PTGR3_HUMAN
ID PTGR3_HUMAN Reviewed; 377 AA.
AC Q8N4Q0; A8KA15; B4DZ91;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Prostaglandin reductase 3;
DE Short=PRG-3;
DE EC=1.3.1.48 {ECO:0000250|UniProtKB:Q8BGC4};
DE AltName: Full=Zinc-binding alcohol dehydrogenase domain-containing protein 2;
GN Name=PTGR3 {ECO:0000312|HGNC:HGNC:28697}; Synonyms=ZADH2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 33-371 IN COMPLEX WITH NADP.
RA Bunkoczi G., Shafqat N., Guo K., Smee C., Arrowsmith C., Edwards A.,
RA Weigelt J., Sundstrom M., Gileadi O., Von Delft F., Oppermann U.;
RT "The structure of MGC45594 gene product.";
RL Submitted (SEP-2005) to the PDB data bank.
CC -!- FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on
CC 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha
CC with highest efficiency towards 15-keto-PGE2-alpha. Overexpression
CC represses transcriptional activity of PPARG and inhibits adipocyte
CC differentiation. {ECO:0000250|UniProtKB:Q8BGC4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin E2 + NADP(+) = 15-
CC oxoprostaglandin E2 + H(+) + NADPH; Xref=Rhea:RHEA:11912,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57402,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q8BGC4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin E1 + NADP(+) = 15-
CC oxoprostaglandin E1 + H(+) + NADPH; Xref=Rhea:RHEA:50584,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57401, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:133408;
CC Evidence={ECO:0000250|UniProtKB:Q8BGC4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-PGF2alpha + NADP(+) = 15-oxoprostaglandin
CC F2alpha + H(+) + NADPH; Xref=Rhea:RHEA:50588, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133374,
CC ChEBI:CHEBI:133409; Evidence={ECO:0000250|UniProtKB:Q8BGC4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13,14-dihydro-15-oxo-prostaglandin F1alpha + NADP(+) = 15-
CC oxoprostaglandin F1alpha + H(+) + NADPH; Xref=Rhea:RHEA:50592,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:79072, ChEBI:CHEBI:133411;
CC Evidence={ECO:0000250|UniProtKB:Q8BGC4};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q8BGC4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N4Q0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N4Q0-2; Sequence=VSP_055796;
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; AK292880; BAF85569.1; -; mRNA.
DR EMBL; AK302801; BAG64003.1; -; mRNA.
DR EMBL; AC025105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471117; EAW66569.1; -; Genomic_DNA.
DR EMBL; BC033780; AAH33780.1; -; mRNA.
DR EMBL; BC078661; AAH78661.1; -; mRNA.
DR CCDS; CCDS12008.1; -. [Q8N4Q0-1]
DR CCDS; CCDS77198.1; -. [Q8N4Q0-2]
DR RefSeq; NP_001293022.1; NM_001306093.1. [Q8N4Q0-2]
DR RefSeq; NP_787103.1; NM_175907.5. [Q8N4Q0-1]
DR PDB; 2C0C; X-ray; 1.45 A; A/B=33-371.
DR PDB; 2WEK; X-ray; 1.90 A; A/B=33-371.
DR PDB; 2X1H; X-ray; 1.75 A; A/B=33-371.
DR PDB; 2X7H; X-ray; 1.60 A; A/B=25-371.
DR PDBsum; 2C0C; -.
DR PDBsum; 2WEK; -.
DR PDBsum; 2X1H; -.
DR PDBsum; 2X7H; -.
DR AlphaFoldDB; Q8N4Q0; -.
DR SMR; Q8N4Q0; -.
DR BioGRID; 129813; 32.
DR IntAct; Q8N4Q0; 9.
DR STRING; 9606.ENSP00000323678; -.
DR iPTMnet; Q8N4Q0; -.
DR PhosphoSitePlus; Q8N4Q0; -.
DR BioMuta; ZADH2; -.
DR DMDM; 74728888; -.
DR EPD; Q8N4Q0; -.
DR jPOST; Q8N4Q0; -.
DR MassIVE; Q8N4Q0; -.
DR MaxQB; Q8N4Q0; -.
DR PaxDb; Q8N4Q0; -.
DR PeptideAtlas; Q8N4Q0; -.
DR PRIDE; Q8N4Q0; -.
DR ProteomicsDB; 5583; -.
DR ProteomicsDB; 71957; -. [Q8N4Q0-1]
DR Antibodypedia; 10355; 147 antibodies from 26 providers.
DR DNASU; 284273; -.
DR Ensembl; ENST00000322342.4; ENSP00000323678.3; ENSG00000180011.7. [Q8N4Q0-1]
DR Ensembl; ENST00000537114.2; ENSP00000440111.2; ENSG00000180011.7. [Q8N4Q0-2]
DR GeneID; 284273; -.
DR KEGG; hsa:284273; -.
DR MANE-Select; ENST00000322342.4; ENSP00000323678.3; NM_175907.6; NP_787103.1.
DR UCSC; uc002llx.4; human. [Q8N4Q0-1]
DR CTD; 284273; -.
DR DisGeNET; 284273; -.
DR GeneCards; ZADH2; -.
DR HGNC; HGNC:28697; PTGR3.
DR HPA; ENSG00000180011; Low tissue specificity.
DR neXtProt; NX_Q8N4Q0; -.
DR OpenTargets; ENSG00000180011; -.
DR VEuPathDB; HostDB:ENSG00000180011; -.
DR eggNOG; KOG1196; Eukaryota.
DR GeneTree; ENSGT00920000149172; -.
DR HOGENOM; CLU_026673_3_1_1; -.
DR InParanoid; Q8N4Q0; -.
DR OMA; VKPPFDI; -.
DR PhylomeDB; Q8N4Q0; -.
DR TreeFam; TF328691; -.
DR PathwayCommons; Q8N4Q0; -.
DR SignaLink; Q8N4Q0; -.
DR BioGRID-ORCS; 284273; 8 hits in 1079 CRISPR screens.
DR ChiTaRS; ZADH2; human.
DR EvolutionaryTrace; Q8N4Q0; -.
DR GenomeRNAi; 284273; -.
DR Pharos; Q8N4Q0; Tbio.
DR PRO; PR:Q8N4Q0; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q8N4Q0; protein.
DR Bgee; ENSG00000180011; Expressed in left ventricle myocardium and 182 other tissues.
DR ExpressionAtlas; Q8N4Q0; baseline and differential.
DR Genevisible; Q8N4Q0; HS.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0036132; F:13-prostaglandin reductase activity; ISS:UniProtKB.
DR GO; GO:0047522; F:15-oxoprostaglandin 13-oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Lipid metabolism; NADP;
KW Oxidoreductase; Peroxisome; Phosphoprotein; Reference proteome.
FT CHAIN 1..377
FT /note="Prostaglandin reductase 3"
FT /id="PRO_0000223467"
FT BINDING 185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 205
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 209
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 224
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 247
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 303..305
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 361
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGC4"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055796"
FT VARIANT 323
FT /note="C -> F (in dbSNP:rs17056661)"
FT /id="VAR_048202"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:2C0C"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:2C0C"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:2C0C"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 186..195
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:2C0C"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 229..236
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 289..296
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:2C0C"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:2X1H"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:2C0C"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:2C0C"
SQ SEQUENCE 377 AA; 40140 MW; 9CDC927D815314D1 CRC64;
MLRLVPTGAR AIVDMSYARH FLDFQGSAIP QAMQKLVVTR LSPNFREAVT LSRDCPVPLP
GDGDLLVRNR FVGVNASDIN YSAGRYDPSV KPPFDIGFEG IGEVVALGLS ASARYTVGQA
VAYMAPGSFA EYTVVPASIA TPVPSVKPEY LTLLVSGTTA YISLKELGGL SEGKKVLVTA
AAGGTGQFAM QLSKKAKCHV IGTCSSDEKS AFLKSLGCDR PINYKTEPVG TVLKQEYPEG
VDVVYESVGG AMFDLAVDAL ATKGRLIVIG FISGYQTPTG LSPVKAGTLP AKLLKKSASV
QGFFLNHYLS KYQAAMSHLL EMCVSGDLVC EVDLGDLSPE GRFTGLESIF RAVNYMYMGK
NTGKIVVELP HSVNSKL
