UBP33_MOUSE
ID UBP33_MOUSE Reviewed; 909 AA.
AC Q8R5K2; Q3UP32; Q5FWK0; Q8K0I3; Q99K22;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 33;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 33;
DE AltName: Full=Ubiquitin thioesterase 33;
DE AltName: Full=Ubiquitin-specific-processing protease 33;
DE AltName: Full=VHL-interacting deubiquitinating enzyme 1;
GN Name=Usp33; Synonyms=Vdu1;
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 [MRNA] (ISOFORM 1).
RX PubMed=11739384; DOI=10.1074/jbc.m108269200;
RA Li Z., Na X., Wang D., Schoen S.R., Messing E.M., Wu G.;
RT "Ubiquitination of a novel deubiquitinating enzyme requires direct binding
RT to von Hippel-Lindau tumor suppressor protein.";
RL J. Biol. Chem. 277:4656-4662(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 225-909 (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Eye, and Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-880 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=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 [4]
RP FUNCTION, INTERACTION WITH ROBO1, AND TISSUE SPECIFICITY.
RX PubMed=19684588; DOI=10.1038/nn.2382;
RA Yuasa-Kawada J., Kinoshita-Kawada M., Wu G., Rao Y., Wu J.Y.;
RT "Midline crossing and Slit responsiveness of commissural axons require
RT USP33.";
RL Nat. Neurosci. 12:1087-1089(2009).
RN [5]
RP FUNCTION, AND INTERACTION WITH ROBO1.
RX PubMed=19706539; DOI=10.1073/pnas.0801262106;
RA Yuasa-Kawada J., Kinoshita-Kawada M., Rao Y., Wu J.Y.;
RT "Deubiquitinating enzyme USP33/VDU1 is required for Slit signaling in
RT inhibiting breast cancer cell migration.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14530-14535(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Spleen;
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).
CC -!- FUNCTION: Deubiquitinating enzyme involved in various processes such as
CC centrosome duplication, cellular migration and beta-2 adrenergic
CC receptor/ADRB2 recycling. Involved in regulation of centrosome
CC duplication by mediating deubiquitination of CCP110 in S and G2/M
CC phase, leading to stabilize CCP110 during the period which centrioles
CC duplicate and elongate. Involved in cell migration via its interaction
CC with intracellular domain of ROBO1, leading to regulate the Slit
CC signaling. Plays a role in commissural axon guidance cross the ventral
CC midline of the neural tube in a Slit-dependent manner, possibly by
CC mediating the deubiquitination of ROBO1. Acts as a regulator of G-
CC protein coupled receptor (GPCR) signaling by mediating the
CC deubiquitination of beta-arrestins (ARRB1 and ARRB2) and beta-2
CC adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling
CC and resensitization after prolonged agonist stimulation by
CC constitutively binding ADRB2, mediating deubiquitination of ADRB2 and
CC inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is
CC probably transferred to the translocated beta-arrestins, leading to
CC beta-arrestins deubiquitination and disengagement from ADRB2. This
CC suggests the existence of a dynamic exchange between the ADRB2 and
CC beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid
CC hormone regulation. Mediates deubiquitination of both 'Lys-48'- and
CC 'Lys-63'-linked polyubiquitin chains. {ECO:0000269|PubMed:19684588,
CC ECO:0000269|PubMed:19706539}.
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 VHL, leading to its ubiquitination and
CC subsequent degradation (By similarity). Interacts with ARRB1 and ARRB2
CC (By similarity). Interacts with ADRB2 (By similarity). Interacts with
CC DIO2 (By similarity). Interacts with SELENBP1; in a selenium-dependent
CC manner (By similarity). Interacts with CCP110 (By similarity).
CC Interacts with ROBO1 (PubMed:19684588, PubMed:19706539). Interacts with
CC ADRB2 (By similarity). {ECO:0000250|UniProtKB:Q8TEY7,
CC ECO:0000269|PubMed:19684588, ECO:0000269|PubMed:19706539}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}.
CC Note=Associates with centrosomes predominantly in S and G2 phases but
CC less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R5K2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R5K2-2; Sequence=VSP_038531;
CC -!- TISSUE SPECIFICITY: Present in 9.5 and 11.5 dpc commissural neurons (at
CC protein level). {ECO:0000269|PubMed:19684588}.
CC -!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions. However, it does
CC not bind ubiquitin, probably because the conserved Arg in position 55
CC is replaced by a Glu residue (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal
CC degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05506.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH89315.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF383174; AAL78316.1; -; mRNA.
DR EMBL; BC005506; AAH05506.1; ALT_INIT; mRNA.
DR EMBL; BC031366; AAH31366.1; -; mRNA.
DR EMBL; BC089315; AAH89315.1; ALT_INIT; mRNA.
DR EMBL; AK143844; BAE25565.1; -; mRNA.
DR CCDS; CCDS17918.1; -. [Q8R5K2-1]
DR CCDS; CCDS57261.1; -. [Q8R5K2-2]
DR RefSeq; NP_001239415.1; NM_001252486.1. [Q8R5K2-2]
DR RefSeq; NP_573510.2; NM_133247.3. [Q8R5K2-1]
DR AlphaFoldDB; Q8R5K2; -.
DR BioGRID; 228458; 2.
DR IntAct; Q8R5K2; 1.
DR STRING; 10090.ENSMUSP00000113265; -.
DR MEROPS; C19.037; -.
DR iPTMnet; Q8R5K2; -.
DR PhosphoSitePlus; Q8R5K2; -.
DR EPD; Q8R5K2; -.
DR MaxQB; Q8R5K2; -.
DR PaxDb; Q8R5K2; -.
DR PRIDE; Q8R5K2; -.
DR ProteomicsDB; 298415; -. [Q8R5K2-1]
DR ProteomicsDB; 298416; -. [Q8R5K2-2]
DR Antibodypedia; 33489; 292 antibodies from 31 providers.
DR DNASU; 170822; -.
DR Ensembl; ENSMUST00000117492; ENSMUSP00000113265; ENSMUSG00000025437. [Q8R5K2-2]
DR Ensembl; ENSMUST00000197748; ENSMUSP00000142708; ENSMUSG00000025437. [Q8R5K2-1]
DR GeneID; 170822; -.
DR KEGG; mmu:170822; -.
DR UCSC; uc008rti.2; mouse. [Q8R5K2-1]
DR UCSC; uc008rtj.2; mouse. [Q8R5K2-2]
DR CTD; 23032; -.
DR MGI; MGI:2159711; Usp33.
DR VEuPathDB; HostDB:ENSMUSG00000025437; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000157311; -.
DR InParanoid; Q8R5K2; -.
DR OMA; PSSNCPH; -.
DR OrthoDB; 147564at2759; -.
DR PhylomeDB; Q8R5K2; -.
DR TreeFam; TF352179; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-9010553; Regulation of expression of SLITs and ROBOs.
DR BioGRID-ORCS; 170822; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Usp33; mouse.
DR PRO; PR:Q8R5K2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8R5K2; protein.
DR Bgee; ENSMUSG00000025437; Expressed in retinal neural layer and 261 other tissues.
DR ExpressionAtlas; Q8R5K2; baseline and differential.
DR Genevisible; Q8R5K2; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; ISO:MGI.
DR GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.2230.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF143791; SSF143791; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51283; DUSP; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase;
KW Metal-binding; Phosphoprotein; Protease; Reference proteome; Repeat;
KW Thiol protease; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..909
FT /note="Ubiquitin carboxyl-terminal hydrolase 33"
FT /id="PRO_0000390424"
FT DOMAIN 154..682
FT /note="USP"
FT DOMAIN 684..777
FT /note="DUSP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 785..888
FT /note="DUSP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT ZN_FING 6..109
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 261..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 163
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 640
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEY7"
FT VAR_SEQ 519..526
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038531"
FT CONFLICT 309
FT /note="P -> S (in Ref. 1; AAL78316)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="L -> P (in Ref. 1; AAL78316 and 2; AAH05506)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="I -> V (in Ref. 1; AAL78316 and 2; AAH05506)"
FT /evidence="ECO:0000305"
FT CONFLICT 779
FT /note="T -> S (in Ref. 2; AAH89315)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 909 AA; 102728 MW; F8A2BDA9FBCD633A CRC64;
MTTFRNHCPH LDSVGEITKE DLIQKSLGAC QDCKVRGPNL WACLENRCSY VGCGESQVDH
STIHSQETKH YLTVNLTTLR VWCYACSKEV FLDRKLGTPP SLPHVRQPQQ TQENSVQDFK
IPSNPALKTP MVAVSEDLDI EVEEEDELKA RGLTGLKNIG NTCYMNAALQ ALSNCPPLTQ
FFLDCGGLAR TDKKPAICKS YLKLMTELWH KSRPGSVVPA NLFQGIKTVN PTFRGYSQQD
AQEFLRCLMD LLHEELKEQV MEMEEEPQTL TSEETVEEEK SQSDVDFQSC ESCSSSEKAE
NESGSKGFPE DSNETTMLIQ DEDDLEMAKD WQKEKVCNKI NKANADVELD KDRDTVCETV
DLNSQETVKV QIHGRASESI TDVHLNDLAT SQILPSNESV SPRLSASPPK LGSLWPGLSP
PHKKAQSTSA KRKKQHKKYR SVISDIFDGT VISSVQCLTC DRVSITLETF QDLSLPIPGK
EDLAKLHSSS HPTIVKAGSC GEAYAPQGWI AFFMEYVKRF VVSCVPSWFW GPVVTLQDCL
AAFFARDELK GDNMYSCEKC KKLRNGVKFC KVQKFPEILC IHLKRFRHEL MFSTKISTHV
SFPLEGLDLQ PFLAKDSPAQ IVTYDLLSVI CHHGTASSGH YIAYCRNNLN NLWYEFDDQS
VTEVSESTVQ NAEAYVLFYR KSSEEAQKER RRISNLLNIM EPSLLQFYIS RQWLNKFKTF
AEPGPISNND FLCIHGGIPP RKASYIEDLV LMLPQNIWDN LYSRYGGGPA VNHLYICHTC
QIELEKIEKR RKTELEIFIR LNRAFQEEDS PATFYCISMQ WFREWESFVK GKDGDPPGPI
DNTKIAVTKC GSVMLKQGAD SGQISEETWN FLQSIYGGGP EVILRPPVVH VDPDVLQAEE
KIEVETRSL
