UBP47_MOUSE
ID UBP47_MOUSE Reviewed; 1376 AA.
AC Q8BY87; Q32NY0; Q5EBP2; Q6KAR9; Q80V06; Q8BHU1; Q8BI15; Q8BI16; Q8BUW4;
AC Q91X25;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 47;
DE AltName: Full=Ubiquitin thioesterase 47;
DE AltName: Full=Ubiquitin-specific-processing protease 47;
GN Name=Usp47;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-379 (ISOFORM 1), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-591 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 637-1376 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1376.
RC TISSUE=Brain;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He, and Czech II;
RC TISSUE=Brain, Liver, Mammary gland, and Mesenchymal stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1016, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911; SER-934; SER-1014 AND
RP THR-1016, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION.
RX PubMed=19966869; DOI=10.1038/onc.2009.430;
RA Peschiaroli A., Skaar J.R., Pagano M., Melino G.;
RT "The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor
RT regulating cell survival.";
RL Oncogene 29:1384-1393(2010).
CC -!- FUNCTION: Ubiquitin-specific protease that specifically deubiquitinates
CC monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby
CC playing a role in base-excision repair (BER) (By similarity). Acts as a
CC regulator of cell growth and genome integrity. May also indirectly
CC regulate CDC25A expression at a transcriptional level. {ECO:0000250,
CC ECO:0000269|PubMed:19966869}.
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 BTRC and FBXW11. Interacts with POLB (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BY87-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BY87-2; Sequence=VSP_014416;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP47 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27179.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC27195.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC38411.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK030909; BAC27179.1; ALT_INIT; mRNA.
DR EMBL; AK030963; BAC27195.1; ALT_INIT; mRNA.
DR EMBL; AK041541; BAC30979.1; -; mRNA.
DR EMBL; AK082114; BAC38411.1; ALT_FRAME; mRNA.
DR EMBL; AK087981; BAC40073.1; -; mRNA.
DR EMBL; AK131138; BAD21388.1; -; mRNA.
DR EMBL; BC012722; AAH12722.1; -; mRNA.
DR EMBL; BC024117; AAH24117.1; -; mRNA.
DR EMBL; BC089364; AAH89364.1; -; mRNA.
DR EMBL; BC108425; AAI08426.1; -; mRNA.
DR CCDS; CCDS40089.1; -. [Q8BY87-2]
DR CCDS; CCDS85384.1; -. [Q8BY87-1]
DR RefSeq; NP_598519.2; NM_133758.3. [Q8BY87-2]
DR RefSeq; NP_796223.2; NM_177249.3. [Q8BY87-1]
DR AlphaFoldDB; Q8BY87; -.
DR SMR; Q8BY87; -.
DR BioGRID; 217138; 5.
DR IntAct; Q8BY87; 1.
DR MINT; Q8BY87; -.
DR STRING; 10090.ENSMUSP00000102264; -.
DR MEROPS; C19.055; -.
DR iPTMnet; Q8BY87; -.
DR PhosphoSitePlus; Q8BY87; -.
DR EPD; Q8BY87; -.
DR jPOST; Q8BY87; -.
DR MaxQB; Q8BY87; -.
DR PaxDb; Q8BY87; -.
DR PeptideAtlas; Q8BY87; -.
DR PRIDE; Q8BY87; -.
DR ProteomicsDB; 298364; -. [Q8BY87-1]
DR ProteomicsDB; 298365; -. [Q8BY87-2]
DR Antibodypedia; 24483; 159 antibodies from 26 providers.
DR DNASU; 74996; -.
DR Ensembl; ENSMUST00000106653; ENSMUSP00000102264; ENSMUSG00000059263. [Q8BY87-2]
DR Ensembl; ENSMUST00000210309; ENSMUSP00000147619; ENSMUSG00000059263. [Q8BY87-1]
DR GeneID; 74996; -.
DR KEGG; mmu:74996; -.
DR UCSC; uc009jgg.2; mouse. [Q8BY87-2]
DR UCSC; uc009jgh.2; mouse. [Q8BY87-1]
DR CTD; 55031; -.
DR MGI; MGI:1922246; Usp47.
DR VEuPathDB; HostDB:ENSMUSG00000059263; -.
DR eggNOG; KOG4598; Eukaryota.
DR GeneTree; ENSGT00940000157223; -.
DR HOGENOM; CLU_002928_0_0_1; -.
DR InParanoid; Q8BY87; -.
DR OMA; FLCEWIV; -.
DR OrthoDB; 77113at2759; -.
DR PhylomeDB; Q8BY87; -.
DR TreeFam; TF314142; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 74996; 2 hits in 107 CRISPR screens.
DR ChiTaRS; Usp47; mouse.
DR PRO; PR:Q8BY87; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BY87; protein.
DR Bgee; ENSMUSG00000059263; Expressed in ciliary body and 240 other tissues.
DR ExpressionAtlas; Q8BY87; baseline and differential.
DR Genevisible; Q8BY87; MM.
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:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0101005; F:deubiquitinase activity; ISO:MGI.
DR GO; GO:0071987; F:WD40-repeat domain binding; ISO:MGI.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR045578; USP47_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF19718; USP47_C; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 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 Acetylation; Alternative splicing; Cytoplasm; DNA damage; DNA repair;
KW Hydrolase; Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1376
FT /note="Ubiquitin carboxyl-terminal hydrolase 47"
FT /id="PRO_0000080677"
FT DOMAIN 188..564
FT /note="USP"
FT REGION 426..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 503
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96K76"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96K76"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1016
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1018
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96K76"
FT VAR_SEQ 14..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014416"
FT CONFLICT 341
FT /note="A -> G (in Ref. 1; BAC38411)"
FT /evidence="ECO:0000305"
FT CONFLICT 376..379
FT /note="GLRF -> VRDL (in Ref. 1; BAC38411)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="R -> G (in Ref. 3; AAI08426)"
FT /evidence="ECO:0000305"
FT CONFLICT 1174
FT /note="I -> T (in Ref. 3; AAI08426)"
FT /evidence="ECO:0000305"
FT CONFLICT 1178
FT /note="R -> H (in Ref. 1; BAC27195)"
FT /evidence="ECO:0000305"
FT CONFLICT 1200..1203
FT /note="DINI -> IYNF (in Ref. 1; BAC40073)"
FT /evidence="ECO:0000305"
FT CONFLICT 1257
FT /note="R -> Q (in Ref. 1; BAC27195)"
FT /evidence="ECO:0000305"
FT CONFLICT 1299..1301
FT /note="VST -> TRP (in Ref. 3; AAH12722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1376 AA; 157455 MW; 09729C3B691C3709 CRC64;
MVPGEENQLV PKEDVFWRCR QNIFDEMKKK FLQIENAAEE PRVLCIIQDT TNSKTVSERI
TLNLPASTPV RKLFEDVANK VGYINGTFDL TRENGVTTAD MAPLDHTSDK SLLDANFEPG
KKNFLHLTDK DGEPPQMLLE DSNNVDDSVH DRFIGPLPRE GSVASTNDYV SQNYSYSSIL
NKSETGYVGL VNQAMTCYLN SLLQTLFMTP EFRNALYKWE FEDSEEDPVT SIPYQLQRLF
VLLQTSKKRA IETTDVTRSF GWDSSEAWQQ HDVQELCRVM FDALEQKWKQ TEQADLINEL
YQGKLKDYVR CLECGYEGWR IDTYLDIPLV IRPYGSSQAF ASVEEALHAF IQPEILDGPN
QYFCERCKKK CDARKGLRFL HFPYLLTLQL KRFDFDYTTM HRIKLNDRMS FPEELDMSTF
IDIEDEKSPQ TESCTDSGAE NEGSCHSDQM SNDFSTDDAV DEGICLESSS GSEKISKPGL
EKNSLMYELF SVMVHSGSAA GGHYYACIKS FSDDQWYSFN DQHVSRITQE DIKKTHGGSS
GSRGYYSSAF ASSTNAYMLI YRLKDPTRNA KFLEVDEYPE HIKNLVQKER ELEEQEKRQR
EIERNTCKIK LFCLHPVKQV MMENKLEVHK DKTLKEAVEM AYKMMDLEDV IPLDCCRLVK
YDEFHDYLER SYEGEEDTPM GLLLGGVKST YMFDLLLETR KPDQIFQSYK PGEVMVKVHV
VDLKAETVAA PVTVRAYLNQ TVTEFKQLIS KATHLPADSM RIVLERCYND LRLLSMPSKT
LKAEGFFRSN KVFVESSETV DHQAAFTDSH LWKLLDRHAN TIRLFVLLPE QSPGSYSKRT
AYQKAGGDSG NVDDDCERVK GPAGNLKSVD AILEESTEKL KSLSLQQQQQ DGDNGDSSKS
TETSDFENIE SPLNERGSST SVDNRELEQH IQTSDPENFQ SEERSDSDVN NDRSTSSVDS
DILSSSHSSD TLCNADSAQI PLANGLDSHS ITSSRRTKAN EGKKETWDTA EEDSGTDSEY
DESGKSRGDM QYMYFKADPY TADEGSGEGH KWLMVHVDKR ITLAAFKQHL EPFVGVLSSH
FKVFRVYTSN QEFETVRLNE TLSSFSDDNK ITIRLGRALK KGEYRVKVCQ LLVNEQEPCK
FLLDAVFAKG MTVRQSKEEL IPQLREQCGL DLSIDRFRLR KKTWKNPGTV FLDYHIYEED
INISSNWEVF LEVLDGVEKM KSMSQLAILT RRWRPAEMKL DPFQELVLES NSVDELREKL
SEISGIPLED IEFAKGRGTF PCDISVLDIH QDLDWNPKVS TLNVWPLYIC DDGAVIFYRD
RTEEVMELTD EQRNELMKKE SSRLQKTGHR VTYSPRKEKA LKIYLDGAPN KDVAQD
