ZNRF3_MOUSE
ID ZNRF3_MOUSE Reviewed; 913 AA.
AC Q5SSZ7; B2RXA5; Q3V095;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=E3 ubiquitin-protein ligase ZNRF3;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase ZNRF3;
DE AltName: Full=Zinc/RING finger protein 3;
DE Flags: Precursor;
GN Name=Znrf3;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22575959; DOI=10.1038/nature11019;
RA Hao H.X., Xie Y., Zhang Y., Charlat O., Oster E., Avello M., Lei H.,
RA Mickanin C., Liu D., Ruffner H., Mao X., Ma Q., Zamponi R., Bouwmeester T.,
RA Finan P.M., Kirschner M.W., Porter J.A., Serluca F.C., Cong F.;
RT "ZNRF3 promotes Wnt receptor turnover in an R-spondin-sensitive manner.";
RL Nature 485:195-200(2012).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22895187; DOI=10.1038/nature11308;
RA Koo B.K., Spit M., Jordens I., Low T.Y., Stange D.E., van de Wetering M.,
RA van Es J.H., Mohammed S., Heck A.J., Maurice M.M., Clevers H.;
RT "Tumour suppressor RNF43 is a stem-cell E3 ligase that induces endocytosis
RT of Wnt receptors.";
RL Nature 488:665-669(2012).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=29769720; DOI=10.1038/s41586-018-0118-y;
RA Szenker-Ravi E., Altunoglu U., Leushacke M., Bosso-Lefevre C., Khatoo M.,
RA Thi Tran H., Naert T., Noelanders R., Hajamohideen A., Beneteau C.,
RA de Sousa S.B., Karaman B., Latypova X., Basaran S., Yuecel E.B., Tan T.T.,
RA Vlaminck L., Nayak S.S., Shukla A., Girisha K.M., Le Caignec C.,
RA Soshnikova N., Uyguner Z.O., Vleminckx K., Barker N., Kayserili H.,
RA Reversade B.;
RT "RSPO2 inhibition of RNF43 and ZNRF3 governs limb development independently
RT of LGR4/5/6.";
RL Nature 557:564-569(2018).
RN [7]
RP INTERACTION WITH LMBR1L.
RX PubMed=31073040; DOI=10.1126/science.aau0812;
RA Choi J.H., Zhong X., McAlpine W., Liao T.C., Zhang D., Fang B., Russell J.,
RA Ludwig S., Nair-Gill E., Zhang Z., Wang K.W., Misawa T., Zhan X., Choi M.,
RA Wang T., Li X., Tang M., Sun Q., Yu L., Murray A.R., Moresco E.M.Y.,
RA Beutler B.;
RT "LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling.";
RL Science 364:0-0(2019).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as a negative regulator
CC of the Wnt signaling pathway by mediating the ubiquitination and
CC subsequent degradation of Wnt receptor complex components Frizzled and
CC LRP6. Acts on both canonical and non-canonical Wnt signaling pathway.
CC Acts as a tumor suppressor in the intestinal stem cell zone by
CC inhibiting the Wnt signaling pathway, thereby resticting the size of
CC the intestinal stem cell zone (PubMed:22575959, PubMed:22895187). Along
CC with RSPO2 and RNF43, constitutes a master switch that governs limb
CC specification (By similarity). {ECO:0000250|UniProtKB:Q08D68,
CC ECO:0000269|PubMed:22575959, ECO:0000269|PubMed:22895187}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- ACTIVITY REGULATION: Negatively regulated by R-spondin proteins such as
CC RSPO1: interaction with RSPO1 induces the indirect association between
CC ZNRF3 and LGR4, promoting membrane clearance of ZNRF3. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with LRP6, FZD4, FZD5, FZD6 and FZD8 (By
CC similarity). Interacts with RSPO1; interaction promotes indirect
CC interaction with LGR4 and membrane clearance of ZNRF3 (By similarity).
CC Interacts with LMBR1L (PubMed:31073040). {ECO:0000250|UniProtKB:Q9ULT6,
CC ECO:0000269|PubMed:31073040}.
CC -!- INTERACTION:
CC Q5SSZ7; Q2MKA7: RSPO1; Xeno; NbExp=3; IntAct=EBI-21993315, EBI-10045219;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ULT6};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SSZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SSZ7-2; Sequence=VSP_023089, VSP_023090, VSP_023091;
CC -!- DEVELOPMENTAL STAGE: During limb development, at 14.5 dpc, ubiquitously
CC expressed in the limb bud. In developing lungs, at 14.5 dpc,
CC ubiquitously expressed. {ECO:0000269|PubMed:29769720}.
CC -!- DISRUPTION PHENOTYPE: Embryos die around birth due to activation of Wnt
CC signaling pathway. Embryos display a lack of lens formation due to Wnt
CC activation. Conditional knockout mice lacking both Rnf43 and Znrf3 in
CC intestine show a marked expansion of the proliferative compartment,
CC resembling the effects of acute deletion of Apc.
CC {ECO:0000269|PubMed:22575959, ECO:0000269|PubMed:22895187}.
CC -!- SIMILARITY: Belongs to the ZNRF3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI51081.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI51084.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK133342; BAE21609.1; -; mRNA.
DR EMBL; AL662853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151080; AAI51081.1; ALT_INIT; mRNA.
DR EMBL; BC151083; AAI51084.1; ALT_INIT; mRNA.
DR CCDS; CCDS36102.1; -. [Q5SSZ7-1]
DR CCDS; CCDS70134.1; -. [Q5SSZ7-2]
DR RefSeq; NP_001074393.1; NM_001080924.2. [Q5SSZ7-1]
DR RefSeq; NP_001277430.1; NM_001290501.1. [Q5SSZ7-2]
DR PDB; 4C86; X-ray; 2.00 A; A/B=53-205.
DR PDB; 4C8A; X-ray; 2.70 A; A/B/C=53-205.
DR PDB; 4C8C; X-ray; 2.40 A; A/B=53-205.
DR PDB; 4C8F; X-ray; 2.69 A; A/B/C/D=53-205.
DR PDB; 4C8P; X-ray; 2.10 A; A=53-205.
DR PDB; 4C99; X-ray; 2.80 A; A/C=53-205.
DR PDB; 4C9A; X-ray; 2.40 A; A/C=53-205.
DR PDB; 4C9E; X-ray; 3.00 A; A/C/E/G=53-205.
DR PDB; 4CDJ; X-ray; 1.50 A; A/B=53-205.
DR PDB; 4CDK; X-ray; 2.80 A; A/B/C/D=53-205.
DR PDB; 4UFS; X-ray; 4.80 A; C=53-205.
DR PDBsum; 4C86; -.
DR PDBsum; 4C8A; -.
DR PDBsum; 4C8C; -.
DR PDBsum; 4C8F; -.
DR PDBsum; 4C8P; -.
DR PDBsum; 4C99; -.
DR PDBsum; 4C9A; -.
DR PDBsum; 4C9E; -.
DR PDBsum; 4CDJ; -.
DR PDBsum; 4CDK; -.
DR PDBsum; 4UFS; -.
DR AlphaFoldDB; Q5SSZ7; -.
DR SMR; Q5SSZ7; -.
DR BioGRID; 240468; 6.
DR CORUM; Q5SSZ7; -.
DR IntAct; Q5SSZ7; 2.
DR STRING; 10090.ENSMUSP00000105493; -.
DR iPTMnet; Q5SSZ7; -.
DR PhosphoSitePlus; Q5SSZ7; -.
DR MaxQB; Q5SSZ7; -.
DR PaxDb; Q5SSZ7; -.
DR PRIDE; Q5SSZ7; -.
DR ProteomicsDB; 275305; -. [Q5SSZ7-1]
DR ProteomicsDB; 275306; -. [Q5SSZ7-2]
DR Antibodypedia; 48546; 84 antibodies from 14 providers.
DR Ensembl; ENSMUST00000109867; ENSMUSP00000105493; ENSMUSG00000041961. [Q5SSZ7-1]
DR Ensembl; ENSMUST00000172492; ENSMUSP00000134698; ENSMUSG00000041961. [Q5SSZ7-2]
DR GeneID; 407821; -.
DR KEGG; mmu:407821; -.
DR UCSC; uc007hwj.2; mouse. [Q5SSZ7-1]
DR UCSC; uc007hwk.4; mouse. [Q5SSZ7-2]
DR CTD; 84133; -.
DR MGI; MGI:3039616; Znrf3.
DR VEuPathDB; HostDB:ENSMUSG00000041961; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000154006; -.
DR HOGENOM; CLU_018099_1_0_1; -.
DR InParanoid; Q5SSZ7; -.
DR OMA; CGPTGGE; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q5SSZ7; -.
DR TreeFam; TF317074; -.
DR Reactome; R-MMU-4641263; Regulation of FZD by ubiquitination.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 407821; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Znrf3; mouse.
DR PRO; PR:Q5SSZ7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SSZ7; protein.
DR Bgee; ENSMUSG00000041961; Expressed in otolith organ and 191 other tissues.
DR ExpressionAtlas; Q5SSZ7; baseline and differential.
DR Genevisible; Q5SSZ7; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005109; F:frizzled binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0060173; P:limb development; ISS:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:2000051; P:negative regulation of non-canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:2000095; P:regulation of Wnt signaling pathway, planar cell polarity pathway; IMP:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0038018; P:Wnt receptor catabolic process; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd16799; RING-H2_ZNRF3; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR040700; ZNRF-3_ecto.
DR InterPro; IPR045903; ZNRF3_Znf_RING.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF18212; ZNRF_3_ecto; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Developmental protein;
KW Membrane; Metal-binding; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Wnt signaling pathway; Zinc; Zinc-finger.
FT SIGNAL 1..52
FT /evidence="ECO:0000255"
FT CHAIN 53..913
FT /note="E3 ubiquitin-protein ligase ZNRF3"
FT /id="PRO_0000277807"
FT TOPO_DOM 53..216
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..913
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ZN_FING 290..331
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023089"
FT VAR_SEQ 97
FT /note="Q -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023090"
FT VAR_SEQ 903..913
FT /note="PGSGPGIGTGA -> ENR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023091"
FT CONFLICT 683
FT /note="G -> W (in Ref. 1; BAE21609)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="S -> T (in Ref. 3; AAI51084/AAI51081)"
FT /evidence="ECO:0000305"
FT CONFLICT 798
FT /note="S -> T (in Ref. 3; AAI51084/AAI51081)"
FT /evidence="ECO:0000305"
FT CONFLICT 903..905
FT /note="PGS -> ENR (in Ref. 3; AAI51084/AAI51081)"
FT /evidence="ECO:0000305"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:4CDJ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4C8A"
FT STRAND 72..82
FT /evidence="ECO:0007829|PDB:4CDJ"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:4CDJ"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:4CDJ"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:4CDJ"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4C86"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:4CDJ"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:4CDJ"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:4C86"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:4CDJ"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:4CDJ"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:4CDJ"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:4C86"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:4C86"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:4CDJ"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:4CDJ"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:4CDJ"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:4CDJ"
SQ SEQUENCE 913 AA; 98967 MW; D57C8EF69AAE5C0F CRC64;
MRPRSGGRPG APGRRRRRLR RGPRGRRLPP PPPLPLLLGL LLAAAGPGAA RAKETAFVEV
VLFESSPSGD YTTHTTGLTG RFSRAGAMLS AEGEIVQMHP LGLCNNNDEE DLYEYGWVGV
VKLEQPELDP KPCLTVLGKA KRAVQRGATA VIFDVSENPE AIDQLNQGSE DPLKRPVVYV
KGADAIKLMN IVNKQKVARA RIQHLPPRQP TEYFDMGIFL AFFVVVSLVC LILLVKIKLK
QRRSQNSMNR LAVQALEKME TRKFNSKSKG RREGSCGALD TLSSGSTSDC AICLEKYIDG
EELRVIPCTH RFHRKCVDPW LLQHHTCPHC RHNIIEQKGN PGAVCVETSN LTRGRQPRVT
LPVHYPGRVH RTNAIPAYPT RTSMDSHGNP VTLLTMDRHG EQNLYSPQTP TYVRGYPPLH
LDHTLAPHRC SLEHRAYSPA HPFRRPKFSS RSFSKAACFS QYETMYQHYY FQGLSYPEQE
GQTIPSVTPR GQSRAFPPSG ASSLLFPTMV HVAPPTHVES GSTSSFSCYH GHRSVCSGYL
ADCPGSDSSS NSSGQCRCSS SDSVVDCTEV SNQGVYGSCS TFRSSLSSDY DPFIYRSRGP
AVHLEGSPPP EELPAGHSQS AGRGEPWLGP ASPSGDQLST CSLEMNYSSN SSLEPRGPNS
STSEVGLEVS PGAALDLRRT WKGGPEGPSC ACCFEPQPFP PGSGIETSAG GSSLFLGPRL
LEDCNPPSGE PQLGSSQGLY GLHSDHYPRT DGVKYEGLPC CFYEEKQVAH SAGRGNGCYT
EDYSVSVQYT LTEEPPPSCY AGPRDLSQRI PIIPEDVDCD LGLPQDCHGM HNHSPWGGAL
SLDVPRLHWS LGTTREEEQA PCYQAEVQPG CSPEEAGASR ASLSSAPQDT QESHALAAEA
SGPGSGPGIG TGA
