PSD2_YEAST
ID PSD2_YEAST Reviewed; 1138 AA.
AC P53037; D6VUV4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme 2 {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:7890740};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:7890739};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 2 beta chain {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:20016005};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 2 alpha chain {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:20016005};
GN Name=PSD2 {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000303|PubMed:7890739};
GN OrderedLocusNames=YGR170W {ECO:0000312|SGD:S000003402};
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 SUBCELLULAR LOCATION.
RC STRAIN=PTY36;
RX PubMed=7890740; DOI=10.1074/jbc.270.11.6071;
RA Trotter P.J., Pedretti J., Yates R., Voelker D.R.;
RT "Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae. Cloning
RT and mapping of the gene, heterologous expression, and creation of the null
RT allele.";
RL J. Biol. Chem. 270:6071-6080(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
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 [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=7890739; DOI=10.1074/jbc.270.11.6062;
RA Trotter P.J., Voelker D.R.;
RT "Identification of a non-mitochondrial phosphatidylserine decarboxylase
RT activity (PSD2) in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:6062-6070(1995).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11104779; DOI=10.1074/jbc.m010278200;
RA Wu W.I., Voelker D.R.;
RT "Characterization of phosphatidylserine transport to the locus of
RT phosphatidylserine decarboxylase 2 in permeabilized yeast.";
RL J. Biol. Chem. 276:7114-7121(2001).
RN [7]
RP FUNCTION.
RX PubMed=11294902; DOI=10.1091/mbc.12.4.997;
RA Birner R., Buergermeister M., Schneiter R., Daum G.;
RT "Roles of phosphatidylethanolamine and of its several biosynthetic pathways
RT in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 12:997-1007(2001).
RN [8]
RP DOMAIN.
RX PubMed=12093819; DOI=10.1074/jbc.m205672200;
RA Kitamura H., Wu W.I., Voelker D.R.;
RT "The C2 domain of phosphatidylserine decarboxylase 2 is not required for
RT catalysis but is essential for in vivo function.";
RL J. Biol. Chem. 277:33720-33726(2002).
RN [9]
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 1041-GLY--SER-1043, AND
RP INTERACTION WITH PDR17.
RX PubMed=20016005; DOI=10.1091/mbc.e09-06-0519;
RA Gulshan K., Shahi P., Moye-Rowley W.S.;
RT "Compartment-specific synthesis of phosphatidylethanolamine is required for
RT normal heavy metal resistance.";
RL Mol. Biol. Cell 21:443-455(2010).
RN [11]
RP FUNCTION, DOMAIN, AND INTERACTION WITH PDR17.
RX PubMed=24366873; DOI=10.1074/jbc.m113.518217;
RA Riekhof W.R., Wu W.I., Jones J.L., Nikrad M., Chan M.M., Loewen C.J.,
RA Voelker D.R.;
RT "An assembly of proteins and lipid domains regulates transport of
RT phosphatidylserine to phosphatidylserine decarboxylase 2 in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 289:5809-5819(2014).
CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC from phosphatidylserine (PtdSer). Plays a central role in phospholipid
CC metabolism and in the interorganelle trafficking of phosphatidylserine
CC (PubMed:7890740, PubMed:7890739, PubMed:24366873).
CC Phosphatidylethanolamine produced by PSD2 is insufficient to completely
CC provide the PtdEtn pool required by mitochondria under respiratory
CC conditions (PubMed:11294902). PSD2 is also involved in the PtdSer
CC transport step to the site of PtdEtn synthesis on the Golgi/endosome
CC membranes (PubMed:24366873). Required for normal heavy metal resistance
CC (PubMed:20016005). {ECO:0000255|HAMAP-Rule:MF_03209,
CC ECO:0000269|PubMed:11294902, ECO:0000269|PubMed:20016005,
CC ECO:0000269|PubMed:24366873, ECO:0000269|PubMed:7890739,
CC ECO:0000269|PubMed:7890740}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03209, ECO:0000269|PubMed:7890739};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000250|UniProtKB:P0A8K1,
CC ECO:0000255|HAMAP-Rule:MF_03209};
CC Note=Binds 1 pyruvoyl group covalently per subunit.
CC {ECO:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-Rule:MF_03209};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:7890739}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit (By similarity). Interacts with
CC pstB2/PDR17 (PubMed:20016005, PubMed:24366873). This interaction may be
CC a means to structurally tether the donor membrane (ER) harboring
CC PstB2/PDR17 to acceptor membranes (Golgi/endosomes) harboring PSD2
CC during PtdSer transport to the site of PtdEtn synthesis
CC (PubMed:24366873). {ECO:0000250|UniProtKB:P0A8K1,
CC ECO:0000269|PubMed:20016005, ECO:0000269|PubMed:24366873,
CC ECO:0000305|PubMed:24366873}.
CC -!- INTERACTION:
CC P53037; P53844: PDR17; NbExp=3; IntAct=EBI-14018, EBI-2076838;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000255|HAMAP-
CC Rule:MF_03209, ECO:0000269|PubMed:7890739}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:11104779,
CC ECO:0000305|PubMed:20016005}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_03209, ECO:0000305|PubMed:24366873}. Endosome membrane
CC {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000269|PubMed:20016005};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03209,
CC ECO:0000305|PubMed:11104779, ECO:0000305|PubMed:20016005}; Cytoplasmic
CC side {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000305|PubMed:24366873}.
CC -!- DOMAIN: The C2 domains have an essential, but non-catalytic function
CC (Probable) (PubMed:24366873). Both C2-1 and C2-2 facilitate interaction
CC with PstB2/PDR17 and are required for lipid transport function
CC (PubMed:24366873). {ECO:0000269|PubMed:24366873,
CC ECO:0000305|PubMed:12093819}.
CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC the active enzyme involves a self-maturation process in which the
CC active site pyruvoyl group is generated from an internal serine residue
CC via an autocatalytic post-translational modification. Two non-identical
CC subunits are generated from the proenzyme in this reaction, and the
CC pyruvate is formed at the N-terminus of the alpha chain, which is
CC derived from the carboxyl end of the proenzyme. The autoendoproteolytic
CC cleavage occurs by a canonical serine protease mechanism, in which the
CC side chain hydroxyl group of the serine supplies its oxygen atom to
CC form the C-terminus of the beta chain, while the remainder of the
CC serine residue undergoes an oxidative deamination to produce ammonia
CC and the pyruvoyl prosthetic group on the alpha chain. During this
CC reaction, the Ser that is part of the protease active site of the
CC proenzyme becomes the pyruvoyl prosthetic group, which constitutes an
CC essential element of the active site of the mature decarboxylase.
CC {ECO:0000255|HAMAP-Rule:MF_03209}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Eukaryotic type II sub-subfamily.
CC {ECO:0000250|UniProtKB:B3L2V1, ECO:0000250|UniProtKB:P0A8K1,
CC ECO:0000255|HAMAP-Rule:MF_03209}.
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DR EMBL; U19910; AAA69819.1; -; Genomic_DNA.
DR EMBL; Z72955; CAA97196.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08265.1; -; Genomic_DNA.
DR PIR; S64484; S64484.
DR RefSeq; NP_011686.1; NM_001181299.1.
DR AlphaFoldDB; P53037; -.
DR SMR; P53037; -.
DR BioGRID; 33422; 191.
DR ComplexPortal; CPX-1319; PSTB lipid transfer acceptor membrane complex.
DR DIP; DIP-6756N; -.
DR IntAct; P53037; 3.
DR MINT; P53037; -.
DR STRING; 4932.YGR170W; -.
DR iPTMnet; P53037; -.
DR MaxQB; P53037; -.
DR PaxDb; P53037; -.
DR PRIDE; P53037; -.
DR EnsemblFungi; YGR170W_mRNA; YGR170W; YGR170W.
DR GeneID; 853080; -.
DR KEGG; sce:YGR170W; -.
DR SGD; S000003402; PSD2.
DR VEuPathDB; FungiDB:YGR170W; -.
DR eggNOG; KOG2419; Eukaryota.
DR GeneTree; ENSGT00390000013484; -.
DR HOGENOM; CLU_002661_1_0_1; -.
DR InParanoid; P53037; -.
DR OMA; KTSWRKH; -.
DR BioCyc; YEAST:YGR170W-MON; -.
DR UniPathway; UPA00558; UER00616.
DR PRO; PR:P53037; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53037; protein.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IDA:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IGI:SGD.
DR GO; GO:0120010; P:intermembrane phospholipid transfer; IC:ComplexPortal.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:SGD.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0016540; P:protein autoprocessing; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.150; -; 2.
DR HAMAP; MF_00663; PS_decarb_PSD_B_type2; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD.
DR InterPro; IPR033179; PSD_type2_pro.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
DR PROSITE; PS50004; C2; 2.
PE 1: Evidence at protein level;
KW Calcium; Decarboxylase; Endosome; Golgi apparatus; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Membrane; Metal-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Reference proteome; Repeat; Zymogen.
FT CHAIN 1..1138
FT /note="Phosphatidylserine decarboxylase proenzyme 2"
FT /id="PRO_0000045200"
FT CHAIN 1..1042
FT /note="Phosphatidylserine decarboxylase 2 beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT /id="PRO_0000045201"
FT CHAIN 1043..1138
FT /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT /id="PRO_0000045202"
FT DOMAIN 1..122
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 478..600
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 90..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..445
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 899
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:B3L2V1, ECO:0000255|HAMAP-
FT Rule:MF_03209"
FT ACT_SITE 956
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:B3L2V1, ECO:0000255|HAMAP-
FT Rule:MF_03209"
FT ACT_SITE 1043
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:B3L2V1, ECO:0000255|HAMAP-
FT Rule:MF_03209"
FT ACT_SITE 1043
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-
FT Rule:MF_03209"
FT BINDING 571
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 574
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 577
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT SITE 1042..1043
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-
FT Rule:MF_03209"
FT MOD_RES 1043
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-
FT Rule:MF_03209"
FT MUTAGEN 1041..1043
FT /note="GGS->AAA: No processing of the proenzyme, complete
FT loss of activity."
FT /evidence="ECO:0000269|PubMed:20016005"
FT CONFLICT 801
FT /note="E -> G (in Ref. 1; AAA69819)"
FT /evidence="ECO:0000305"
FT CONFLICT 974
FT /note="Y -> N (in Ref. 1; AAA69819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1138 AA; 130065 MW; 934BA6579E121053 CRC64;
MRIIKGRKRG KNKKPTLILK IHVIQAENIE ALKTFNCNPV CFVTTNTFYS QKTNKLKNSN
THWNQTLRIK LPRNPTSEWL RIIVYDALPT GAPPTTPSRP RTTTANTSSS TLSNSGLSSH
SHSSRNLNVT SKGNQTSTSI NSVSSSATPA PSHSSSSLST TGPGSTHKNR INSYLYLGEA
KISLLDLFKR KDTTTSYKFS IEAQRYHLYD MKGGKDQDSL NCNFLVGDIL LGFKLECNVK
RTPTFQAFNA WRNELNTYLG RIDRNKARMR SSSSLPPPLE DMLSNSSAVS GNEIRREKPY
SDTDLAHDEE VNAEDEIDAE ESIEDMNSSG SICTERRYDI DNDTIFDSIS EVVSLNDEEL
DILNDFEEAD HPNVPDINVH DIDEDTRISL SSMITALDEY DIVEPEDVAK LPAVSENDIT
SVDDEESENQ QESDEEFDIY NEDEREDSDF QSKEYIGSRL LHLQRGKHNK SYANYLYRRA
KSNFFISKKE HAMGVVFMHI GAIKNLPALR NRLSKTNYEM DPFIVISFGR RVFKTSWRKH
TLNPEFNEYA AFEVFPHETN FAFSIKVVDK DSFSFNDDVA KCELAWFDML QQQQHENEWI
PYEIPLDLTV EPAHAPKQPV LYSSFKYVSY PFLKKSFWKE AVDTSVNLER LDIIQVMLYL
ERLGSFTMAD SFELFQHFNK SAWAGQSITR SQLVEGLQSW RKSTNFKRIW TCPRCMRSCK
PTRNARRSKL VLENDLITHF AICTFSKEHK TLKPSYVSSA FASKRWFSKV LIKLTYGKYA
LGSNNANILV QDRDTGIIIE EKISAHVKLG MRIIYNGKSP ESKKFRSLLK TLSIRQGKKF
DSTASAKQIE PFIKFHSLDL SQCRDKDFKT FNEFFYRKLK PGSRLPESNN KEILFSPADS
RCTVFPTIQE SKEIWVKGRK FSIKKLANNY NPETFNDNNC SIGIFRLAPQ DYHRFHSPCN
GTIGKPVYVD GEYYTVNPMA VRSELDVFGE NIRVIIPIDS PQFGKLLYIP IGAMMVGSIL
LTCKENDVVE SGQELGYFKF GGSTIIIIIP HNNFMFDSDL VKNSSERIET LVKVGMSIGH
TSNVNELKRI RIKVDDPKKI ERIKRTISVS DENAKSTGNV TWEYHTLREM MNKDFAGL
