FAF_DROME
ID FAF_DROME Reviewed; 2778 AA.
AC P55824; Q9V9T6; Q9Y0Z7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase FAF;
DE EC=3.4.19.12 {ECO:0000269|PubMed:23919485};
DE AltName: Full=Protein fat facets;
DE AltName: Full=Ubiquitin thioesterase FAF;
DE AltName: Full=Ubiquitin-specific-processing protease FAF;
DE Short=Deubiquitinating enzyme FAF;
GN Name=faf; ORFNames=CG1945;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Eye imaginal disk;
RX PubMed=1295747; DOI=10.1242/dev.116.4.985;
RA Fischer-Vize J.A., Rubin G.M., Lehmann R.;
RT "The fat facets gene is required for Drosophila eye and embryo
RT development.";
RL Development 116:985-1000(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1089-2778 (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH IMD, TISSUE SPECIFICITY,
RP UBIQUITINATION, AND MUTAGENESIS OF CYS-1677.
RX PubMed=23919485; DOI=10.1111/gtc.12085;
RA Yagi Y., Lim Y.M., Tsuda L., Nishida Y.;
RT "fat facets induces polyubiquitination of Imd and inhibits the innate
RT immune response in Drosophila.";
RL Genes Cells 18:934-945(2013).
CC -!- FUNCTION: Ubiquitin C-terminal hydrolase involved in development and
CC the imd/NF-kappa-B (IMD) signaling cascade (PubMed:23919485,
CC PubMed:1295747). Required for eye and embryo development, and plays a
CC role in compound eye assembly and oogenesis respectively
CC (PubMed:1295747). In the larval eye disks, cells outside the assembling
CC facets require this protein for short-range cell interactions that
CC prevent the mystery cells from becoming photoreceptors
CC (PubMed:1295747). Also required for nuclear migration and
CC cellularization in early embryogenesis and could play a role in pole
CC cell determination, development or function (PubMed:1295747). Regulates
CC the IMD signaling cascade at later stages of infection (around 6 hours
CC post-infection) by inhibiting the expression of the antimicrobial
CC peptides Dpt and Dro (PubMed:23919485). Acts by modulating the state of
CC imd polyubiquitination and/or stability; a function which appears to be
CC independent of its enzymatic activity (PubMed:23919485). In turn, imd
CC enhances the polyubiquitination and stability of faf suggesting that
CC they may form a regulatory feedback mechanism within the Imd pathway
CC (PubMed:23919485). {ECO:0000269|PubMed:1295747,
CC ECO:0000269|PubMed:23919485}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:23919485};
CC -!- SUBUNIT: Interacts with imd. {ECO:0000269|PubMed:23919485}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=P55824-1; Sequence=Displayed;
CC Name=3;
CC IsoId=P55824-3; Sequence=VSP_005269;
CC -!- TISSUE SPECIFICITY: Eye disks and ovaries (PubMed:1295747). Expressed
CC in larval fat body (PubMed:23919485). {ECO:0000269|PubMed:1295747,
CC ECO:0000269|PubMed:23919485}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:1295747}.
CC -!- PTM: Ubiquitinated. Ubiquitination is enhanced by the expression of
CC imd. {ECO:0000269|PubMed:23919485}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION: [Isoform 1]:
CC Sequence=AAF01345.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L04959; AAF01345.1; ALT_FRAME; mRNA.
DR EMBL; L04958; AAF01346.1; -; mRNA.
DR EMBL; L04960; AAF01347.1; -; Genomic_DNA.
DR EMBL; L04960; AAF01348.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF57198.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14291.1; -; Genomic_DNA.
DR EMBL; AF145677; AAD38652.1; -; mRNA.
DR PIR; B49132; B49132.
DR RefSeq; NP_524612.2; NM_079873.5. [P55824-1]
DR RefSeq; NP_733455.1; NM_170576.3. [P55824-3]
DR SMR; P55824; -.
DR BioGRID; 68590; 29.
DR IntAct; P55824; 8.
DR STRING; 7227.FBpp0085202; -.
DR MEROPS; C19.007; -.
DR iPTMnet; P55824; -.
DR PaxDb; P55824; -.
DR PRIDE; P55824; -.
DR EnsemblMetazoa; FBtr0085843; FBpp0085202; FBgn0005632. [P55824-1]
DR EnsemblMetazoa; FBtr0085844; FBpp0085203; FBgn0005632. [P55824-3]
DR GeneID; 43749; -.
DR KEGG; dme:Dmel_CG1945; -.
DR CTD; 43749; -.
DR FlyBase; FBgn0005632; faf.
DR VEuPathDB; VectorBase:FBgn0005632; -.
DR eggNOG; KOG1866; Eukaryota.
DR GeneTree; ENSGT00940000168609; -.
DR InParanoid; P55824; -.
DR OMA; CCDVSSK; -.
DR PhylomeDB; P55824; -.
DR Reactome; R-DME-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-DME-9013420; RHOU GTPase cycle.
DR Reactome; R-DME-9013424; RHOV GTPase cycle.
DR Reactome; R-DME-9033241; Peroxisomal protein import.
DR SignaLink; P55824; -.
DR BioGRID-ORCS; 43749; 1 hit in 3 CRISPR screens.
DR ChiTaRS; faf; fly.
DR GenomeRNAi; 43749; -.
DR PRO; PR:P55824; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0005632; Expressed in egg chamber and 30 other tissues.
DR ExpressionAtlas; P55824; baseline and differential.
DR Genevisible; P55824; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0008354; P:germ cell migration; TAS:FlyBase.
DR GO; GO:0008583; P:mystery cell differentiation; IMP:FlyBase.
DR GO; GO:0045824; P:negative regulation of innate immune response; HMP:FlyBase.
DR GO; GO:0035192; P:nuclear cortical migration; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:FlyBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021905; DUF3517.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF12030; DUF3517; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation; Hydrolase;
KW Oogenesis; Phosphoprotein; Protease; Reference proteome;
KW Sensory transduction; Thiol protease; Ubl conjugation;
KW Ubl conjugation pathway; Vision.
FT CHAIN 1..2778
FT /note="Probable ubiquitin carboxyl-terminal hydrolase FAF"
FT /id="PRO_0000080688"
FT DOMAIN 1668..2062
FT /note="USP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2568..2632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2644..2691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2568..2584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2605..2626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1677
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093,
FT ECO:0000305|PubMed:23919485"
FT ACT_SITE 1986
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 2705..2778
FT /note="KCRRVIIKKLVESKDEEDATTATTAATTEVTTSPATAIATAATLEPAGMSEL
FT TTMVEKNLIISQENPQAKSSLQ -> VTRANNV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:1295747"
FT /id="VSP_005269"
FT MUTAGEN 1677
FT /note="C->S: Loss of enzymatic activity. Increased
FT susceptibility to infections by E.cloacae. No effect on
FT binding and polyubiquitination of imd."
FT /evidence="ECO:0000269|PubMed:23919485"
FT CONFLICT 234
FT /note="E -> D (in Ref. 1; AAF01345/AAF01346)"
FT /evidence="ECO:0000305"
FT CONFLICT 2725
FT /note="T -> S (in Ref. 1; AAF01345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2778 AA; 311143 MW; FFB90438BA53A02B CRC64;
MTFDTRRHTT GQPGSTAPSS SSSTTSTTTT TTSPAQSAGS GSGIGTGTGT VANSSLPGGG
SGSLDGNQDQ QPATDSQSSD DVAASLSANS VDSTITIVPP EKLISSFPTT KLRSLTQKIS
NPRWVVPVLP EQELEVLLNA AIELTQAGVD HDCEPCVEFY RNGLSTSFAK ILTDEAVNSW
KNNIHHCILV SCGKLLHLIA IHMQRDNPYL LDLLAIVFDP ENKFNTFNAG RQPECFAAPD
YIWGQLDSNK MYARPPPEPK NARGWLVDLI NRFGQLGGFD NLLERFNIGL ELLKRNQNKC
TGKNISVEGR VENGAQDNRL TLALIHSLLR PFGQCYELLM PATIAKYFMP TWNVVLDLLD
SFTDEELKRE VKPEGRNDYI NGIVKSARLL ASRLTGQEEL IRDLEMFRLK MILRLLQVSS
FNGKMNALNE INKVLSSVAY FSHRSQPLPH CMPEDEMDWL TADRMAQWIK SSDVLGVVLK
DSLHQPQYVE KLEKIIRFLI KEQALTLDDL DAVWRAQAGK HEAIVKNVHD LLAKLAWDFT
PEQLDHLFEA FQASMTTANK RQRERLLELI RRLAEDDKNG VMAQKVLKLF WTLAHSQEVP
PEVLDQALGA HVKILDYSCS QERDAQKTIW LDKCVDELKS GDGWVLPALR LIRDICCLYD
TTTNHAQRTQ TSTNRQQVIE RLQNDYSLVI LVTNSLTAYM EKVRQMVTDS PGLDATRILI
DGRFPHHVQI AERLEFLKFL LKDGQLWLCA DQAKQIWHCL AVNAVFPADR EECFRWFGKL
MGEEPDLDPG INKDFFENNI LQLDPHLLTE SGIKCFERFF KAVNSKEDKL KAIHRGYMLD
NEDLIGKDYL WRVITTGGEE IASKAIDLLK EVSTALGPRL QENIAEFHEM FIGECCSRLR
THYGNIVILG KTQLQEELDA PDQSDNTNDE SKDSKMRFIE AEKMCRILKV LQEYVKECDR
SFSGDRVHLP LSRVTRGKNT ILYIRFQNPG RSIDDMEIVT HSNETMAAFK RNLLKRIKGT
STANIKVDLF YANDEMIGVS DEINPLYQYT IRDKMNLTAK LTPVGTGLAS SPDSSSDSST
GSPPRPCPDM QRVESESTLP GVIISQNYQY TEFFLKLYQL GSDLEHGRLR DSAKVLLHLL
PCDRQTIRQL KIMCKVPKAA VTVAVTGDKI AKDEEEKLYP TEQAGIEDEE EHCTPEQMFL
HPTPAQVLYN LSVLHGLLIP ALDPLGESAL LVQSAWMHSG CAHFVLELLT KNNFLPSADM
HTKRASFQCV LRLAKLFLYI VGSVLSRVGD EPMICDLDNG SRSQVDILKQ NFSTMPSSSQ
GTLRAISAKL AVILAREMLS ASPEGDRCRT LFSSTLQWSC PDISTIKAVV QLAWASSCGN
LQALGNSSGD FEDEVIVPDG QDFSMCKEAL EVLTISFILN PSANEALTSD PNWPKFITSI
VLKNPLRHVR QVASEQLFLA STYCAGDRRP FVYMVNLLVG ALKTLVPQYE STCAEFFSVL
CRTLSYGCIY NWPLQISEGL LGDEIKWLQR IRENVHATGD TQVHEELLEG HLCLAKELMF
FLGADSKAQL NELIHELIDD FLFTASREFL HLRRHGSLRQ DTVPPPVCRS PHTIAAACDL
LIALCQLCVP NMKLLTNTLI DFVCTDTDPL REWDYLPPVG ARPTKGFCGL KNAGATCYMN
SVLQQLYMVP AVRVGILRAH GAATTDGEDF SGDSDLTGGG LGSALFSGPA SALVSLPSSS
STIEDGLHDV RKNYHVVILK HVQAIFAHLG HSALQYYVPR GLWTHFKLLG EPVNLREQQD
AVEFFMSLLE SLDEGLKALG QPQLMNATLG GSFSDQKICQ ECPHRYSKEE PFSVFSVDIR
NHSSLTESLE QYVKGELLEG ADAYHCDKCD KKVVTVKRVC VKKLPPVLAI QLKRFEYDYE
RVCAIKFNDY FEFPRILDME PYTVSGLAKL EGEVVEVGDN CQTNVETTKY ELTGIVVHSG
QASGGHYFSY ILSKNPANGK CQWYKFDDGE VTECKMHEDE EMKAECFGGE YMGETYDNNL
KRMQYRRQKR WWNAYMLFYT RCDQTPVQYE PSVEQLSLAE SRNMVLPLPK PIERSVRHQN
IRFLHSRSIF SVEFFNFIKK LVSCNLLSAR SNKITPAAEE LSLLGVQLAS QFLFHTGFRT
KKSLRGPVME WYDALSHHIR SSALVRKWFA NHALLSPPSR LGEYILMAPS PDVRTVFVKL
VVFFCHFAIN DEPLTGYDGA NLCEQVLISV LRLLKSEAAD YGKHLPHYFS LFSMYVGLGT
REKQQLLRLN VPLQFIQVAL DDGPGPAIKY QYPEFSKLHQ VVSHLIRCSD VSEKCQSSNQ
NARPLSNPFK DPNVAHEELT PLSTECMDLL FNRTGYIKKV IEDTNVGDEG LKLLQYCSWE
NPHFSRAVLT ELLWQCGFAY CHDMRHHTDL LLNILLIDDS WQHHRIHNAL NGVAEEREGL
LETIQRAKTH YQKRAYQIIK CLTQLFHKSP IALQMLHTNS NITRHWSIAV EWLQGELDRQ
RGIGCQYNSY SWSPPAQSND NTNGYMLERS QSAKNTWSMA FELCPDEVSE KTDENNEPNL
ETNMDENKSE PVAQPGGVLE GSTGGTEQLP ENKTPTTSSP STAAWPARGD SNAIPRLSRQ
LFGAYTSTGS GSTSGGSAPT SALTTTAGSG ANSETESSAQ ETTGETTING LTNSLDQMEI
TAKKKCRRVI IKKLVESKDE EDATTATTAA TTEVTTSPAT AIATAATLEP AGMSELTTMV
EKNLIISQEN PQAKSSLQ
