4.16.6;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=284 uM for benzoyl-Phe-Ala-Arg {ECO:0000269|PubMed:8416959};
CC KM=516 uM for furylacryloyl-Ala-Arg {ECO:0000269|PubMed:8416959};
CC KM=962 uM for furylacryloyl-Ala-Lys {ECO:0000269|PubMed:8416959};
CC Vmax=64.25 umol/min/mg enzyme toward benzoyl-Phe-Ala-Arg
CC {ECO:0000269|PubMed:8416959};
CC Vmax=22.35 umol/min/mg enzyme toward furylacryloyl-Ala-Arg
CC {ECO:0000269|PubMed:8416959};
CC Vmax=11.55 umol/min/mg enzyme toward furylacryloyl-Ala-Lys
CC {ECO:0000269|PubMed:8416959};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:1469044}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:1469044}.
CC -!- MISCELLANEOUS: Present with 8550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M17231; AAA34717.1; -; Genomic_DNA.
DR EMBL; Z72725; CAA96915.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07912.1; -; Genomic_DNA.
DR PIR; A29651; A29651.
DR RefSeq; NP_011312.1; NM_001181068.1.
DR PDB; 1AC5; X-ray; 2.40 A; A=23-505.
DR PDBsum; 1AC5; -.
DR AlphaFoldDB; P09620; -.
DR SMR; P09620; -.
DR BioGRID; 33053; 223.
DR IntAct; P09620; 58.
DR MINT; P09620; -.
DR STRING; 4932.YGL203C; -.
DR ESTHER; yeast-kex01; Carboxypeptidase_S10.
DR MEROPS; S10.007; -.
DR iPTMnet; P09620; -.
DR MaxQB; P09620; -.
DR PaxDb; P09620; -.
DR PRIDE; P09620; -.
DR EnsemblFungi; YGL203C_mRNA; YGL203C; YGL203C.
DR GeneID; 852670; -.
DR KEGG; sce:YGL203C; -.
DR SGD; S000003171; KEX1.
DR VEuPathDB; FungiDB:YGL203C; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_11_2_1; -.
DR InParanoid; P09620; -.
DR OMA; EMADQFV; -.
DR BioCyc; MetaCyc:YGL203C-MON; -.
DR BioCyc; YEAST:YGL203C-MON; -.
DR BRENDA; 3.4.16.6; 984.
DR EvolutionaryTrace; P09620; -.
DR PRO; PR:P09620; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P09620; protein.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IDA:SGD.
DR GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Carboxypeptidase; Glycoprotein; Golgi apparatus;
KW Hydrolase; Membrane; Phosphoprotein; Protease; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT CHAIN 23..729
FT /note="Pheromone-processing carboxypeptidase KEX1"
FT /id="PRO_0000004287"
FT TOPO_DOM 23..616
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 638..729
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 502..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..580
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT ACT_SITE 405
FT /evidence="ECO:0000250"
FT ACT_SITE 470
FT /evidence="ECO:0000250"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1469044"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1469044"
FT MUTAGEN 198
FT /note="S->A: Inactivates enzyme."
FT /evidence="ECO:0000269|PubMed:3301004"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1AC5"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 166..183
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 200..217
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 263..279
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:1AC5"
FT TURN 327..333
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:1AC5"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 369..374
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 387..392
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 396..402
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 410..419
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 433..439
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 452..457
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 472..475
FT /evidence="ECO:0007829|PDB:1AC5"
FT HELIX 477..487
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 492..496
FT /evidence="ECO:0007829|PDB:1AC5"
FT STRAND 499..504
FT /evidence="ECO:0007829|PDB:1AC5"
SQ SEQUENCE 729 AA; 82245 MW; 70583F279AC02A41 CRC64;
MFYNRWLGTW LAMSALIRIS VSLPSSEEYK VAYELLPGLS EVPDPSNIPQ MHAGHIPLRS
EDADEQDSSD LEYFFWKFTN NDSNGNVDRP LIIWLNGGPG CSSMDGALVE SGPFRVNSDG
KLYLNEGSWI SKGDLLFIDQ PTGTGFSVEQ NKDEGKIDKN KFDEDLEDVT KHFMDFLENY
FKIFPEDLTR KIILSGESYA GQYIPFFANA ILNHNKFSKI DGDTYDLKAL LIGNGWIDPN
TQSLSYLPFA MEKKLIDESN PNFKHLTNAH ENCQNLINSA STDEAAHFSY QECENILNLL
LSYTRESSQK GTADCLNMYN FNLKDSYPSC GMNWPKDISF VSKFFSTPGV IDSLHLDSDK
IDHWKECTNS VGTKLSNPIS KPSIHLLPGL LESGIEIVLF NGDKDLICNN KGVLDTIDNL
KWGGIKGFSD DAVSFDWIHK SKSTDDSEEF SGYVKYDRNL TFVSVYNASH MVPFDKSLVS
RGIVDIYSND VMIIDNNGKN VMITTDDDSD QDATTESGDK PKENLEEEEQ EAQNEEGKEK
EGNKDKDGDD DNDNDDDDED DHNSEGDDDD DDDDDEDDNN EKQSNQGLED SRHKSSEYEQ
EEEEVEEFAE EISMYKHKAV VVTIVTFLIV VLGVYAYDRR VRRKARHTIL VDPNNRQHDS
PNKTVSWADD LESGLGAEDD LEQDEQLEGG APISSTSNKA GSKLKTKKKK KYTSLPNTEI
DESFEMTDF
