R213B_DANRE
ID R213B_DANRE Reviewed; 5061 AA.
AC A0A0R4I9Y1;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=E3 ubiquitin-protein ligase rnf213-beta {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q63HN8};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:Q63HN8};
DE AltName: Full=E3 ubiquitin-lipopolysaccharide ligase rnf213-beta {ECO:0000305};
DE EC=2.3.2.- {ECO:0000250|UniProtKB:Q63HN8};
DE AltName: Full=Mysterin-B;
DE AltName: Full=Mysterin-beta {ECO:0000303|PubMed:26530008};
DE AltName: Full=RING finger protein 213-B {ECO:0000305};
DE AltName: Full=RING finger protein 213-beta {ECO:0000303|PubMed:21799892};
GN Name=rnf213b;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=21799892; DOI=10.1371/journal.pone.0022542;
RA Liu W., Morito D., Takashima S., Mineharu Y., Kobayashi H., Hitomi T.,
RA Hashikata H., Matsuura N., Yamazaki S., Toyoda A., Kikuta K., Takagi Y.,
RA Harada K.H., Fujiyama A., Herzig R., Krischek B., Zou L., Kim J.E.,
RA Kitakaze M., Miyamoto S., Nagata K., Hashimoto N., Koizumi A.;
RT "Identification of RNF213 as a susceptibility gene for moyamoya disease and
RT its possible role in vascular development.";
RL PLoS ONE 6:E22542-E22542(2011).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=26530008; DOI=10.1038/srep16161;
RA Kotani Y., Morito D., Yamazaki S., Ogino K., Kawakami K., Takashima S.,
RA Hirata H., Nagata K.;
RT "Neuromuscular regulation in zebrafish by a large AAA+ ATPase/ubiquitin
RT ligase, mysterin/RNF213.";
RL Sci. Rep. 5:16161-16161(2015).
CC -!- FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination
CC of both proteins and lipids, and which is involved in various
CC processes, such as lipid metabolism, angiogenesis and cell-autonomous
CC immunity. Acts as a key immune sensor by catalyzing ubiquitination of
CC the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-
CC type zinc-finger: restricts the proliferation of cytosolic bacteria,
CC such as Salmonella, by generating the bacterial ubiquitin coat through
CC the ubiquitination of LPS. Ubiquitination of LPS triggers cell-
CC autonomous immunity, such as antibacterial autophagy, leading to
CC degradation of the microbial invader (By similarity). Involved in lipid
CC metabolism by regulating fat storage and lipid droplet formation; act
CC by inhibiting the lipolytic process (By similarity). Also regulates
CC lipotoxicity by inhibiting desaturation of fatty acids. Also acts as an
CC E3 ubiquitin-protein ligase via its RING-type zinc finger. Involved in
CC the non-canonical Wnt signaling pathway in vascular development: acts
CC by mediating ubiquitination and degradation of proteins downstream of
CC rspo3, leading to inhibit the non-canonical Wnt signaling pathway and
CC promoting vessel regression. Also has ATPase activity; ATPase activity
CC is required for ubiquitination of LPS (By similarity).
CC {ECO:0000250|UniProtKB:A0A0R4IBK5, ECO:0000250|UniProtKB:Q63HN8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q63HN8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q63HN8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q63HN8};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q63HN8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q63HN8}.
CC -!- DOMAIN: Composed of an N-terminal stalk, a dynein-like core comprised
CC of two catalytically active and four inactive ATPase domains, and a C-
CC terminal E3 module. The ATPase regions do not generate movement but
CC rather act like an intricate molecular 'switch'.
CC {ECO:0000250|UniProtKB:E9Q555}.
CC -!- DOMAIN: The RING-type zinc finger domain is required for the ubiquitin-
CC protein ligase activity. {ECO:0000250|UniProtKB:Q63HN8}.
CC -!- DOMAIN: The RZ-type (RNF213-ZNFX1) zinc-finger is required for the
CC ubiquitination of the lipid A moiety of bacterial lipopolysaccharide
CC (LPS). {ECO:0000250|UniProtKB:Q63HN8}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:21799892,
CC PubMed:26530008). No vascular phenotype (PubMed:21799892,
CC PubMed:26530008). {ECO:0000269|PubMed:21799892,
CC ECO:0000269|PubMed:26530008}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; CU459056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; A0A0R4I9Y1; -.
DR STRING; 7955.ENSDARP00000127221; -.
DR PaxDb; A0A0R4I9Y1; -.
DR ZFIN; ZDB-GENE-110822-1; rnf213b.
DR eggNOG; ENOG502QQ65; Eukaryota.
DR OMA; DCENSIF; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:A0A0R4I9Y1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
DR GO; GO:0120323; P:lipid ubiquitination; ISS:UniProtKB.
DR GO; GO:2000051; P:negative regulation of non-canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0002040; P:sprouting angiogenesis; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0098792; P:xenophagy; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031248; RNF213.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR22605; PTHR22605; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51981; ZF_RZ; 1.
PE 3: Inferred from homology;
KW Angiogenesis; ATP-binding; Cytoplasm; Hydrolase; Immunity; Lipid droplet;
KW Lipid metabolism; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..5061
FT /note="E3 ubiquitin-protein ligase rnf213-beta"
FT /id="PRO_0000435805"
FT ZN_FING 3957..3997
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 4429..4501
FT /note="RZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT REGION 1..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4462
FT /note="Nucleophile; for E3 ubiquitin-lipopolysaccharide
FT ligase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 1923..1928
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 2023
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 2074
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 2417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 2492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 3957
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 3960
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 3972
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 3974
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 3977
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 3980
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 3993
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 3996
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:E9Q555"
FT BINDING 4451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 4455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 4471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
FT BINDING 4474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325"
SQ SEQUENCE 5061 AA; 577550 MW; 11C60D242B171DE7 CRC64;
MTRKRKSGKK GKPLAQKKEA QKRGGSTSSS TTQKEGAQKG DGSSSSSTTQ KDGAQKRDDS
TSSSSTAQKE EGQKSDGSTS SSTTNKEGAQ KRDGSTSSRL QKKGPQKRKG STSSSRAHSR
SRSKSKQTSY PSQARSRSHG QHNISTTESG PLSKEAQTQT SASLLVDKDT QTETVGQASQ
QTQTEINGNT ETAEVSQPPQ LSHEDVEMEG TVQPRTKGSE SDGEKEESVK RKKRKLSEIG
EPAKETEDST KLSHECEEKV GDNQKNEDTN KHYGGDSLKD LKSVTEEPKS YAAAAATGKT
GKVSKEQTNQ IEANQDSTME SKSTQRKPSP VRAPAGPPML TFYIYAVLDK RFRFNEQYDS
LFLDYGNGNI KLQMKHFNIG KDGYLIEATF SVEDSAVRGG TIQYKYVVQQ RQNQKSEIAV
RYIEVPSYTT EKEFHLYEGY ISCSSTVSIT EWMMSLFHSE QKAVYKGWET SAHVLLDRIF
LKWHPSNEES NMTFVQHLRS YKNAFESGFV EFPGNYTPFP IKVSELISAK LRMILKKESE
ALRTSESLDG VKSEALSVAL SVFKVCCGCD VDLSLKDWGK LCQVVSECMG SFGEIQTTQT
APFINTVTGL MNLCAKKLIT EVVLLVPVLH LLRNSEVNEA GPGSSMDEQR WTGLENISYQ
SFRERIRGLP DKRRMILKLI KDNLPMTKDN PKLLKSWLSL VAFEDVSEFV QLTGSFPELL
IQSLMCRIIE AEKNTDANRT EKNLEVTGKV LNLLLKSIKK DRERIMKTEQ LKLILQCCCN
VHKSVCKTAR LVPQYKVTVL SFQLLLKMAE IVYDGFFKGG EQMKQHQNEV LSKLNIIQED
FRKWRVELLL KPLMQTTGFT YPREMELWND LYGIESSIPG VTERWKGFLD HDLRRRISQI
SDTDKIVVYV LVTSAKAVEN SHANIQSCLK ELCEAAIKNQ CQSKKEGTLL CHLFSKTISW
PVLSSIIVES AACFGEDHKG RLLDPQSAIN FFLSQDKWNE WKLEDGASQL IAESQSFLGR
LIQTLCQGSI PLGHLKTIFK YKTQFQKLYN QYKNNNKEMN VSISVSDLLS QREDDLKAFE
QQKGYMTNLI NMLGKISDVI NVPELSSLEE IAKTNVQEVA LDKLVEVETY FSKDDLKKNN
TRRVLFYSDD QQVQDMAREM HDVNSSNLIL SFWQEKAKDY FMAGPELLSL DLTEIYEDIW
TPCLTKFLNF GNRIAVGQAC FKEVEEALVG CGETGEGDRL KKEFMLMATM LDGHNENWPE
QRLKQIREYR CLYDAAESAE VILKLKDRLG LQGDFSHIHS LTLVRDDSFK QNTLGSLSED
LIKARQKLAD VERRHTACLE AFLKSDTLIK WIKAEIPSLK ELKVFMELAT ISAGENDADI
DRLASFETAV MGYAPLLYSL PQNVGFEEFF DYAKQVLDTL NKDEKLGDKL VDSNRWLDWL
KGLRETHGSV EQSSLSLASA INTGGVYHVG WPDDFNGKTG LDNIFYVKVT KNNEEKTYRL
NELLELQNKL MLMSSKGEKG KEQVIKFTQV FEGIQRMGRI LLQLHRSGNM LFRNWAAEIT
CNHQNQPCIQ VKFPLLSKCI VYQGEVEEEL QKLSRSLEDF HKDWCNHLTK MRSQYYPLNH
YSSEQIVYLC EWINSINIKK KPVPQQVWHL LTPIKPDCML NDIKEAFEIA TEPQSILQED
TAEELGPNSD FDLPLSFSLL DVSTECLEDL WKQFKENMSG FLTHHVDVET LGRFLSNLSN
MNQLHIKRKI PSFLQEGRPN LVQCPAAELM STTLSFYMES PENPLPTTDE VLMCQEETTE
EEVEIFLRRC LGGAASNHKK IYTLVNPGSM SYDVSVALVE YFETQEVCAG PYYRLVMVCP
VNQDRYIPSF FSNYKVQTGI TISAERSQKY IRHHFKISYE LATHSSVYPE RLSVWMIASK
RPAVGKSLYV RRLFEKFKGE FPRATLLTIR LIDPYIDMDG FVQTLSERLA PLRQQDPVLL
HIDVAAVCHG LEEFLFKLLI LECISDSKGT IWRRNKAHLV VIETLQRGHK TQTKMEPSHG
FLNTLPTIFC RPPKDIKEIM KTNESFRSLD PLMDKEEFES EDIQRPYQYL RRFNRSMNLD
RFTYQAHSVE GDPVDCLHHL LSNYGLKDPS WAELKHFTWF LNLQLKDCEK SLFCDSDFCG
ETLSGFKDFI VKFMIHMARD FASPSIDISD QSPSFFSKNE DEEEILSFRK RWENESHPYI
FFNADHVSMS FLGFHVKQNG TILNAVDSKS GKVLMRNVMT QELFSDIQRQ MINLSKDFDD
LTREDKLQKM SFVVGAEKGC EKGKFDPDPT YELTTDNVMK MLAIHMRFRC EIPVIIMGET
GCGKTRLVRF LCDLQREGRD VENMKLVKVH GGTTSETIYK KVREAEELAQ KNRQKYKLDT
VLFFDEANTT EAIFAIKEVL CDKTVKGYPL KKNSGLKIIA ACNPYRRHTT KMVDRLERAG
LGYRVKAEET EDRLGKVPMR QLVYRVHPLP PSMVPLVWDF GQLSDSTELS YIRQIVKKKM
RDHRLPLSCQ NVITNVLAAS QKYMRNQADE CSFVSLRDVE RSMGVLLWFY NHRDIFFPSQ
DFPRFENVQM VLKCLVLAVG VCYYPSLENK RPYLATISKC FPDQFNSEES LEQEIASCQD
FLLKNIQTRE TIAKNMALKE NVFLMVVCIE LRIPLFLVGK PGSSKSLAKT VIADAMQRQA
SHCDLFKKLK EVHMVSFQCS PHSSPEGIIG TFRNCARFQK DKNLDEYVSV VVLDEIGLAE
DSPQMPLKTL HPLLEDGCID SDNPESYMKV GFVGISNWAL DPAKMNRGIF VSRWDPSEKD
LVETAEGICS SSQPVLLKIK HLLSKLAKCF LSICKTDSEQ FFGLRDYYGL IKMLFDTVKC
SDQEPSDKEL AEAVLRNFSG QRDGFDPLDY FKDIFQNIQN VQRPNTLNMI EQNLDHHIDK
ECRYLLLLTT NNAALYIIQH HIFSKENYTQ KCPEIVFGSG FPKDQEYAQI CRNVSRIKAC
METGRTVILL NLLNLYESLY DALNQYYVYF SGQQYVDLGL GSHRVKCRVH RDFRLVVVED
QEKVYKKFPV PLKNRLEKHK VDRSTDLAPW QHRVLEKLKK WAREFSKIQH SDSSEANFSV
TDAFVGFHGD ACASALLQAL KKIDKLHHNK EENREESEAH HIDREFTEFQ EKVNKFPDEA
QEDDASMEVD KVQDAEIDEE METLEDDSDL VKMVEGPVFV ETRDKIESNK TMDEEEVYEI
AKSFLLNCST PDSVLRLKYS EFGNQETEEL QKMYFHLQTH QSLRDLLNNH LNKTNQDKNR
FLEVTTFSNL LTGADVRNLG PALGLSTERF LLLSLHQFDT EASFCNKIQS FLRESGPSVH
ILLIQMDMEE SLCKNELIAS AKYCTMNEIL HLKSDECNIY TVFITKLSRI GEQCTSITGD
KYIGFQGGVW LSAHIDDLRD SDDLCLNLKA FCGIPISQLI SQTIESDVKE SDEMNTNRQQ
SEKGDSVHLH SLSLLRSCTQ KAVSLLRDTD EKTSRSMERM NILLGLLACD PGRTGARFQQ
VLLKRLVFAL IQKEELIPNA KDWVYKVAKN HEALQECGTL RHTLWRYLQD FLTPVLARIL
EVIDRDCNLY QLYGEGLSEG LTQFWLDIFE DQQLLDLIPS QNTRAPDQEI NVQCHLFVGE
VEQPCAAPYS WLIKTYCQSL WEESEFVRSS EQDIKARIQQ FVSAVSGSRL GSYIQKLSDV
ENVELGQRYL TDYVLLAFKV NSEDEHWVLQ SAVLGCVFTL QTMMSVSPEL SPSWIHAAAQ
IYNPRMDTLS HVLQLNPQLV SLIQQERPKR ESPDMCEDIL AVGICVEETK LLPVTSLTEC
LTFLQRVEQL QPCIERVLSP DYSALCSPGC LKYLETIQSV WQGILLVAVF IEKVVIKMKK
GDERIIALTL KHCSQLHGLV EGSPDFRSKD NLQQIIRILN DYHEESISSE LRYGVKCRVC
LMELSEPFAL PCEHVFCRSC LRRSMEREEA QHCPVCREPL SNNYQPTVST TLNYSFALKQ
HKEIIKCCNT FFLEVVSRFC LTDDQDPPDD LVELLFSLLI SAQGDVYKTR ELTPFLECVD
QSPVVRSVLP KLLMQYSLKQ VKKHIQSYLE DLENKLLDKE DRTELYRLFV NCFQDTLLCS
DSNGDHKHLR ENTNFLSRLA RKQTPSRQND PAEFLMSMAR LRMCLDSAAY ILSKAICQKN
NFVEAEFKFM EQVKAVCDYC DNDWYRVYLL RALNRQAGMD FLQALINSTD YEWIFPAEMM
RLHRLIPAEV DRFLCCGQSY RALRDGVGES TQVGTTDGLK EALQASVGSS PLKNALLTLA
VFRQVTCHFM SPERTLHPQE QQISILEKVI RDNMSGHARE FCTALLSNHI GGPGSNLRLG
TGVPAQRRPV LELLVHACTV FYSGNRLISP LFNIASQPQN MTGAFLPTMP DDHTSEAKQW
LSEKKLKMYF CSNSHACFVG ECGRPMAKSK CATCGVEIGG EGHIPVPGFT EAYGDYDRTR
PGHILGQART RSEAPNRKLT LAQSCVLRLC LHLAMLQGLI HYQQGIRNMI HPEVSDVYQF
LWQHLEKDME VLGKTLTLNI DDSAIVIHLI FSRFLQTTPV ANVDLSTRKS REQWEITVCK
TAISPVLQNL DRELNNAQDL IAADNRLSNS PLVKVLRGDP QRMLQLPANC PTEHSAFWSP
SSVLAVESIS QQIDQAQAPL LTLFVQKVHY IRQLDCLPAL AALLSDLIKV LPPGSETQNH
TIASLLHCIP AGHQKKLMSE RVEIYMKVWN QLRMEISSNA SLGLDSTHCE KDITSESSGQ
FLFPSRKGAG SCLHAVIDVL SETHNSLVRE ARKLCQQTDS DYKVPLAVLS KSQLALCHPE
REFLPLVLAN CHYTLEKGQQ TVSSYDHQGI ERELSRRFFA GKPRIQTDTE KYLRRHHQNF
TEVLNEVRAK IPQEMFWNPK QIHQAFSTNY HSTNRHKGLS RFYPDQPLSI TTVPDLVIPR
RPVGFQTQER HTLTPPGSHL TALNSLPAFS FCAPPISIRS TMELHLEEKD ITSFPGLDSL
PEELTWAKAA EIWRLAVQFK H
