AOX4_ARATH
ID AOX4_ARATH Reviewed; 351 AA.
AC Q56X52; O49631; Q9SBA4; Q9ZSQ3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ubiquinol oxidase 4, chloroplastic/chromoplastic;
DE EC=1.10.3.11;
DE AltName: Full=Alternative oxidase 4;
DE AltName: Full=Plastid terminal oxidase;
DE AltName: Full=Protein IMMUTANS;
DE Flags: Precursor;
GN Name=AOX4; Synonyms=IM, PTOX; OrderedLocusNames=At4g22260;
GN ORFNames=T10I14_90;
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], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9878631; DOI=10.2307/3870837;
RA Wu D., Wright D.A., Wetzel C., Voytas D.F., Rodermel S.R.;
RT "The IMMUTANS variegation locus of Arabidopsis defines a mitochondrial
RT alternative oxidase homolog that functions during early chloroplast
RT biogenesis.";
RL Plant Cell 11:43-55(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=9878632; DOI=10.2307/3870838;
RA Carol P., Stevenson D., Bisanz C., Breitenbach J., Sandmann G., Mache R.,
RA Coupland G., Kuntz M.;
RT "Mutations in the Arabidopsis gene IMMUTANS cause a variegated phenotype by
RT inactivating a chloroplast terminal oxidase associated with phytoene
RT desaturation.";
RL Plant Cell 11:57-68(1999).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-351.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7920709; DOI=10.1046/j.1365-313x.1994.6020161.x;
RA Wetzel C.M., Jiang C.Z., Meehan L.J., Voytas D.F., Rodermel S.R.;
RT "Nuclear-organelle interactions: the immutans variegation mutant of
RT Arabidopsis is plastid autonomous and impaired in carotenoid
RT biosynthesis.";
RL Plant J. 6:161-175(1994).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10938359; DOI=10.1104/pp.123.4.1427;
RA Josse E.-M., Simkin A.J., Gaffe J., Laboure A.-M., Kuntz M., Carol P.;
RT "A plastid terminal oxidase associated with carotenoid desaturation during
RT chromoplast differentiation.";
RL Plant Physiol. 123:1427-1436(2000).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11553735; DOI=10.1104/pp.127.1.67;
RA Aluru M.R., Bae H., Wu D., Rodermel S.R.;
RT "The Arabidopsis immutans mutation affects plastid differentiation and the
RT morphogenesis of white and green sectors in variegated plants.";
RL Plant Physiol. 127:67-77(2001).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Col-1;
RX PubMed=14504923; DOI=10.1007/s00425-003-1111-7;
RA Lennon A.M., Prommeenate P., Nixon P.J.;
RT "Location, expression and orientation of the putative chlororespiratory
RT enzymes, Ndh and IMMUTANS, in higher-plant plastids.";
RL Planta 218:254-260(2003).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15032871; DOI=10.1111/j.0031-9317.2004.0217.x;
RA Aluru M.R., Rodermel S.R.;
RT "Control of chloroplast redox by the IMMUTANS terminal oxidase.";
RL Physiol. Plantarum 120:4-11(2004).
RN [12]
RP FUNCTION, IRON-BINDING SITES, AND MUTAGENESIS OF GLU-136; GLU-175; HIS-178;
RP GLU-227; GLU-296 AND HIS-299.
RX PubMed=16249174; DOI=10.1074/jbc.m508940200;
RA Fu A., Park S., Rodermel S.;
RT "Sequences required for the activity of PTOX (IMMUTANS), a plastid terminal
RT oxidase: in vitro and in planta mutagenesis of iron-binding sites and a
RT conserved sequence that corresponds to Exon 8.";
RL J. Biol. Chem. 280:42489-42496(2005).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-136; GLU-175; HIS-177;
RP HIS-178; GLU-224; GLU-227; GLU-296; GLU-298 AND HIS-299.
RX PubMed=16449381; DOI=10.1093/jxb/erj008;
RA Aluru M.R., Yu F., Fu A., Rodermel S.;
RT "Arabidopsis variegation mutants: new insights into chloroplast
RT biogenesis.";
RL J. Exp. Bot. 57:1871-1881(2006).
RN [14]
RP FUNCTION.
RX PubMed=19386811; DOI=10.1104/pp.109.135780;
RA Aluru M.R., Zola J., Foudree A., Rodermel S.R.;
RT "Chloroplast photooxidation-induced transcriptome reprogramming in
RT Arabidopsis immutans white leaf sectors.";
RL Plant Physiol. 150:904-923(2009).
CC -!- FUNCTION: Acts early in chloroplast biogenesis as a component of a
CC redox chain responsible for phytoene desaturation. Prevents the
CC generation of toxic oxygen radicals and photooxidation of the nascent
CC photosynthetic apparatus. Involved in the differentiation of multiple
CC plastid types, including chloroplasts, amyloplasts, and etioplasts.
CC Might participate in the chloroplast respiratory chain.
CC {ECO:0000269|PubMed:10938359, ECO:0000269|PubMed:11553735,
CC ECO:0000269|PubMed:14504923, ECO:0000269|PubMed:15032871,
CC ECO:0000269|PubMed:16249174, ECO:0000269|PubMed:16449381,
CC ECO:0000269|PubMed:19386811, ECO:0000269|PubMed:7920709,
CC ECO:0000269|PubMed:9878631, ECO:0000269|PubMed:9878632}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O;
CC Xref=Rhea:RHEA:30255, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976; EC=1.10.3.11;
CC Evidence={ECO:0000269|PubMed:15032871, ECO:0000269|PubMed:16449381};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:Q39219};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250|UniProtKB:Q39219};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:14504923, ECO:0000269|PubMed:9878632}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14504923,
CC ECO:0000269|PubMed:9878632}; Stromal side {ECO:0000269|PubMed:9878632}.
CC Plastid, chromoplast membrane {ECO:0000269|PubMed:10938359}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10938359}. Note=localized to the
CC stromal thylakoid lamellae. {ECO:0000269|PubMed:14504923}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11553735}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the development of the
CC leaves. {ECO:0000269|PubMed:14504923}.
CC -!- DISRUPTION PHENOTYPE: Variegated cotyledons and leaves. The amount of
CC white tissue increases with light intensity.
CC {ECO:0000269|PubMed:7920709}.
CC -!- SIMILARITY: Belongs to the alternative oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94037.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA16776.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79181.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF098072; AAD03599.1; -; mRNA.
DR EMBL; AJ004881; CAA06190.1; -; mRNA.
DR EMBL; AL021712; CAA16776.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161557; CAB79181.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84583.1; -; Genomic_DNA.
DR EMBL; AF324663; AAG40014.1; -; mRNA.
DR EMBL; AF326898; AAG41480.1; -; mRNA.
DR EMBL; AF339717; AAK00399.1; -; mRNA.
DR EMBL; AY045699; AAK74057.1; -; mRNA.
DR EMBL; BT000558; AAN18127.1; -; mRNA.
DR EMBL; AK221825; BAD94037.1; ALT_INIT; mRNA.
DR PIR; T04907; T04907.
DR PIR; T52422; T52422.
DR RefSeq; NP_567658.1; NM_118352.4.
DR AlphaFoldDB; Q56X52; -.
DR SMR; Q56X52; -.
DR STRING; 3702.AT4G22260.1; -.
DR PaxDb; Q56X52; -.
DR PRIDE; Q56X52; -.
DR ProteomicsDB; 244472; -.
DR EnsemblPlants; AT4G22260.1; AT4G22260.1; AT4G22260.
DR GeneID; 828321; -.
DR Gramene; AT4G22260.1; AT4G22260.1; AT4G22260.
DR KEGG; ath:AT4G22260; -.
DR Araport; AT4G22260; -.
DR TAIR; locus:2005514; AT4G22260.
DR eggNOG; ENOG502QRMM; Eukaryota.
DR HOGENOM; CLU_057018_0_0_1; -.
DR InParanoid; Q56X52; -.
DR OMA; YIISPRM; -.
DR OrthoDB; 884390at2759; -.
DR PhylomeDB; Q56X52; -.
DR PRO; PR:Q56X52; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q56X52; baseline and differential.
DR Genevisible; Q56X52; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046862; C:chromoplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; IDA:TAIR.
DR GO; GO:0009916; F:alternative oxidase activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106292; F:superoxide-generating NADPH oxidase activity; IDA:TAIR.
DR GO; GO:0102721; F:ubiquinol:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0010230; P:alternative respiration; IBA:GO_Central.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IMP:TAIR.
DR GO; GO:0009657; P:plastid organization; IMP:TAIR.
DR CDD; cd01053; AOX; 1.
DR Gene3D; 1.20.1260.140; -; 1.
DR InterPro; IPR002680; AOX.
DR InterPro; IPR038659; AOX_sf.
DR PANTHER; PTHR31803; PTHR31803; 1.
DR Pfam; PF01786; AOX; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Chloroplast; Chromoplast; Electron transport;
KW Iron; Membrane; Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW Respiratory chain; Thylakoid; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..56
FT /note="Chloroplast and chromoplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..351
FT /note="Ubiquinol oxidase 4, chloroplastic/chromoplastic"
FT /id="PRO_0000045423"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 71..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 175
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 178
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT BINDING 299
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q26710"
FT MUTAGEN 136
FT /note="E->A,D,H: Abolishes cyanide-resistant oxygen
FT consumption."
FT /evidence="ECO:0000269|PubMed:16249174,
FT ECO:0000269|PubMed:16449381"
FT MUTAGEN 175
FT /note="E->A,D,H: Abolishes cyanide-resistant oxygen
FT consumption."
FT /evidence="ECO:0000269|PubMed:16249174,
FT ECO:0000269|PubMed:16449381"
FT MUTAGEN 177
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:16449381"
FT MUTAGEN 178
FT /note="H->A,E,N: Abolishes cyanide-resistant oxygen
FT consumption."
FT /evidence="ECO:0000269|PubMed:16249174,
FT ECO:0000269|PubMed:16449381"
FT MUTAGEN 224
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:16449381"
FT MUTAGEN 227
FT /note="E->A,D,H: Abolishes cyanide-resistant oxygen
FT consumption."
FT /evidence="ECO:0000269|PubMed:16249174,
FT ECO:0000269|PubMed:16449381"
FT MUTAGEN 296
FT /note="E->A,D,H: Abolishes cyanide-resistant oxygen
FT consumption."
FT /evidence="ECO:0000269|PubMed:16249174,
FT ECO:0000269|PubMed:16449381"
FT MUTAGEN 298
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:16449381"
FT MUTAGEN 299
FT /note="H->A,E,N: Abolishes cyanide-resistant oxygen
FT consumption."
FT /evidence="ECO:0000269|PubMed:16249174,
FT ECO:0000269|PubMed:16449381"
FT CONFLICT 320
FT /note="E -> D (in Ref. 2; CAA06190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 40574 MW; D8A38C9A4EC0EF69 CRC64;
MAAISGISSG TLTISRPLVT LRRSRAAVSY SSSHRLLHHL PLSSRRLLLR NNHRVQATIL
QDDEEKVVVE ESFKAETSTG TEPLEEPNMS SSSTSAFETW IIKLEQGVNV FLTDSVIKIL
DTLYRDRTYA RFFVLETIAR VPYFAFMSVL HMYETFGWWR RADYLKVHFA ESWNEMHHLL
IMEELGGNSW WFDRFLAQHI ATFYYFMTVF LYILSPRMAY HFSECVESHA YETYDKFLKA
SGEELKNMPA PDIAVKYYTG GDLYLFDEFQ TSRTPNTRRP VIENLYDVFV NIRDDEAEHC
KTMRACQTLG SLRSPHSILE DDDTEEESGC VVPEEAHCEG IVDCLKKSIT S
