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   02-SEP-2026, entry version 195.
DE   RecName: Full=Ubiquitinyl hydrolase FAF {ECO:0000305};
DE            EC=3.4.19.12 {ECO:0000269|PubMed:23919485};
DE   AltName: Full=Protein fat facets {ECO:0000312|FlyBase:FBgn0005632};
DE   AltName: Full=Ubiquitin thioesterase FAF;
DE   AltName: Full=Ubiquitin-specific-processing protease FAF;
DE            Short=Deubiquitinating enzyme FAF;
GN   Name=faf {ECO:0000312|FlyBase:FBgn0005632};
GN   ORFNames=CG1945 {ECO:0000312|FlyBase:FBgn0005632};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; 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, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=22745309; DOI=10.1242/dev.077206;
RA   Stinchfield M.J., Takaesu N.T., Quijano J.C., Castillo A.M., Tiusanen N.,
RA   Shimmi O., Enzo E., Dupont S., Piccolo S., Newfeld S.J.;
RT   "Fat facets deubiquitylation of Medea/Smad4 modulates interpretation of a
RT   Dpp morphogen gradient.";
RL   Development 139:2721-2729(2012).
RN   [7]
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 (PubMed:1295747,
CC       PubMed:23919485). involved imd/NF-kappa-B (IMD) signaling cascade
CC       during development (PubMed:1295747, PubMed:23919485). Required for eye
CC       and embryo development, and plays a role in compound eye assembly and
CC       oogenesis respectively (PubMed:1295747). Involved in dpp/BMP-like
CC       signaling-dependent dorsoventral patterning during embryogenesis,
CC       probably by regulating the ubiquitination of the co-SMAD Med
CC       (PubMed:22745309). In the larval eye disks, cells outside the
CC       assembling facets require this protein for short-range cell
CC       interactions that prevent the mystery cells from becoming
CC       photoreceptors (PubMed:1295747). Also required for nuclear migration
CC       and cellularization in early embryogenesis and could play a role in
CC       pole cell determination, development or function (PubMed:1295747).
CC       Regulates the IMD signaling cascade at later stages of infection
CC       (around 6 hours post-infection) by inhibiting the expression of the
CC       antimicrobial peptides Dpt and Dro (PubMed:23919485). Acts by
CC       modulating the state of imd polyubiquitination and/or stability; a
CC       function which appears to be independent of its enzymatic activity
CC       (PubMed:23919485). In turn, imd enhances the polyubiquitination and
CC       stability of faf suggesting that they may form a regulatory feedback
CC       mechanism within the IMD pathway (PubMed:23919485).
CC       {ECO:0000269|PubMed:1295747, ECO:0000269|PubMed:22745309,
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, ECO:0000269|PubMed:22745309}.
CC   -!- PTM: Ubiquitinated. Ubiquitination is enhanced by the expression of
CC       imd. {ECO:0000269|PubMed:23919485}.
CC   -!- DISRUPTION PHENOTYPE: Early embryonic lethal with arrest in the
CC       blastoderm stage. {ECO:0000305|PubMed:22745309}.
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; 34.
DR   FunCoup; P55824; 2131.
DR   IntAct; P55824; 12.
DR   STRING; 7227.FBpp0085202; -.
DR   MEROPS; C19.007; -.
DR   GlyGen; P55824; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P55824; -.
DR   PaxDb; 7227-FBpp0085202; -.
DR   PeptideAtlas; P55824; -.
DR   EnsemblMetazoa; FBtr0085843; FBpp0085202; FBgn0005632.
DR   GeneID; 43749; -.
DR   KEGG; dme:Dmel_CG1945; -.
DR   AGR; FB:FBgn0005632; -.
DR   CTD; 43749; -.
DR   FlyBase; FBgn0005632; faf.
DR   VEuPathDB; VectorBase:FBgn0005632; -.
DR   eggNOG; KOG1866; Eukaryota.
DR   InParanoid; P55824; -.
DR   OMA; YDYEREC; -.
DR   OrthoDB; 289038at2759; -.
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   GenomeRNAi; 43749; -.
DR   PRO; PR:P55824; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0005632; Expressed in adult midgut enterocyte in digestive tract and 248 other cell types or tissues.
DR   ExpressionAtlas; P55824; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:FlyBase.
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:0030513; P:positive regulation of BMP signaling pathway; IGI:FlyBase.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   CDD; cd02659; peptidase_C19C; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR056850; ARM_UBP34_24_USP9X_Y.
DR   InterPro; IPR021905; DUF3517.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR050164; Peptidase_C19.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR055176; UBP24/USP9X/USP9Y_UBL.
DR   InterPro; IPR028889; USP.
DR   InterPro; IPR018200; USP_CS.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF925; UBIQUITINYL HYDROLASE 1; 1.
DR   Pfam; PF25010; ARM_UBP24_USP9X-Y; 1.
DR   Pfam; PF12030; DUF3517; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF22900; UCH_UBL1; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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="Ubiquitinyl 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        10..39
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1070..1082
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2614..2627
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2644..2671
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2672..2691
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
//