USP9Y_HUMAN
ID USP9Y_HUMAN Reviewed; 2555 AA.
AC O00507; O14601;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase FAF-Y;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme FAF-Y;
DE AltName: Full=Fat facets protein-related, Y-linked;
DE AltName: Full=Ubiquitin thioesterase FAF-Y;
DE AltName: Full=Ubiquitin-specific protease 9, Y chromosome;
DE AltName: Full=Ubiquitin-specific-processing protease FAF-Y;
GN Name=USP9Y; Synonyms=DFFRY;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=8922996; DOI=10.1093/hmg/5.11.1695;
RA Jones M.H., Furlong R.A., Burkin H., Chalmers I.J., Brown G.M., Khwaja O.,
RA Affara N.A.;
RT "The Drosophila developmental gene fat facets has a human homologue in
RT Xp11.4 which escapes X-inactivation and has related sequences on Yq11.2.";
RL Hum. Mol. Genet. 5:1695-1701(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9381176; DOI=10.1126/science.278.5338.675;
RA Lahn B.T., Page D.C.;
RT "Functional coherence of the human Y chromosome.";
RL Science 278:675-680(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE MAPPING, AND VARIANT THR-1060.
RC TISSUE=Fetal brain, Retina, and Testis;
RX PubMed=9384609; DOI=10.1093/hmg/7.1.97;
RA Brown G.M., Furlong R.A., Sargent C.A., Erickson R.P., Longepied G.,
RA Mitchell M., Jones M.H., Hargreave T.B., Cooke H.J., Affara N.A.;
RT "Characterisation of the coding sequence and fine mapping of the human
RT DFFRY gene and comparative expression analysis and mapping to the Sxrb
RT interval of the mouse Y chromosome of the Dffry gene.";
RL Hum. Mol. Genet. 7:97-107(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12815422; DOI=10.1038/nature01722;
RA Skaletsky H., Kuroda-Kawaguchi T., Minx P.J., Cordum H.S., Hillier L.W.,
RA Brown L.G., Repping S., Pyntikova T., Ali J., Bieri T., Chinwalla A.,
RA Delehaunty A., Delehaunty K., Du H., Fewell G., Fulton L., Fulton R.,
RA Graves T.A., Hou S.-F., Latrielle P., Leonard S., Mardis E., Maupin R.,
RA McPherson J., Miner T., Nash W., Nguyen C., Ozersky P., Pepin K., Rock S.,
RA Rohlfing T., Scott K., Schultz B., Strong C., Tin-Wollam A., Yang S.-P.,
RA Waterston R.H., Wilson R.K., Rozen S., Page D.C.;
RT "The male-specific region of the human Y chromosome is a mosaic of discrete
RT sequence classes.";
RL Nature 423:825-837(2003).
RN [5]
RP POSSIBLE INVOLVEMENT IN SPGFY2.
RX PubMed=10581029; DOI=10.1038/70539;
RA Sun C., Skaletsky H., Birren B., Devon K., Tang Z., Silber S., Oates R.,
RA Page D.C.;
RT "An azoospermic man with a de novo point mutation in the Y-chromosomal gene
RT USP9Y.";
RL Nat. Genet. 23:429-432(1999).
RN [6]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [7]
RP LACK OF INVOLVEMENT IN SPERMATOGENIC FAILURE.
RX PubMed=19246359; DOI=10.1056/nejmoa0806218;
RA Luddi A., Margollicci M., Gambera L., Serafini F., Cioni M., De Leo V.,
RA Balestri P., Piomboni P.;
RT "Spermatogenesis in a man with complete deletion of USP9Y.";
RL N. Engl. J. Med. 360:881-885(2009).
CC -!- FUNCTION: May function as a ubiquitin-protein or polyubiquitin
CC hydrolase involved both in the processing of ubiquitin precursors and
CC of ubiquitinated proteins. May therefore play an important regulatory
CC role at the level of protein turnover by preventing degradation of
CC proteins through the removal of conjugated ubiquitin. Essential
CC component of TGF-beta/BMP signaling cascade. Deubiquitinates
CC monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein
CC ligase TRIM33. Monoubiquitination of SMAD4 hampers its ability to form
CC a stable complex with activated SMAD2/3 resulting in inhibition of TGF-
CC beta/BMP signaling cascade. Deubiquitination of SMAD4 by USP9X re-
CC empowers its competence to mediate TGF-beta signaling (By similarity).
CC {ECO:0000250}.
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;
CC -!- SUBUNIT: Interacts with SMAD4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long;
CC IsoId=O00507-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O00507-2; Sequence=VSP_005272;
CC -!- TISSUE SPECIFICITY: Widely expressed in embryonic and adult tissues.
CC -!- DISEASE: Note=USP9Y is located in the 'azoospermia factor a' (AZFa)
CC region on chromosome Y which is deleted in Sertoli cell-only syndrome.
CC This is an infertility disorder in which no germ cells are visible in
CC seminiferous tubules leading to azoospermia. However, AZFa deletions
CC resulting in complete loss of USP9Y have also been found in
CC normospermic men (PubMed:19246359). {ECO:0000269|PubMed:19246359}.
CC -!- DISEASE: Spermatogenic failure Y-linked 2 (SPGFY2) [MIM:415000]: A
CC disorder resulting in the absence (azoospermia) or reduction
CC (oligozoospermia) of sperm in the semen, leading to male infertility.
CC {ECO:0000269|PubMed:10581029}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry. The role of
CC USP9Y in spermatogenesis failure is uncertain (PubMed:19246359). A 4-bp
CC deletion in a splice-donor site, causing exon skipping and protein
CC truncation has been observed in non-obstructive azoospermia
CC (PubMed:10581029). However, complete USP9Y deletion has been detected
CC in individuals with no spermatogenic defects (PubMed:19246359).
CC {ECO:0000269|PubMed:10581029, ECO:0000269|PubMed:19246359}.
CC -!- MISCELLANEOUS: [Isoform Short]: May be produced at very low levels due
CC to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AF000986; AAC51833.1; -; mRNA.
DR EMBL; Y13618; CAA73940.1; -; mRNA.
DR EMBL; Y13619; CAA73941.1; -; mRNA.
DR EMBL; AC002531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14781.1; -. [O00507-1]
DR RefSeq; NP_004645.2; NM_004654.3. [O00507-1]
DR AlphaFoldDB; O00507; -.
DR SMR; O00507; -.
DR BioGRID; 113892; 67.
DR IntAct; O00507; 18.
DR MINT; O00507; -.
DR MEROPS; C19.028; -.
DR CarbonylDB; O00507; -.
DR iPTMnet; O00507; -.
DR PhosphoSitePlus; O00507; -.
DR BioMuta; USP9Y; -.
DR EPD; O00507; -.
DR jPOST; O00507; -.
DR MassIVE; O00507; -.
DR MaxQB; O00507; -.
DR PaxDb; O00507; -.
DR PeptideAtlas; O00507; -.
DR PRIDE; O00507; -.
DR ProteomicsDB; 47948; -. [O00507-1]
DR ProteomicsDB; 47949; -. [O00507-2]
DR Antibodypedia; 21866; 33 antibodies from 14 providers.
DR DNASU; 8287; -.
DR Ensembl; ENST00000338981.7; ENSP00000342812.3; ENSG00000114374.13. [O00507-1]
DR Ensembl; ENST00000651177.1; ENSP00000498372.1; ENSG00000114374.13. [O00507-1]
DR GeneID; 8287; -.
DR KEGG; hsa:8287; -.
DR MANE-Select; ENST00000338981.7; ENSP00000342812.3; NM_004654.4; NP_004645.2.
DR UCSC; uc004fst.2; human. [O00507-1]
DR CTD; 8287; -.
DR DisGeNET; 8287; -.
DR GeneCards; USP9Y; -.
DR GeneReviews; USP9Y; -.
DR HGNC; HGNC:12633; USP9Y.
DR HPA; ENSG00000114374; Low tissue specificity.
DR MalaCards; USP9Y; -.
DR MIM; 400005; gene.
DR MIM; 415000; phenotype.
DR neXtProt; NX_O00507; -.
DR OpenTargets; ENSG00000114374; -.
DR Orphanet; 1646; Partial chromosome Y deletion.
DR PharmGKB; PA37258; -.
DR VEuPathDB; HostDB:ENSG00000114374; -.
DR GeneTree; ENSGT00940000155375; -.
DR HOGENOM; CLU_000331_1_0_1; -.
DR InParanoid; O00507; -.
DR OMA; KVCARGK; -.
DR OrthoDB; 625455at2759; -.
DR PhylomeDB; O00507; -.
DR TreeFam; TF323966; -.
DR PathwayCommons; O00507; -.
DR SignaLink; O00507; -.
DR BioGRID-ORCS; 8287; 13 hits in 705 CRISPR screens.
DR ChiTaRS; USP9Y; human.
DR GeneWiki; USP9Y; -.
DR GenomeRNAi; 8287; -.
DR Pharos; O00507; Tdark.
DR PRO; PR:O00507; -.
DR Proteomes; UP000005640; Chromosome Y.
DR RNAct; O00507; protein.
DR Bgee; ENSG00000114374; Expressed in right lung and 173 other tissues.
DR ExpressionAtlas; O00507; baseline and differential.
DR Genevisible; O00507; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070410; F:co-SMAD binding; ISS:BHF-UCL.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
DR GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Hydrolase; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..2555
FT /note="Probable ubiquitin carboxyl-terminal hydrolase FAF-
FT Y"
FT /id="PRO_0000080690"
FT DOMAIN 1559..1958
FT /note="USP"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2476..2555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2503..2517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2524..2548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1568
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 1881
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93008"
FT MOD_RES 591
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q93008"
FT MOD_RES 2444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93008"
FT MOD_RES 2541
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q93008"
FT MOD_RES 2548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93008"
FT VAR_SEQ 2071..2555
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_005272"
FT VARIANT 65
FT /note="E -> D (in dbSNP:rs7067496)"
FT /id="VAR_055350"
FT VARIANT 211
FT /note="R -> C (in dbSNP:rs2032596)"
FT /id="VAR_055351"
FT VARIANT 1035
FT /note="P -> S (in dbSNP:rs20319)"
FT /id="VAR_029328"
FT VARIANT 1060
FT /note="A -> T (in dbSNP:rs20320)"
FT /evidence="ECO:0000269|PubMed:9384609"
FT /id="VAR_016194"
FT VARIANT 1705
FT /note="A -> S (in dbSNP:rs2032606)"
FT /id="VAR_055352"
FT CONFLICT 206
FT /note="D -> E (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="I -> M (in Ref. 2; AAC51833)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="D -> Y (in Ref. 2; AAC51833)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="S -> A (in Ref. 2; AAC51833)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="L -> V (in Ref. 2; AAC51833)"
FT /evidence="ECO:0000305"
FT CONFLICT 883
FT /note="R -> C (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 907
FT /note="S -> F (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 946
FT /note="D -> N (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1002
FT /note="E -> K (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1017
FT /note="R -> K (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1025..1027
FT /note="VAD -> FAN (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1038..1039
FT /note="RD -> KN (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1067
FT /note="K -> N (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1258
FT /note="V -> F (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1733
FT /note="Y -> F (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 1953
FT /note="L -> P (in Ref. 3; CAA73940/CAA73941)"
FT /evidence="ECO:0000305"
FT CONFLICT 2086
FT /note="R -> G (in Ref. 2; AAC51833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2555 AA; 291077 MW; 421D47D5899F4415 CRC64;
MTAITHGSPV GGNDSQGQVL DGQSQHLFQQ NQTSSPDSSN ENSVATPPPE EQGQGDAPPQ
HEDEEPAFPH TELANLDDMI NRPRWVVPVL PKGELEVLLE AAIDLSVKGL DVKSEACQRF
FRDGLTISFT KILMDEAVSG WKFEIHRCII NNTHRLVELC VAKLSQDWFP LLELLAMALN
PHCKFHIYNG TRPCELISSN AQLPEDELFA RSSDPRSPKG WLVDLINKFG TLNGFQILHD
RFFNGSALNI QIIAALIKPF GQCYEFLSQH TLKKYFIPVI EIVPHLLENL TDEELKKEAK
NEAKNDALSM IIKSLKNLAS RISGQDETIK NLEIFRLKMI LRLLQISSFN GKMNALNEIN
KVISSVSYYT HRHSNPEEEE WLTAERMAEW IQQNNILSIV LQDSLHQPQY VEKLEKILRF
VIKEKALTLQ DLDNIWAAQA GKHEAIVKNV HDLLAKLAWD FSPGQLDHLF DCFKASWTNA
SKKQREKLLE LIRRLAEDDK DGVMAHKVLN LLWNLAQSDD VPVDIMDLAL SAHIKILDYS
CSQDRDAQKI QWIDHFIEEL RTNDKWVIPA LKQIREICSL FGEASQNLSQ TQRSPHIFYR
HDLINQLQQN HALVTLVAEN LATYMNSIRL YAGDHEDYDP QTVRLGSRYS HVQEVQERLN
FLRFLLKDGQ LWLCAPQAKQ IWKCLAENAV YLCDREACFK WYSKLMGDEP DLDPDINKDF
FESNVLQLDP SLLTENGMKC FERFFKAVNC RERKLIAKRR SYMMDDLELI GLDYLWRVVI
QSSDEIANRA IDLLKEIYTN LGPRLKANQV VIHEDFIQSC FDRLKASYDT LCVFDGDKNS
INCARQEAIR MVRVLTVIKE YINECDSDYH KERMILPMSR AFRGKHLSLI VRFPNQGRQV
DELDIWSHTN DTIGSVRRCI VNRIKANVAH KKIELFVGGE LIDSEDDRKL IGQLNLKDKS
LITAKLTQIN FNMPSSPDSS SDSSTASPGN HRNHYNDGPN LEVESCLPGV IMSVHPRYIS
FLWQVADLGS NLNMPPLRDG ARVLMKLMPP DRTAVEKLRA VCLDHAKLGE GKLSPPLDSL
FFGPSASQVL YLTEVVYALL MPAGVPLTDG SSDFQVHFLK SGGLPLVLSM LIRNNFLPNT
DMETRRGAYL NALKIAKLLL TAIGYGHVRA VAEACQPVVD GTDPITQINQ VTHDQAVVLQ
SALQSIPNPS SECVLRNESI LLAQEISNEA SRYMPDICVI RAIQKIIWAS ACGALGLVFS
PNEEITKIYQ MTTNGSNKLE VEDEQVCCEA LEVMTLCFAL LPTALDALSK EKAWQTFIID
LLLHCPSKTV RQLAQEQFFL MCTRCCMGHR PLLFFITLLF TILGSTAREK GKYSGDYFTL
LRHLLNYAYN GNINIPNAEV LLVSEIDWLK RIRDNVKNTG ETGVEEPILE GHLGVTKELL
AFQTSEKKYH FGCEKGGANL IKELIDDFIF PASKVYLQYL RSGELPAEQA IPVCSSPVTI
NAGFELLVAL AIGCVRNLKQ IVDCLTEMYY MGTAITTCEA LTEWEYLPPV GPRPPKGFVG
LKNAGATCYM NSVIQQLYMI PSIRNSILAI EGTGSDLHDD MFGDEKQDSE SNVDPRDDVF
GYPHQFEDKP ALSKTEDRKE YNIGVLRHLQ VIFGHLAASQ LQYYVPRGFW KQFRLWGEPV
NLREQHDALE FFNSLVDSLD EALKALGHPA ILSKVLGGSF ADQKICQGCP HRYECEESFT
TLNVDIRNHQ NLLDSLEQYI KGDLLEGANA YHCEKCDKKV DTVKRLLIKK LPRVLAIQLK
RFDYDWEREC AIKFNDYFEF PRELDMGPYT VAGVANLERD NVNSENELIE QKEQSDNETA
GGTKYRLVGV LVHSGQASGG HYYSYIIQRN GKDDQTDHWY KFDDGDVTEC KMDDDEEMKN
QCFGGEYMGE VFDHMMKRMS YRRQKRWWNA YILFYEQMDM IDEDDEMIRY ISELTIARPH
QIIMSPAIER SVRKQNVKFM HNRLQYSLEY FQFVKKLLTC NGVYLNPAPG QDYLLPEAEE
ITMISIQLAA RFLFTTGFHT KKIVRGPASD WYDALCVLLR HSKNVRFWFT HNVLFNVSNR
FSEYLLECPS AEVRGAFAKL IVFIAHFSLQ DGSCPSPFAS PGPSSQACDN LSLSDHLLRA
TLNLLRREVS EHGHHLQQYF NLFVMYANLG VAEKTQLLKL NVPATFMLVS LDEGPGPPIK
YQYAELGKLY SVVSQLIRCC NVSSTMQSSI NGNPPLPNPF GDLNLSQPIM PIQQNVLDIL
FVRTSYVKKI IEDCSNSEDT IKLLRFCSWE NPQFSSTVLS ELLWQVAYSY TYELRPYLDL
LFQILLIEDS WQTHRIHNAL KGIPDDRDGL FDTIQRSKNH YQKRAYQCIK CMVALFSSCP
VAYQILQGNG DLKRKWTWAV EWLGDELERR PYTGNPQYSY NNWSPPVQSN ETANGYFLER
SHSARMTLAK ACELCPEEEP DDQDAPDEHE PSPSEDAPLY PHSPASQYQQ NNHVHGQPYT
GPAAHHLNNP QKTGQRTQEN YEGNEEVSSP QMKDQ
