RBX1B_ARATH
ID RBX1B_ARATH Reviewed; 115 AA.
AC Q9M2B0; Q1PEJ6;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=RING-box protein 1b;
DE AltName: Full=At-Rbx1;2;
DE AltName: Full=RBX1-1;
DE AltName: Full=RBX1b-At;
GN Name=RBX1B; OrderedLocusNames=At3g42830; ORFNames=T21C14.50;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP DISCUSSION OF SEQUENCE.
RX PubMed=12215511; DOI=10.1105/tpc.003178;
RA Gray W.M., Hellmann H., Dharmasiri S., Estelle M.;
RT "Role of the Arabidopsis RING-H2 protein RBX1 in RUB modification and SCF
RT function.";
RL Plant Cell 14:2137-2144(2002).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12381738; DOI=10.1074/jbc.m204254200;
RA Lechner E., Xie D., Grava S., Pigaglio E., Planchais S., Murray J.A.H.,
RA Parmentier Y., Mutterer J., Dubreucq B., Shen W.-H., Genschik P.;
RT "The AtRbx1 protein is part of plant SCF complexes, and its down-regulation
RT causes severe growth and developmental defects.";
RL J. Biol. Chem. 277:50069-50080(2002).
CC -!- FUNCTION: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC ligase complex, which mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins. The SCF complex plays a
CC crucial role in regulating response to auxin and is essential for
CC growth and development. Through the RING-type zinc finger, seems to
CC recruit the E2 ubiquitination enzyme, to the complex and brings it into
CC close proximity to the substrate (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of SCF complexes, which consist of a SKP1-related
CC protein, a cullin, a RBX protein and a F-box protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Not detected in floral buds, stems and roots.
CC {ECO:0000269|PubMed:12381738}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. It coordinates an additional third zinc ion.
CC -!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
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DR EMBL; AL138639; CAB87200.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77754.1; -; Genomic_DNA.
DR EMBL; DQ446722; ABE65984.1; -; mRNA.
DR PIR; T47341; T47341.
DR RefSeq; NP_189869.1; NM_114151.1.
DR AlphaFoldDB; Q9M2B0; -.
DR SMR; Q9M2B0; -.
DR ComplexPortal; CPX-1449; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1A.
DR ComplexPortal; CPX-1450; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1B.
DR ComplexPortal; CPX-1451; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK3.
DR ComplexPortal; CPX-1452; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK4.
DR ComplexPortal; CPX-1453; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK5.
DR ComplexPortal; CPX-1454; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK6.
DR ComplexPortal; CPX-1455; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK7.
DR ComplexPortal; CPX-1456; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK8.
DR ComplexPortal; CPX-1457; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK9.
DR ComplexPortal; CPX-1458; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK10.
DR ComplexPortal; CPX-1459; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK11.
DR ComplexPortal; CPX-1460; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK12.
DR ComplexPortal; CPX-1461; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK13.
DR ComplexPortal; CPX-1462; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK14.
DR ComplexPortal; CPX-1463; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK15.
DR ComplexPortal; CPX-1464; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK16.
DR ComplexPortal; CPX-1465; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK17.
DR ComplexPortal; CPX-1466; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK18.
DR ComplexPortal; CPX-1467; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK19.
DR ComplexPortal; CPX-1468; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK20.
DR ComplexPortal; CPX-1469; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK21.
DR ComplexPortal; CPX-1492; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1A.
DR ComplexPortal; CPX-1493; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1B.
DR ComplexPortal; CPX-1494; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK3.
DR ComplexPortal; CPX-1495; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK4.
DR ComplexPortal; CPX-1496; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK5.
DR ComplexPortal; CPX-1497; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK6.
DR ComplexPortal; CPX-1498; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK7.
DR ComplexPortal; CPX-1499; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK8.
DR ComplexPortal; CPX-1502; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK9.
DR ComplexPortal; CPX-1503; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK10.
DR ComplexPortal; CPX-1504; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK11.
DR ComplexPortal; CPX-1505; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK12.
DR ComplexPortal; CPX-1506; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK13.
DR ComplexPortal; CPX-1507; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK14.
DR ComplexPortal; CPX-1508; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK15.
DR ComplexPortal; CPX-1509; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK16.
DR ComplexPortal; CPX-1510; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK17.
DR ComplexPortal; CPX-1511; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK18.
DR ComplexPortal; CPX-1512; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK19.
DR ComplexPortal; CPX-1513; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK20.
DR ComplexPortal; CPX-1514; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK21.
DR ComplexPortal; CPX-1535; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1A.
DR ComplexPortal; CPX-1536; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1B.
DR ComplexPortal; CPX-1537; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK3.
DR ComplexPortal; CPX-1538; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK4.
DR ComplexPortal; CPX-1539; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK5.
DR ComplexPortal; CPX-1540; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK6.
DR ComplexPortal; CPX-1541; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK7.
DR ComplexPortal; CPX-1542; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK8.
DR ComplexPortal; CPX-1543; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK9.
DR ComplexPortal; CPX-1544; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK10.
DR ComplexPortal; CPX-1545; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK11.
DR ComplexPortal; CPX-1546; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK12.
DR ComplexPortal; CPX-1547; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK13.
DR ComplexPortal; CPX-1548; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK14.
DR ComplexPortal; CPX-1549; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK15.
DR ComplexPortal; CPX-1550; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK16.
DR ComplexPortal; CPX-1551; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK17.
DR ComplexPortal; CPX-1552; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK18.
DR ComplexPortal; CPX-1553; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK19.
DR ComplexPortal; CPX-1554; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK20.
DR ComplexPortal; CPX-1555; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK21.
DR ComplexPortal; CPX-1578; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1A.
DR ComplexPortal; CPX-1579; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1B.
DR ComplexPortal; CPX-1580; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK3.
DR ComplexPortal; CPX-1581; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK4.
DR ComplexPortal; CPX-1582; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK5.
DR ComplexPortal; CPX-1583; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK6.
DR ComplexPortal; CPX-1584; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK7.
DR ComplexPortal; CPX-1585; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK8.
DR ComplexPortal; CPX-1586; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK9.
DR ComplexPortal; CPX-1587; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK10.
DR ComplexPortal; CPX-1588; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK11.
DR ComplexPortal; CPX-1589; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK12.
DR ComplexPortal; CPX-1590; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK13.
DR ComplexPortal; CPX-1591; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK14.
DR ComplexPortal; CPX-1592; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK15.
DR ComplexPortal; CPX-1593; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK16.
DR ComplexPortal; CPX-1594; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK17.
DR ComplexPortal; CPX-1595; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK18.
DR ComplexPortal; CPX-1596; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK19.
DR ComplexPortal; CPX-1597; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK20.
DR ComplexPortal; CPX-1598; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK21.
DR STRING; 3702.AT3G42830.1; -.
DR PaxDb; Q9M2B0; -.
DR PRIDE; Q9M2B0; -.
DR ProteomicsDB; 225978; -.
DR EnsemblPlants; AT3G42830.1; AT3G42830.1; AT3G42830.
DR GeneID; 823327; -.
DR Gramene; AT3G42830.1; AT3G42830.1; AT3G42830.
DR KEGG; ath:AT3G42830; -.
DR Araport; AT3G42830; -.
DR TAIR; locus:2099341; AT3G42830.
DR eggNOG; KOG2930; Eukaryota.
DR HOGENOM; CLU_115512_2_1_1; -.
DR InParanoid; Q9M2B0; -.
DR OMA; TARERYM; -.
DR OrthoDB; 1587140at2759; -.
DR PhylomeDB; Q9M2B0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9M2B0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2B0; baseline and differential.
DR Genevisible; Q9M2B0; AT.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IC:ComplexPortal.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IC:ComplexPortal.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:ComplexPortal.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IC:ComplexPortal.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR Pfam; PF12678; zf-rbx1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..115
FT /note="RING-box protein 1b"
FT /id="PRO_0000056020"
FT ZN_FING 60..107
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
SQ SEQUENCE 115 AA; 12999 MW; 1515E3E417DB1FAF CRC64;
MASLNSDVIM GESSSISVPS SSSKNSKRFE LKKWSAVALW AWDIVVDNCA ICRNHIMDLC
IECLANQASA TSEECTVAWG VCNHAFHFHC ISRWLKTRQV CPLDVCEWEF QKYGH
