C90C1_ARATH
ID C90C1_ARATH Reviewed; 524 AA.
AC Q9M066; O23242; Q058J8; Q0WS16;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=3-epi-6-deoxocathasterone 23-monooxygenase CYP90C1 {ECO:0000305};
DE Short=3-dehydro-6-deoxoteasterone {ECO:0000303|PubMed:17138693};
DE EC=1.14.14.147 {ECO:0000269|PubMed:17138693};
DE AltName: Full=(22R,23R)-22,23-dihydroxy-campest-4-en-3-one synthase {ECO:0000303|PubMed:17138693};
DE EC=1.14.14.- {ECO:0000269|PubMed:17138693};
DE AltName: Full=(22R,23R)-22,23-dihydroxycampesterol synthase {ECO:0000303|PubMed:17138693};
DE EC=1.14.14.- {ECO:0000269|PubMed:17138693};
DE AltName: Full=6-deoxoteasterone synthase {ECO:0000303|PubMed:17138693};
DE EC=1.14.14.- {ECO:0000269|PubMed:17138693};
DE AltName: Full=Cytochrome P450 90C1 {ECO:0000303|PubMed:9694802};
DE AltName: Full=Protein ROTUNDIFOLIA 3 {ECO:0000303|PubMed:9694802};
DE AltName: Full=Teasterone synthase {ECO:0000303|PubMed:17138693};
DE EC=1.14.14.- {ECO:0000269|PubMed:17138693};
GN Name=CYP90C1 {ECO:0000303|PubMed:9694802};
GN Synonyms=ROT3 {ECO:0000303|PubMed:9694802};
GN OrderedLocusNames=At4g36380 {ECO:0000312|Araport:AT4G36380};
GN ORFNames=AP22.10 {ECO:0000305}, C7A10.980 {ECO:0000312|EMBL:CAB16850.1},
GN F23E13.220 {ECO:0000312|EMBL:CAA18139.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=9694802; DOI=10.1101/gad.12.15.2381;
RA Kim G.-T., Tsukaya H., Uchimiya H.;
RT "The ROTUNDIFOLIA3 gene of Arabidopsis thaliana encodes a new member of the
RT cytochrome P-450 family that is required for the regulated polar elongation
RT of leaf cells.";
RL Genes Dev. 12:2381-2391(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=10430960; DOI=10.1073/pnas.96.16.9433;
RA Kim G.T., Tsukaya H., Saito Y., Uchimiya H.;
RT "Changes in the shapes of leaves and flowers upon overexpression of
RT cytochrome P450 in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9433-9437(1999).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15703058; DOI=10.1111/j.1365-313x.2004.02330.x;
RA Kim G.T., Fujioka S., Kozuka T., Tax F.E., Takatsuto S., Yoshida S.,
RA Tsukaya H.;
RT "CYP90C1 and CYP90D1 are involved in different steps in the brassinosteroid
RT biosynthesis pathway in Arabidopsis thaliana.";
RL Plant J. 41:710-721(2005).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17138693; DOI=10.1105/tpc.106.045443;
RA Ohnishi T., Szatmari A.M., Watanabe B., Fujita S., Bancos S., Koncz C.,
RA Lafos M., Shibata K., Yokota T., Sakata K., Szekeres M., Mizutani M.;
RT "C-23 hydroxylation by Arabidopsis CYP90C1 and CYP90D1 reveals a novel
RT shortcut in brassinosteroid biosynthesis.";
RL Plant Cell 18:3275-3288(2006).
CC -!- FUNCTION: Involved in brassinosteroid (BR) biosynthesis
CC (PubMed:15703058, PubMed:17138693). Converts typhasterol (TY) to
CC cathasterone (CS) and 6-deoxotyphasterol (6-deoxoTY) to 6-
CC deoxocathasterone (6-deoxoCT) (PubMed:15703058). C-23 hydroxylase that
CC converts directly (22S,24R)-22-hydroxy-5-alpha-ergostan-3-one and 3-
CC epi-6-deoxocathasterone to 3-dehydro-6-deoxoteasterone (6-deoxo3DT, 6-
CC deoxo3DHT) and 6-deoxotyphasterol (6-deoxoTY), respectively
CC (PubMed:17138693). These C-23 hydroxylation shortcuts bypass
CC campestanol, 6-deoxocathasterone, and 6-deoxoteasterone (6-deoxoTE)
CC (PubMed:17138693). Catalyzes also the conversion of cathasterone to
CC teasterone (TE), (22S,24R)-22-hydroxyergost-4-en-3-one (22-OH-4-en-3-
CC one) to (22R,23R)-22,23-dihydroxy-campest-4-en-3-one (22,23-diOH-4-en-
CC 3-one) and (22S)-22-hydroxycampesterol (22-OHCR) to (22R,23R)-22,23-
CC dihydroxycampesterol (22,23-diOHCR) (PubMed:17138693). Required for the
CC regulation of polar elongation of leaf cells (PubMed:9694802,
CC PubMed:10430960). Required for the longitudinal elongation of floral
CC organs (PubMed:10430960). {ECO:0000269|PubMed:10430960,
CC ECO:0000269|PubMed:15703058, ECO:0000269|PubMed:17138693,
CC ECO:0000269|PubMed:9694802}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-epi-6-deoxocathasterone + O2 + reduced [NADPH--hemoprotein
CC reductase] = 6-deoxotyphasterol + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:27321, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:20717, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:59410; EC=1.14.14.147;
CC Evidence={ECO:0000269|PubMed:17138693};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(22S,24R)-22-hydroxy-5alpha-ergostan-3-one + O2 + reduced
CC [NADPH--hemoprotein reductase] = 3-dehydro-6-deoxoteasterone + H(+) +
CC H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:27325,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:20710,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:59411;
CC EC=1.14.14.147; Evidence={ECO:0000269|PubMed:17138693};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.4 uM for (22S)-22-hydroxycampesterol
CC {ECO:0000269|PubMed:17138693};
CC KM=8.61 uM for (22S,24R)-22-hydroxy-5-alpha-ergostan-3-one
CC {ECO:0000269|PubMed:17138693};
CC KM=4.94 uM for (22S,24R)-22-hydroxyergost-4-en-3-one
CC {ECO:0000269|PubMed:17138693};
CC KM=6.61 uM for 3-epi-6-deoxocathasterone
CC {ECO:0000269|PubMed:17138693};
CC KM=35.9 uM for 6-deoxocathasterone {ECO:0000269|PubMed:17138693};
CC Note=kcat is 0.11 min(-1) for (22S)-22-hydroxycampesterol
CC (PubMed:17138693). kcat is 2.75 min(-1) for (22S,24R)-22-hydroxy-5-
CC alpha-ergostan-3-one (PubMed:17138693). kcat is 1.40 min(-1) for
CC (22S,24R)-22-hydroxyergost-4-en-3-one (PubMed:17138693). kcat is 3.01
CC min(-1) for 3-epi-6-deoxocathasterone (PubMed:17138693). kcat is 0.14
CC min(-1) for 6-deoxocathasterone (PubMed:17138693).
CC {ECO:0000269|PubMed:17138693};
CC -!- PATHWAY: Plant hormone biosynthesis; brassinosteroid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15703058,
CC ECO:0000269|PubMed:9694802}.
CC -!- DISRUPTION PHENOTYPE: Plants with short petioles and round leaves.
CC Altered polar elongation of leaf cells (PubMed:9694802). The double
CC mutant plants cyp90c1 and cyp90d1 exhibit a characteristic
CC brassinosteroid-deficient dwarf phenotype (PubMed:15703058).
CC {ECO:0000269|PubMed:15703058, ECO:0000269|PubMed:9694802}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18139.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB16850.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB80304.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB008097; BAA37167.1; -; mRNA.
DR EMBL; Z99708; CAB16850.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL022141; CAA18139.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161589; CAB80304.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE86649.1; -; Genomic_DNA.
DR EMBL; AK228126; BAF00083.1; -; mRNA.
DR EMBL; BT029220; ABJ17155.1; -; mRNA.
DR PIR; D85429; D85429.
DR PIR; T04602; T04602.
DR RefSeq; NP_568002.1; NM_119801.4.
DR AlphaFoldDB; Q9M066; -.
DR SMR; Q9M066; -.
DR STRING; 3702.AT4G36380.1; -.
DR PaxDb; Q9M066; -.
DR PRIDE; Q9M066; -.
DR ProteomicsDB; 239144; -.
DR EnsemblPlants; AT4G36380.1; AT4G36380.1; AT4G36380.
DR GeneID; 829790; -.
DR Gramene; AT4G36380.1; AT4G36380.1; AT4G36380.
DR KEGG; ath:AT4G36380; -.
DR Araport; AT4G36380; -.
DR TAIR; locus:2115220; AT4G36380.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_5_1; -.
DR InParanoid; Q9M066; -.
DR OMA; DVFIPCY; -.
DR OrthoDB; 574756at2759; -.
DR PhylomeDB; Q9M066; -.
DR BioCyc; ARA:AT4G36380-MON; -.
DR BioCyc; MetaCyc:AT4G36380-MON; -.
DR BRENDA; 1.14.14.147; 399.
DR UniPathway; UPA00381; -.
DR PRO; PR:Q9M066; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M066; baseline and differential.
DR Genevisible; Q9M066; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102097; F:(22S)-22-hydroxy-5alpha-campestan-3-one C-23 hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0102136; F:3-epi-6-deoxocathasterone C-23 hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:TAIR.
DR GO; GO:0016132; P:brassinosteroid biosynthetic process; IMP:TAIR.
DR GO; GO:0010268; P:brassinosteroid homeostasis; IEP:TAIR.
DR GO; GO:0048366; P:leaf development; IGI:TAIR.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0042814; P:monopolar cell growth; IMP:TAIR.
DR GO; GO:0048441; P:petal development; IGI:TAIR.
DR GO; GO:0048443; P:stamen development; IGI:TAIR.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Brassinosteroid biosynthesis; Endoplasmic reticulum; Heme; Iron;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Steroid biosynthesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..524
FT /note="3-epi-6-deoxocathasterone 23-monooxygenase CYP90C1"
FT /id="PRO_0000052186"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 463
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q96242"
FT CONFLICT 45
FT /note="L -> F (in Ref. 1; BAA37167)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="F -> S (in Ref. 5; BAF00083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 59356 MW; CB9C910E12346CE8 CRC64;
MQPPASAGLF RSPENLPWPY NYMDYLVAGF LVLTAGILLR PWLWLRLRNS KTKDGDEEED
NEEKKKGMIP NGSLGWPVIG ETLNFIACGY SSRPVTFMDK RKSLYGKVFK TNIIGTPIII
STDAEVNKVV LQNHGNTFVP AYPKSITELL GENSILSING PHQKRLHTLI GAFLRSPHLK
DRITRDIEAS VVLTLASWAQ LPLVHVQDEI KKMTFEILVK VLMSTSPGED MNILKLEFEE
FIKGLICIPI KFPGTRLYKS LKAKERLIKM VKKVVEERQV AMTTTSPAND VVDVLLRDGG
DSEKQSQPSD FVSGKIVEMM IPGEETMPTA MTLAVKFLSD NPVALAKLVE ENMEMKRRKL
ELGEEYKWTD YMSLSFTQNV INETLRMANI INGVWRKALK DVEIKGYLIP KGWCVLASFI
SVHMDEDIYD NPYQFDPWRW DRINGSANSS ICFTPFGGGQ RLCPGLELSK LEISIFLHHL
VTRYSWTAEE DEIVSFPTVK MKRRLPIRVA TVDDSASPIS LEDH
