UBP19_MOUSE
ID UBP19_MOUSE Reviewed; 1360 AA.
AC Q3UJD6; Q3TAC9; Q3TUE6; Q6P9T0; Q80TP5; Q80ZW5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 19;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 19;
DE AltName: Full=Ubiquitin thioesterase 19;
DE AltName: Full=Ubiquitin-specific-processing protease 19;
GN Name=Usp19; Synonyms=Kiaa0891;
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] (ISOFORM 2).
RC TISSUE=Fetal 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Kidney, and Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 395-1360 (ISOFORM 2).
RC STRAIN=C57BL/6J; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY
RP 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 [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=21971047; DOI=10.1074/jbc.m111.276824;
RA Ogawa M., Yamaji R., Higashimura Y., Harada N., Ashida H., Nakano Y.,
RA Inui H.;
RT "17beta-estradiol represses myogenic differentiation by increasing
RT ubiquitin-specific peptidase 19 through estrogen receptor alpha.";
RL J. Biol. Chem. 286:41455-41465(2011).
CC -!- FUNCTION: Deubiquitinating enzyme that regulates the degradation of
CC various proteins. Deubiquitinates and prevents proteasomal degradation
CC of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent
CC degradation thereby playing a role in cell proliferation. Involved in
CC decreased protein synthesis in atrophying skeletal muscle. Modulates
CC transcription of major myofibrillar proteins. Also involved in turnover
CC of endoplasmic-reticulum-associated degradation (ERAD) substrates (By
CC similarity). Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2
CC by preventing thier ubiquitination. Required for cells to mount an
CC appropriate response to hypoxia and rescues HIF1A from degradation in a
CC non-catalytic manner. Exhibits a preference towards 'Lys-63'-linked
CC ubiquitin chains (By similarity). Plays an important role in 17 beta-
CC estradiol (E2)-inhibited myogenesis. Decreases the levels of
CC ubiquitinated proteins during skeletal muscle formation and acts to
CC repress myogenesis. {ECO:0000250, ECO:0000269|PubMed:21971047}.
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 and stabilizes RNF123 (By similarity).
CC Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts
CC with HIF1A (via N-terminus) (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q3UJD6-2; O75344: FKBP6; Xeno; NbExp=2; IntAct=EBI-9359023, EBI-744771;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UJD6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UJD6-2; Sequence=VSP_026769, VSP_026770;
CC -!- INDUCTION: Up-regulated by ESR1 in the presence of 17 beta-estradiol
CC (E2). {ECO:0000269|PubMed:21971047}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65678.4; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122396; BAC65678.4; ALT_INIT; mRNA.
DR EMBL; AK146504; BAE27219.1; -; mRNA.
DR EMBL; AK160807; BAE36025.1; -; mRNA.
DR EMBL; AK171942; BAE42739.1; -; mRNA.
DR EMBL; BC046824; AAH46824.1; -; mRNA.
DR EMBL; BC060613; AAH60613.1; -; mRNA.
DR CCDS; CCDS23529.1; -. [Q3UJD6-1]
DR CCDS; CCDS52924.1; -. [Q3UJD6-2]
DR RefSeq; NP_001161843.1; NM_001168371.2.
DR RefSeq; NP_001161844.1; NM_001168372.2. [Q3UJD6-2]
DR RefSeq; NP_001161845.1; NM_001168373.2.
DR RefSeq; NP_082080.3; NM_027804.4. [Q3UJD6-1]
DR RefSeq; NP_663382.2; NM_145407.3.
DR AlphaFoldDB; Q3UJD6; -.
DR SMR; Q3UJD6; -.
DR BioGRID; 214730; 14.
DR IntAct; Q3UJD6; 26.
DR STRING; 10090.ENSMUSP00000006854; -.
DR MEROPS; C19.024; -.
DR iPTMnet; Q3UJD6; -.
DR PhosphoSitePlus; Q3UJD6; -.
DR SwissPalm; Q3UJD6; -.
DR EPD; Q3UJD6; -.
DR MaxQB; Q3UJD6; -.
DR PaxDb; Q3UJD6; -.
DR PeptideAtlas; Q3UJD6; -.
DR PRIDE; Q3UJD6; -.
DR ProteomicsDB; 298097; -. [Q3UJD6-1]
DR ProteomicsDB; 298098; -. [Q3UJD6-2]
DR Antibodypedia; 30419; 184 antibodies from 32 providers.
DR DNASU; 71472; -.
DR Ensembl; ENSMUST00000006854; ENSMUSP00000006854; ENSMUSG00000006676. [Q3UJD6-1]
DR Ensembl; ENSMUST00000085044; ENSMUSP00000082119; ENSMUSG00000006676. [Q3UJD6-2]
DR GeneID; 71472; -.
DR KEGG; mmu:71472; -.
DR UCSC; uc009rpt.2; mouse. [Q3UJD6-1]
DR UCSC; uc009rpv.2; mouse. [Q3UJD6-2]
DR CTD; 10869; -.
DR MGI; MGI:1918722; Usp19.
DR VEuPathDB; HostDB:ENSMUSG00000006676; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000159085; -.
DR InParanoid; Q3UJD6; -.
DR OMA; SVPCWRI; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; Q3UJD6; -.
DR TreeFam; TF106276; -.
DR BRENDA; 3.4.19.12; 3474.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 71472; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Usp19; mouse.
DR PRO; PR:Q3UJD6; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3UJD6; protein.
DR Bgee; ENSMUSG00000006676; Expressed in secondary oocyte and 270 other tissues.
DR ExpressionAtlas; Q3UJD6; baseline and differential.
DR Genevisible; Q3UJD6; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IMP:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:MGI.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; IMP:UniProtKB.
DR GO; GO:0090068; P:positive regulation of cell cycle process; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0050821; P:protein stabilization; IDA:ParkinsonsUK-UCL.
DR GO; GO:1900037; P:regulation of cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:1904292; P:regulation of ERAD pathway; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR Gene3D; 2.60.40.790; -; 2.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
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 InterPro; IPR002893; Znf_MYND.
DR Pfam; PF04969; CS; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF49764; SSF49764; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51203; CS; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Hydrolase; Membrane;
KW Metal-binding; Phosphoprotein; Protease; Reference proteome; Repeat;
KW Thiol protease; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1360
FT /note="Ubiquitin carboxyl-terminal hydrolase 19"
FT /id="PRO_0000295157"
FT TOPO_DOM 1..1333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1334..1354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1355..1360
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 51..140
FT /note="CS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 322..424
FT /note="CS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT DOMAIN 539..1256
FT /note="USP"
FT ZN_FING 833..875
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 548
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 1207
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 833
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 836
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 850
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 853
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 859
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 863
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 871
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 875
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1286..1340
FT /note="ASRIWQELEAEEEMVPEGPGPLGPWGPQDWVGPPPRGPTTPDEGCLRYFVLG
FT TVA -> GLGPGQAPEVAPTRTAPERFAPPVDRPAPTYSNMEEVD (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_026769"
FT VAR_SEQ 1341..1360
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_026770"
FT CONFLICT 140
FT /note="L -> LK (in Ref. 2; BAE42739)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="P -> S (in Ref. 3; AAH60613)"
FT /evidence="ECO:0000305"
FT CONFLICT 430..431
FT /note="Missing (in Ref. 2; BAE42739)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="A -> T (in Ref. 2; BAE42739)"
FT /evidence="ECO:0000305"
FT CONFLICT 1058
FT /note="D -> E (in Ref. 2; BAE42739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1360 AA; 150549 MW; FE9C3020D2CD9AED CRC64;
MSAGASATGP RRGPPGLEEA TSKKKQKDRA NLESKDGDAR RVSLPRKEPT KDELLLDWRQ
SADEVIVKLR VGTGPVRLED VDAAFTDTDC VVRLPDGRQW GGVFFAEIQS SCTKVQARKG
GLLQLVLPKK VPLLTWPSLL KPLGTQELVP GLQCQENGQE LSPIALEPGS EPRRAKQEAR
NQKRAQGRGE VGSGAGPGTQ AGPSAKRAVH LRRGPEGEGS MDGPGPQGDA PSFLSDSATQ
VEAEEKLCAP PMNTQTSLLS SEKSLALLTV EKTVSPRNDP VAPVMVQDRD PEPEQEDQVK
EEMALGADPT ALVEEPESMV NLAFVKNDSY EKGPDSVVVH VYVKEIRRDS SRVLFREQDF
TLIFQTRDGN FLRLHPGCGP HTIFRWQVKL RNLIEPEQCT FCFTASRIDI CLRKRQSQRW
GGLEAPATRG AVGGAKVAVP TGPTPLDSTP PGGGPHPLTG QEEARAVEKE KPKARSEDSG
LDGVVARTPL EHVAPKPDPH LASPKPTCMV PPMPHSPVSG DSVEEDEEEE KKVCLPGFTG
LVNLGNTCFM NSVIQSLSNT RELRDFFHDR SFEAEINYNN PLGTGGRLAI GFAVLLRALW
KGTHQAFQPS KLKAIVASKA SQFTGYAQHD AQEFMAFLLD GLHEDLNRIQ NKPYTETVDS
DGRPDEVVAE EAWQRHKMRN DSFIVDLFQG QYKSKLVCPV CAKVSITFDP FLYLPVPLPQ
KQKVLPIFYF AREPHSKPIK FLVSVSKENS SASEVLDSLS QSVHVKPENL RLAEVIKNRF
HRVFLPSHSL DAVSPTDVLL CFELLSPELA KERVVVLEVQ QRPQVPSIPI SKCAACQRKQ
QSEEEKLKRC TRCYRVGYCN QFCQKTHWPD HKGLCRPENI GYPFLVSVPA SRLTYARLAQ
LLEGYARYSV SVFQPPFQPG RMALESQSPG CTTLLSTSSL EAGDSEREPI QPSELQLVTP
VAEGDTGAHR VWPPADRGPV PSTSGLSSEM LASGPIEGCP LLAGERVSRP EAAVPGYQHS
SESVNTHTPQ FFIYKIDASN REQRLEDKGE TPLELGDDCS LALVWRNNER LQEFVLVASK
ELECAEDPGS AGEAARAGHF TLDQCLNLFT RPEVLAPEEA WYCPQCKQHR EASKQLLLWR
LPNVLIVQLK RFSFRSFIWR DKINDLVEFP VRNLDLSKFC IGQKEEQLPS YDLYAVINHY
GGMIGGHYTA CARLPNDRSS QRSDVGWRLF DDSTVTTVDE SQVVTRYAYV LFYRRRNSPV
ERPPRASHSE HHPDLGPAAE AAASQASRIW QELEAEEEMV PEGPGPLGPW GPQDWVGPPP
RGPTTPDEGC LRYFVLGTVA ALVALVLNVF YPLVSQSRWR
