UBS3B_MOUSE
ID UBS3B_MOUSE Reviewed; 638 AA.
AC Q8BGG7; Q3U8Z2; Q8BMW9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Ubiquitin-associated and SH3 domain-containing protein B;
DE EC=3.1.3.48;
DE AltName: Full=Cbl-interacting protein p70;
DE AltName: Full=Suppressor of T-cell receptor signaling 1;
DE Short=STS-1;
DE AltName: Full=T-cell ubiquitin ligand 2;
DE Short=TULA-2;
DE AltName: Full=Tyrosine-protein phosphatase STS1/TULA2;
GN Name=Ubash3b; Synonyms=Sts1;
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).
RC TISSUE=Megakaryocyte;
RA Nagata Y., Oda M., Haruta H., Todokoro K.;
RT "NF-E2 inducible megakaryocyte specific novel gene.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Cerebellum, Dendritic cell, Diencephalon, and Embryo;
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).
RC TISSUE=Embryonic limb;
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 PROTEIN SEQUENCE OF 93-101; 199-215; 403-410; 482-493 AND 495-515,
RP INTERACTION WITH JAK2, AND TISSUE SPECIFICITY.
RX PubMed=12370296; DOI=10.1128/mcb.22.21.7491-7500.2002;
RA Carpino N., Kobayashi R., Zang H., Takahashi Y., Jou S.-T., Feng J.,
RA Nakajima H., Ihle J.N.;
RT "Identification, cDNA cloning, and targeted deletion of p70, a novel,
RT ubiquitously expressed SH3 domain-containing protein.";
RL Mol. Cell. Biol. 22:7491-7500(2002).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14738763; DOI=10.1016/s1074-7613(03)00351-0;
RA Carpino N., Turner S., Mekala D., Takahashi Y., Zang H., Geiger T.L.,
RA Doherty P., Ihle J.N.;
RT "Regulation of ZAP-70 activation and TCR signaling by two related proteins,
RT Sts-1 and Sts-2.";
RL Immunity 20:37-46(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19733910; DOI=10.1016/j.molimm.2009.08.015;
RA Carpino N., Chen Y., Nassar N., Oh H.W.;
RT "The Sts proteins target tyrosine phosphorylated, ubiquitinated proteins
RT within TCR signaling pathways.";
RL Mol. Immunol. 46:3224-3231(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20585042; DOI=10.1182/blood-2010-02-268136;
RA Thomas D.H., Getz T.M., Newman T.N., Dangelmaier C.A., Carpino N.,
RA Kunapuli S.P., Tsygankov A.Y., Daniel J.L.;
RT "A novel histidine tyrosine phosphatase, TULA-2, associates with Syk and
RT negatively regulates GPVI signaling in platelets.";
RL Blood 116:2570-2578(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
RN [9]
RP CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=20670933; DOI=10.1074/jbc.m110.114181;
RA Chen X., Ren L., Kim S., Carpino N., Daniel J.L., Kunapuli S.P.,
RA Tsygankov A.Y., Pei D.;
RT "Determination of the substrate specificity of protein-tyrosine phosphatase
RT TULA-2 and identification of Syk as a TULA-2 substrate.";
RL J. Biol. Chem. 285:31268-31276(2010).
RN [10]
RP INTERACTION WITH ZAP70.
RX PubMed=26903241; DOI=10.1084/jem.20151426;
RA Hu H., Wang H., Xiao Y., Jin J., Chang J.H., Zou Q., Xie X., Cheng X.,
RA Sun S.C.;
RT "Otud7b facilitates T cell activation and inflammatory responses by
RT regulating Zap70 ubiquitination.";
RL J. Exp. Med. 213:399-414(2016).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 373-636 IN COMPLEX WITH SULFATE,
RP SUBUNIT, AND ACTIVE SITE.
RX PubMed=20516590; DOI=10.1107/s1744309110014259;
RA Jakoncic J., Sondgeroth B., Carpino N., Nassar N.;
RT "The 1.35 A resolution structure of the phosphatase domain of the
RT suppressor of T-cell receptor signaling protein in complex with sulfate.";
RL Acta Crystallogr. F 66:643-647(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 373-633, SUBUNIT, FUNCTION,
RP PHOSPHATASE ACTIVITY, AND ACTIVE SITE.
RX PubMed=17679096; DOI=10.1016/j.molcel.2007.06.015;
RA Mikhailik A., Ford B., Keller J., Chen Y., Nassar N., Carpino N.;
RT "A phosphatase activity of Sts-1 contributes to the suppression of TCR
RT signaling.";
RL Mol. Cell 27:486-497(2007).
CC -!- FUNCTION: Interferes with CBL-mediated down-regulation and degradation
CC of receptor-type tyrosine kinases. Promotes accumulation of activated
CC target receptors, such as T-cell receptors and EGFR, on the cell
CC surface. Exhibits tyrosine phosphatase activity toward several
CC substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins
CC that are dually modified by both protein tyrosine phosphorylation and
CC ubiquitination. {ECO:0000269|PubMed:14738763,
CC ECO:0000269|PubMed:17679096, ECO:0000269|PubMed:19733910,
CC ECO:0000269|PubMed:20585042}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:20670933};
CC -!- SUBUNIT: Homodimer (PubMed:20516590, PubMed:17679096). Interacts with
CC JAK2 (in vitro) (PubMed:12370296). Interacts with CBL. Part of a
CC complex containing CBL and activated EGFR. Interacts with ubiquitin and
CC with mono-ubiquitinated proteins (By similarity). Interacts with ZAP70
CC (ubiquitinated form) (PubMed:26903241). {ECO:0000250|UniProtKB:Q8TF42,
CC ECO:0000269|PubMed:12370296, ECO:0000269|PubMed:17679096,
CC ECO:0000269|PubMed:20516590, ECO:0000269|PubMed:26903241}.
CC -!- INTERACTION:
CC Q8BGG7; P43403: ZAP70; Xeno; NbExp=10; IntAct=EBI-8846415, EBI-1211276;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BGG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGG7-2; Sequence=VSP_019716;
CC -!- TISSUE SPECIFICITY: Detected in splenic T-cells and B-cells, total
CC spleen, skeletal muscle, heart, lung, kidney, thymus, brain and liver
CC (at protein level). Highly expressed in brain. Detected in heart,
CC spleen, lung, liver, kidney and testis. {ECO:0000269|PubMed:12370296,
CC ECO:0000269|PubMed:14738763}.
CC -!- DISRUPTION PHENOTYPE: Mice display strikingly elevated levels of
CC tyrosine phosphorylated, ubiquitinated proteins following TCR
CC stimulation. They are prothrombotic and have shorter bleeding times,
CC which is attributed to insufficient SYK dephosphorylation in platelets.
CC {ECO:0000269|PubMed:19733910, ECO:0000269|PubMed:20585042}.
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DR EMBL; AB075602; BAD06450.1; -; mRNA.
DR EMBL; AK013361; BAC25403.1; -; mRNA.
DR EMBL; AK034450; BAC28714.1; -; mRNA.
DR EMBL; AK035764; BAC29178.1; -; mRNA.
DR EMBL; AK133948; BAE21945.1; -; mRNA.
DR EMBL; AK151895; BAE30779.1; -; mRNA.
DR EMBL; AK152013; BAE30875.1; -; mRNA.
DR EMBL; AK154576; BAE32688.1; -; mRNA.
DR EMBL; BC053436; AAH53436.1; -; mRNA.
DR CCDS; CCDS23085.1; -. [Q8BGG7-1]
DR CCDS; CCDS90541.1; -. [Q8BGG7-2]
DR RefSeq; NP_789830.1; NM_176860.5. [Q8BGG7-1]
DR RefSeq; XP_006510700.1; XM_006510637.3.
DR RefSeq; XP_017169101.1; XM_017313612.1. [Q8BGG7-2]
DR PDB; 2H0Q; X-ray; 1.82 A; A/B/C=373-633.
DR PDB; 2IKQ; X-ray; 2.61 A; A/B/M=369-638.
DR PDB; 3MBK; X-ray; 1.35 A; A/B=373-636.
DR PDBsum; 2H0Q; -.
DR PDBsum; 2IKQ; -.
DR PDBsum; 3MBK; -.
DR AlphaFoldDB; Q8BGG7; -.
DR BMRB; Q8BGG7; -.
DR SMR; Q8BGG7; -.
DR BioGRID; 215592; 23.
DR IntAct; Q8BGG7; 4.
DR MINT; Q8BGG7; -.
DR STRING; 10090.ENSMUSP00000043865; -.
DR iPTMnet; Q8BGG7; -.
DR PhosphoSitePlus; Q8BGG7; -.
DR EPD; Q8BGG7; -.
DR MaxQB; Q8BGG7; -.
DR PaxDb; Q8BGG7; -.
DR PeptideAtlas; Q8BGG7; -.
DR PRIDE; Q8BGG7; -.
DR ProteomicsDB; 297716; -. [Q8BGG7-1]
DR ProteomicsDB; 297717; -. [Q8BGG7-2]
DR Antibodypedia; 32801; 145 antibodies from 26 providers.
DR DNASU; 72828; -.
DR Ensembl; ENSMUST00000044155; ENSMUSP00000043865; ENSMUSG00000032020. [Q8BGG7-1]
DR Ensembl; ENSMUST00000151485; ENSMUSP00000116038; ENSMUSG00000032020. [Q8BGG7-2]
DR GeneID; 72828; -.
DR KEGG; mmu:72828; -.
DR UCSC; uc009pag.1; mouse. [Q8BGG7-1]
DR CTD; 84959; -.
DR MGI; MGI:1920078; Ubash3b.
DR VEuPathDB; HostDB:ENSMUSG00000032020; -.
DR eggNOG; KOG3734; Eukaryota.
DR GeneTree; ENSGT00940000156097; -.
DR HOGENOM; CLU_016516_1_0_1; -.
DR InParanoid; Q8BGG7; -.
DR OMA; PNFMGFF; -.
DR OrthoDB; 243749at2759; -.
DR PhylomeDB; Q8BGG7; -.
DR TreeFam; TF313334; -.
DR BioGRID-ORCS; 72828; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Ubash3b; mouse.
DR EvolutionaryTrace; Q8BGG7; -.
DR PRO; PR:Q8BGG7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BGG7; protein.
DR Bgee; ENSMUSG00000032020; Expressed in lumbar dorsal root ganglion and 204 other tissues.
DR ExpressionAtlas; Q8BGG7; baseline and differential.
DR Genevisible; Q8BGG7; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; IDA:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0038065; P:collagen-activated signaling pathway; IMP:MGI.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IMP:MGI.
DR GO; GO:0045779; P:negative regulation of bone resorption; IMP:MGI.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; IMP:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:MGI.
DR GO; GO:0009968; P:negative regulation of signal transduction; IMP:MGI.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:MGI.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:0070527; P:platelet aggregation; IMP:MGI.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:CACAO.
DR GO; GO:0043393; P:regulation of protein binding; IMP:MGI.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IMP:MGI.
DR CDD; cd07067; HP_PGM_like; 1.
DR CDD; cd11936; SH3_UBASH3B; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR035632; UBASH3B_SH3.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome; SH3 domain.
FT CHAIN 1..638
FT /note="Ubiquitin-associated and SH3 domain-containing
FT protein B"
FT /id="PRO_0000245509"
FT DOMAIN 23..65
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 243..308
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 369..638
FT /note="Protein tyrosine phosphatase"
FT ACT_SITE 379
FT ACT_SITE 380
FT /note="Tele-phosphohistidine intermediate"
FT ACT_SITE 565
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF42"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF42"
FT VAR_SEQ 1..122
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019716"
FT CONFLICT 300
FT /note="E -> G (in Ref. 2; BAE30779/BAE30875)"
FT /evidence="ECO:0000305"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 384..388
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 392..395
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 432..447
FT /evidence="ECO:0007829|PDB:3MBK"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 461..473
FT /evidence="ECO:0007829|PDB:3MBK"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:3MBK"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:3MBK"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 506..511
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 535..553
FT /evidence="ECO:0007829|PDB:3MBK"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:2H0Q"
FT STRAND 558..564
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:3MBK"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 584..591
FT /evidence="ECO:0007829|PDB:3MBK"
FT STRAND 599..604
FT /evidence="ECO:0007829|PDB:3MBK"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:3MBK"
FT STRAND 611..614
FT /evidence="ECO:0007829|PDB:3MBK"
FT HELIX 631..635
FT /evidence="ECO:0007829|PDB:3MBK"
SQ SEQUENCE 638 AA; 71443 MW; 9B665F45AF208EF6 CRC64;
MAAREELYSK VTPRRDRLQR PGTVKHGSAL DVLLSMGFPR ARAQKALAST GGRSVQAACD
WLFSHVGDPF LDDPLPREYV LYLRPTGPLA QKLSDFWQQS KQICGKNKAH NIFPHITLCQ
FFMCEDSKVD ALGEALQTTV SRWKCKFSAP LPLELYTSSN FIGLFVKEDS AEVLKKFAAD
FAAEAASKTE VHVEPHKKQL HVTLAYHFQA SHLPTLEKLA QNIDVKLGCD WVATIFSRDI
RFANHETLQV IYPYSPQNDD ELELVPGDFI FMSPMEQTST SEGWIYGTSL TTGCSGLLPE
NYITKADECS TWIFHGSYSI LNTVSSSSLA FGDGALERRQ YEDQGLGETT PLTIICQPMQ
PLRVNSQPGP QKRCLFVCRH GERMDVVFGK YWLSQCFDAK GRYIRTNLNM PHSLPQRSGG
FRDYEKDAPI TVFGCMQARL VGEALLESNT VIDHVYCSPS LRCVQTAHNI LKGLQQDNHL
KIRVEPGLFE WTKWVAGSTL PAWIPPSELA AANLSVDTTY RPHIPVSKLA ISESYDTYIN
RSFQVTKEII SECKSKGNNI LIVAHASSLE ACTCQLQGLS PQNSKDFVQM VRKIPYLGFC
SCEELGETGI WQLTDPPILP LTHGPTGGFN WRETLLQE
