OTUD4_MOUSE
ID OTUD4_MOUSE Reviewed; 1107 AA.
AC B2RRE7; B7ZNI5; Q80TL3; Q9CUN2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=OTU domain-containing protein 4 {ECO:0000250|UniProtKB:Q01804};
DE EC=3.4.19.12 {ECO:0000305|PubMed:29395066};
GN Name=Otud4 {ECO:0000312|EMBL:AAI38374.1, ECO:0000312|MGI:MGI:1098801};
GN Synonyms=Kiaa1046 {ECO:0000303|PubMed:12693553,
GN ECO:0000312|EMBL:BAC65711.1};
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].
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-1107.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 930-1107.
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-438, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000; SER-1005; SER-1016 AND
RP SER-1017, AND IDENTIFICATION BY 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-1016 AND SER-1017, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442; SER-1000; SER-1005;
RP SER-1016 AND SER-1017, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH MYD88, PHOSPHORYLATION AT
RP SER-202, ACTIVE SITE, MUTAGENESIS OF CYS-45, DISRUPTION PHENOTYPE, AND
RP ACTIVITY REGULATION.
RC TISSUE=Bone marrow macrophage, and Embryonic fibroblast;
RX PubMed=29395066; DOI=10.1016/j.molcel.2018.01.009;
RA Zhao Y., Mudge M.C., Soll J.M., Rodrigues R.B., Byrum A.K.,
RA Schwarzkopf E.A., Bradstreet T.R., Gygi S.P., Edelson B.T.,
RA Mosammaparast N.;
RT "OTUD4 Is a Phospho-Activated K63 Deubiquitinase that Regulates MyD88-
RT Dependent Signaling.";
RL Mol. Cell 69:505-516(2018).
CC -!- FUNCTION: Deubiquitinase which hydrolyzes the isopeptide bond between
CC the ubiquitin C-terminus and the lysine epsilon-amino group of the
CC target protein. May negatively regulate inflammatory and pathogen
CC recognition signaling in innate immune response. Upon phosphorylation
CC at Ser-202 and Ser-204 residues, via IL-1 receptor and Toll-like
CC receptor signaling pathway, specifically deubiquitinates 'Lys-63'-
CC polyubiquitinated MYD88 adapter protein triggering down-regulation of
CC NF-kappa-B-dependent transcription of inflammatory mediators
CC (PubMed:29395066). Independently of the catalytic activity, acts as a
CC scaffold for alternative deubiquitinases to assemble specific
CC deubiquitinase-substrate complexes. Associates with USP7 and USP9X
CC deubiquitinases to stabilize alkylation repair enzyme ALKBH3, thereby
CC promoting the repair of alkylated DNA lesions (By similarity).
CC {ECO:0000250|UniProtKB:Q01804, ECO:0000269|PubMed:29395066}.
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:0000305|PubMed:29395066};
CC -!- ACTIVITY REGULATION: Phosphorylation on Ser-202 and Ser-204 induces
CC 'Lys-63'-specific deubiquitinase activity.
CC {ECO:0000305|PubMed:29395066}.
CC -!- SUBUNIT: Interacts with MYD88; the interaction is direct
CC (PubMed:29395066). Interacts with ALKBH3; the interaction is direct.
CC Interacts with USP7; the interaction is direct. Interacts with USP9X;
CC the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:Q01804, ECO:0000269|PubMed:29395066}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q01804}. Nucleus
CC {ECO:0000250|UniProtKB:Q01804}. Note=Primarily cytoplasmic.
CC {ECO:0000250|UniProtKB:Q01804}.
CC -!- PTM: Phosphorylation at Ser-202 and Ser-204 activates 'Lys-63'-specific
CC deubiquitinase activity. Induced upon stimulation with IL1B.
CC {ECO:0000305|PubMed:29395066}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at sub-Mendelian rate.
CC {ECO:0000269|PubMed:29395066}.
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DR EMBL; BC138373; AAI38374.1; -; mRNA.
DR EMBL; BC145259; AAI45260.1; -; mRNA.
DR EMBL; AK122429; BAC65711.1; -; mRNA.
DR EMBL; AK015275; BAB29777.1; -; mRNA.
DR CCDS; CCDS57625.1; -.
DR RefSeq; NP_001074633.1; NM_001081164.1.
DR RefSeq; NP_001242962.1; NM_001256033.1.
DR AlphaFoldDB; B2RRE7; -.
DR SMR; B2RRE7; -.
DR BioGRID; 216375; 9.
DR IntAct; B2RRE7; 4.
DR MINT; B2RRE7; -.
DR STRING; 10090.ENSMUSP00000133939; -.
DR MEROPS; C85.002; -.
DR iPTMnet; B2RRE7; -.
DR PhosphoSitePlus; B2RRE7; -.
DR SwissPalm; B2RRE7; -.
DR EPD; B2RRE7; -.
DR jPOST; B2RRE7; -.
DR MaxQB; B2RRE7; -.
DR PaxDb; B2RRE7; -.
DR PeptideAtlas; B2RRE7; -.
DR PRIDE; B2RRE7; -.
DR ProteomicsDB; 294406; -.
DR Antibodypedia; 27452; 194 antibodies from 32 providers.
DR Ensembl; ENSMUST00000173078; ENSMUSP00000133939; ENSMUSG00000036990.
DR GeneID; 73945; -.
DR KEGG; mmu:73945; -.
DR UCSC; uc009mir.1; mouse.
DR CTD; 54726; -.
DR MGI; MGI:1098801; Otud4.
DR VEuPathDB; HostDB:ENSMUSG00000036990; -.
DR eggNOG; KOG2605; Eukaryota.
DR GeneTree; ENSGT00940000160512; -.
DR HOGENOM; CLU_291170_0_0_1; -.
DR InParanoid; B2RRE7; -.
DR OMA; IYREPNA; -.
DR OrthoDB; 222767at2759; -.
DR PhylomeDB; B2RRE7; -.
DR TreeFam; TF326812; -.
DR BioGRID-ORCS; 73945; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Otud4; mouse.
DR PRO; PR:B2RRE7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; B2RRE7; protein.
DR Bgee; ENSMUSG00000036990; Expressed in otic placode and 252 other tissues.
DR ExpressionAtlas; B2RRE7; baseline and differential.
DR Genevisible; B2RRE7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:1901537; P:positive regulation of DNA demethylation; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:1903093; P:regulation of protein K48-linked deubiquitination; ISS:UniProtKB.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Immunity; Innate immunity; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1107
FT /note="OTU domain-containing protein 4"
FT /id="PRO_0000394458"
FT DOMAIN 34..155
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 39..45
FT /note="Cys-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 94..104
FT /note="Variable-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 143..148
FT /note="His-loop"
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT REGION 195..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 42
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT ACT_SITE 45
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:29395066"
FT ACT_SITE 148
FT /evidence="ECO:0000250|UniProtKB:Q5VVQ6"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 120
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 131
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29395066"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 438
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 459
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1005
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1017
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01804"
FT MUTAGEN 45
FT /note="C->A: Abolishes 'Lys-48'- and 'Lys-63'-specific
FT deubiquitinase activity. Impairs 'Lys-63'-specific
FT deubiquitination of TRAF6 substrate."
FT /evidence="ECO:0000269|PubMed:29395066"
FT CONFLICT 290
FT /note="Missing (in Ref. 1; AAI45260)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1107 AA; 123055 MW; 746B6BC8589FA672 CRC64;
MEAAVGAPDG VDQGGVGPLE DETPMDAYLR KLGLYRKLVA KDGSCLFRAV AEQVLHSQSR
HVEVRMACIR YLRENREKFE AFIEGSFEEY LKRLENPQEW VGQVEISALS LMYRKDFVIY
QEPNVSPSHV TENNFPEKVL LCFSNGNHYD IVYPITYKDS SAMCQSLLYE LLYEKVFKTD
VSKIMMGLEA SEVAEESNSE ISDSEDDSCK SKSTAATDVN GFKPSGSENP KNNGNSADLP
LSRKVLKSLN PAVYRNVEYE IWLKSKQAQQ KRDYSIAAGL QYEVGDKCHQ VRLDHNGKLS
NADIHGVHSE NGLVLSEELG KKHTPKNLKP PPPESWNTVS GKKMKKPNSG QNFHSDTDYR
GPKNLNKPIK APSALPPRLQ HPSSGVRQHA FSSHSTGSQS QKSSSEHKNL SRMPSQITRK
PDRERAEDFD HVSRESYYFG LSPEERREKQ AIEESRLLYE IQNRDEQAFP ALSSSSVSQS
PSQNSNACVP RKSSHARDRK GSMRRADAEE RKDKDSLRGH THVDKKPEPS TLEISDDKCT
RVSSPSKSKK ECPSPVEQKP AEHIPLSNPA PLLVSPEVHL TPAVPSLPAT VPAWPSEPTT
FGPTGVPAQI PILSVTQTTG PDAAVSQAHL TPSPVPVSIQ AVNQPLMPLP QTMSLYQDPL
YPGFPCSEKG DRAIAPPYSL CQTGEDLPKD KNILRFFFNL GVKAYSCPMW APHSYLYPLH
QAYMAACRMY PKVPVPVYPQ NTWFQEAPPA QSESDCPCTD AHYSLHPEAS VNGQMPQAEM
GPPAFASPLV IPPSQVSEGH GQLSYQPELE SENPGQLLHA EYEESLSGKN MYPQQSFGPN
PFLGPVPIAP PFFPHVWYGY PFQGFVENPV MRQNIVLPPD DKGELDLPLE NLDLSKECDS
VSAVDEFPDA RVEGAHSLSA ASVSSKHEGR VEQSSQTRKA DIDLASGSSA VEGKGHPPTQ
ILNREREPGS AEPEPKRTIQ SLKEKPEKVK DPKTAADVVS PGANSVDRLQ RPKEESSEDE
NEVSNILRSG RSKQFYNQTY GSRKYKSDWG SSGRGGYQHV RGEESWKGQP NRSRDEGYQY
HRHVRGRPYR GDRRRSGMGD GHRGQHT
