CSN1_ARATH
ID CSN1_ARATH Reviewed; 441 AA.
AC P45432; Q8GYL2; Q9C5F0; Q9M2E9; Q9M4G0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=COP9 signalosome complex subunit 1;
DE Short=CSN complex subunit 1;
DE AltName: Full=Constitutive photomorphogenesis protein 11;
DE AltName: Full=Protein FUSCA 6;
GN Name=CSN1; Synonyms=COP11, FUS6; OrderedLocusNames=At3g61140;
GN ORFNames=T20K12.40;
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 [GENOMIC DNA].
RC STRAIN=cv. Wassilewskija; TISSUE=Silique;
RX PubMed=8130643; DOI=10.2307/3869672;
RA Castle L.A., Meinke D.W.;
RT "A FUSCA gene of Arabidopsis encodes a novel protein essential for plant
RT development.";
RL Plant Cell 6:25-41(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CSN7.
RC STRAIN=cv. Columbia;
RX PubMed=11742986; DOI=10.1093/emboj/20.24.7096;
RA Fu H., Reis N., Lee Y., Glickman M.H., Vierstra R.;
RT "Subunit interaction maps for the regulatory particle of the 26S proteasome
RT and the COP9 signalosome.";
RL EMBO J. 20:7096-7107(2001).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130.
RX PubMed=10809443; DOI=10.1023/a:1006368316413;
RA Tavares R., Aubourg S., Lecharny A., Kreis M.;
RT "Organization and structural evolution of four multigene families in
RT Arabidopsis thaliana: AtLCAD, AtLGT, AtMYST and AtHD-GL2.";
RL Plant Mol. Biol. 42:703-717(2000).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND COMPONENT OF THE CSN COMPLEX WITH CSN8.
RX PubMed=8689678; DOI=10.1016/s0092-8674(00)80082-3;
RA Chamovitz D.A., Wei N., Osterlund M.T., von Arnim A.G., Staub J.M.,
RA Matsui M., Deng X.-W.;
RT "The COP9 complex, a novel multisubunit nuclear regulator involved in light
RT control of a plant developmental switch.";
RL Cell 86:115-121(1996).
RN [9]
RP SUBCELLULAR LOCATION, AND COMPONENT OF THE CSN COMPLEX WITH CSN8.
RX PubMed=8953769; DOI=10.2307/3870411;
RA Staub J.M., Wei N., Deng X.-W.;
RT "Evidence for FUS6 as a component of the nuclear-localized COP9 complex in
RT Arabidopsis.";
RL Plant Cell 8:2047-2056(1996).
RN [10]
RP INTERACTION WITH TIF3C1.
RX PubMed=9849901; DOI=10.1016/s0014-5793(98)01367-2;
RA Karniol B., Yahalom A., Kwok S., Tsuge T., Matsui M., Deng X.-W.,
RA Chamovitz D.A.;
RT "The Arabidopsis homologue of an eIF3 complex subunit associates with the
RT COP9 complex.";
RL FEBS Lett. 439:173-179(1998).
RN [11]
RP INTERACTION WITH RPN6.
RX PubMed=9878390; DOI=10.1006/jmbi.1998.2315;
RA Kwok S.F., Staub J.M., Deng X.-W.;
RT "Characterization of two subunits of Arabidopsis 19S proteasome regulatory
RT complex and its possible interaction with the COP9 complex.";
RL J. Mol. Biol. 285:85-95(1999).
RN [12]
RP FUNCTION.
RX PubMed=11337587; DOI=10.1126/science.1059776;
RA Schwechheimer C., Serino G., Callis J., Crosby W.L., Lyapina S.,
RA Deshaies R.J., Gray W.M., Estelle M., Deng X.-W.;
RT "Interactions of the COP9 signalosome with the E3 ubiquitin ligase
RT SCF(TIR1) in mediating auxin response.";
RL Science 292:1379-1382(2001).
RN [13]
RP DOMAIN, INTERACTION WITH CSN2 AND CSN4, AND MUTANT FUS6-T236.
RX PubMed=11854419; DOI=10.1091/mbc.01-08-0427;
RA Wang X., Kang D., Feng S., Serino G., Schwechheimer C., Wei N.;
RT "CSN1 N-terminal-dependent activity is required for Arabidopsis development
RT but not for Rub1/Nedd8 deconjugation of cullins: a structure-function study
RT of CSN1 subunit of COP9 signalosome.";
RL Mol. Biol. Cell 13:646-655(2002).
RN [14]
RP INTERACTION WITH CSN2; CSN3; CSN4 AND CSN7.
RX PubMed=12615944; DOI=10.1105/tpc.009092;
RA Serino G., Su H., Peng Z., Tsuge T., Wei N., Gu H., Deng X.-W.;
RT "Characterization of the last subunit of the Arabidopsis COP9 signalosome:
RT implications for the overall structure and origin of the complex.";
RL Plant Cell 15:719-731(2003).
RN [15]
RP INTERACTION WITH TIF3H1.
RX PubMed=15548739; DOI=10.1105/tpc.104.026880;
RA Kim T.-H., Kim B.-H., Yahalom A., Chamovitz D.A., von Arnim A.G.;
RT "Translational regulation via 5' mRNA leader sequences revealed by
RT mutational analysis of the Arabidopsis translation initiation factor
RT subunit eIF3h.";
RL Plant Cell 16:3341-3356(2004).
RN [16]
RP INTERACTION WITH CSN7.
RX PubMed=18854373; DOI=10.1105/tpc.107.053801;
RA Dessau M., Halimi Y., Erez T., Chomsky-Hecht O., Chamovitz D.A.,
RA Hirsch J.A.;
RT "The Arabidopsis COP9 signalosome subunit 7 is a model PCI domain protein
RT with subdomains involved in COP9 signalosome assembly.";
RL Plant Cell 20:2815-2834(2008).
RN [17]
RP INTERACTION WITH TIF3E1.
RX PubMed=19704582; DOI=10.4161/psb.3.6.5434;
RA Paz-Aviram T., Yahalom A., Chamovitz D.A.;
RT "Arabidopsis eIF3e interacts with subunits of the ribosome, Cop9
RT signalosome and proteasome.";
RL Plant Signal. Behav. 3:409-411(2008).
RN [18]
RP INTERACTION WITH TSA1.
RX PubMed=22133685; DOI=10.1016/j.jgg.2011.08.007;
RA Li W., Zang B., Liu C., Lu L., Wei N., Cao K., Deng X.W., Wang X.;
RT "TSA1 interacts with CSN1/CSN and may be functionally involved in
RT Arabidopsis seedling development in darkness.";
RL J. Genet. Genomics 38:539-546(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 32-379, INTERACTION WITH CSN7,
RP AND MUTAGENESIS OF PHE-350; MET-358; LEU-373; ILE-377; ARG-385; ASP-387 AND
RP ASN-390.
RX PubMed=23818606; DOI=10.1073/pnas.1302418110;
RA Lee J.H., Yi L., Li J., Schweitzer K., Borgmann M., Naumann M., Wu H.;
RT "Crystal structure and versatile functional roles of the COP9 signalosome
RT subunit 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11845-11850(2013).
CC -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a complex
CC involved in various cellular and developmental processes such as
CC photomorphogenesis and auxin and jasmonate responses. The CSN complex
CC is an essential regulator of the ubiquitin (Ubl) conjugation pathway by
CC mediating the deneddylation of the cullin subunits of SCF-type E3
CC ligase complexes, leading to decrease the Ubl ligase activity of SCF.
CC It is involved in repression of photomorphogenesis in darkness by
CC regulating the activity of COP1-containing Ubl ligase complexes. The
CC complex is also required for degradation of IAA6 by regulating the
CC activity of the Ubl ligase SCF-TIR complex. In the complex, it plays a
CC central role in CSN assembly. {ECO:0000269|PubMed:11337587,
CC ECO:0000269|PubMed:8689678}.
CC -!- SUBUNIT: Component of the CSN complex, probably composed of CSN1, CSN2,
CC CSN3, CSN4, CSN5 (CSN5A or CSN5B), CSN6 (CSN6A or CSN6B), CSN7 and
CC CSN8. Interacts with itself and (via PCI domain) with CSN7 (via PCI
CC domain). In the CSN complex, it probably interacts directly with CSN2,
CC CSN3, CSN4 and CSN5B. Interacts with the 26S proteasome subunit RPN6.
CC Interacts (via N-terminal domain) with TSA1 (via C-terminal domain).
CC Binds to the translation initiation factors TIF3C1, TIF3E1 and TIF3H1
CC (PubMed:9849901, PubMed:19704582, PubMed:15548739).
CC {ECO:0000269|PubMed:11742986, ECO:0000269|PubMed:11854419,
CC ECO:0000269|PubMed:12615944, ECO:0000269|PubMed:15548739,
CC ECO:0000269|PubMed:18854373, ECO:0000269|PubMed:19704582,
CC ECO:0000269|PubMed:22133685, ECO:0000269|PubMed:23818606,
CC ECO:0000269|PubMed:9849901, ECO:0000269|PubMed:9878390}.
CC -!- INTERACTION:
CC P45432; Q8W207: CSN2; NbExp=4; IntAct=EBI-530996, EBI-531035;
CC P45432; Q8W575: CSN3; NbExp=3; IntAct=EBI-530996, EBI-531055;
CC P45432; Q8L5U0: CSN4; NbExp=3; IntAct=EBI-530996, EBI-531074;
CC P45432; Q8LAZ7: CSN5A; NbExp=3; IntAct=EBI-530996, EBI-531132;
CC P45432; Q94JU3: CSN7; NbExp=3; IntAct=EBI-530996, EBI-531152;
CC P45432; P43255: CSN8; NbExp=4; IntAct=EBI-530996, EBI-530981;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flowers, immature siliques,
CC and light-grown roots.
CC -!- DOMAIN: The PCI domain is necessary and sufficient for the interactions
CC with other CSN subunits of the complex. {ECO:0000269|PubMed:11854419}.
CC -!- DOMAIN: The N-terminal part (1-211), which is not required for
CC deneddylating activity and CSN complex formation, is nevertheless
CC essential for other aspects of CSN complex function.
CC {ECO:0000269|PubMed:11854419}.
CC -!- SIMILARITY: Belongs to the CSN1 family. {ECO:0000305}.
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DR EMBL; L26498; AAA32792.1; -; Genomic_DNA.
DR EMBL; AF395057; AAL58100.1; -; mRNA.
DR EMBL; AL137898; CAB71044.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80160.1; -; Genomic_DNA.
DR EMBL; AF360295; AAK26005.1; -; mRNA.
DR EMBL; AK117532; BAC42193.1; -; mRNA.
DR EMBL; AY051056; AAK93733.1; -; mRNA.
DR EMBL; AJ243015; CAB91509.1; -; Genomic_DNA.
DR PIR; T47906; T47906.
DR RefSeq; NP_567109.1; NM_115978.4.
DR PDB; 4LCT; X-ray; 2.70 A; A/B/C/D=32-379.
DR PDBsum; 4LCT; -.
DR AlphaFoldDB; P45432; -.
DR SMR; P45432; -.
DR BioGRID; 10600; 21.
DR IntAct; P45432; 12.
DR STRING; 3702.AT3G61140.1; -.
DR PaxDb; P45432; -.
DR PRIDE; P45432; -.
DR ProteomicsDB; 224427; -.
DR EnsemblPlants; AT3G61140.1; AT3G61140.1; AT3G61140.
DR GeneID; 825286; -.
DR Gramene; AT3G61140.1; AT3G61140.1; AT3G61140.
DR KEGG; ath:AT3G61140; -.
DR Araport; AT3G61140; -.
DR TAIR; locus:2098851; AT3G61140.
DR eggNOG; KOG0686; Eukaryota.
DR HOGENOM; CLU_022348_1_0_1; -.
DR InParanoid; P45432; -.
DR OMA; QNWAHVM; -.
DR OrthoDB; 859626at2759; -.
DR PhylomeDB; P45432; -.
DR PRO; PR:P45432; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P45432; baseline and differential.
DR Genevisible; P45432; AT.
DR GO; GO:0008180; C:COP9 signalosome; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006972; P:hyperosmotic response; IEP:TAIR.
DR GO; GO:0000338; P:protein deneddylation; IMP:TAIR.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0009646; P:response to absence of light; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR019585; Rpn7/CSN1.
DR InterPro; IPR045135; Rpn7_N.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR14145; PTHR14145; 1.
DR Pfam; PF01399; PCI; 1.
DR Pfam; PF10602; RPN7; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Nucleus;
KW Phytochrome signaling pathway; Reference proteome; Signalosome.
FT CHAIN 1..441
FT /note="COP9 signalosome complex subunit 1"
FT /id="PRO_0000120965"
FT DOMAIN 230..400
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 222
FT /note="G->R: In fus6-T236; abolishes the interaction with
FT CSN2 and CSN4."
FT MUTAGEN 350
FT /note="F->A: Abolishes the interaction with CSN7."
FT /evidence="ECO:0000269|PubMed:23818606"
FT MUTAGEN 358
FT /note="M->Q: No effect on the interaction with CSN7."
FT /evidence="ECO:0000269|PubMed:23818606"
FT MUTAGEN 373
FT /note="L->D: Abolishes the interaction with CSN7."
FT /evidence="ECO:0000269|PubMed:23818606"
FT MUTAGEN 377
FT /note="I->D: No effect on the interaction with CSN7."
FT /evidence="ECO:0000269|PubMed:23818606"
FT MUTAGEN 385
FT /note="R->D: No effect on the interaction with CSN7."
FT /evidence="ECO:0000269|PubMed:23818606"
FT MUTAGEN 387
FT /note="D->L: Strongly reduced interaction with CSN7."
FT /evidence="ECO:0000269|PubMed:23818606"
FT MUTAGEN 390
FT /note="N->A: No effect on the interaction with CSN7."
FT /evidence="ECO:0000269|PubMed:23818606"
FT CONFLICT 4
FT /note="D -> G (in Ref. 5; BAC42193)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="S -> G (in Ref. 1; AAA32792)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="L -> F (in Ref. 5; BAC42193)"
FT /evidence="ECO:0000305"
FT CONFLICT 277..279
FT /note="QKV -> AF (in Ref. 3; CAB71044)"
FT /evidence="ECO:0000305"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:4LCT"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 105..131
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 135..152
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 172..188
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 211..227
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:4LCT"
FT TURN 246..252
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 255..269
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 307..322
FT /evidence="ECO:0007829|PDB:4LCT"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 331..347
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:4LCT"
FT HELIX 366..378
FT /evidence="ECO:0007829|PDB:4LCT"
SQ SEQUENCE 441 AA; 50579 MW; C2A980E744B23A90 CRC64;
MERDEEASGP MMEMCTNGGE ETSNRRPIIS GEPLDIEAYA ALYKGRTKIM RLLFIANHCG
GNHALQFDAL RMAYDEIKKG ENTQLFREVV NKIGNRLGEK YGMDLAWCEA VDRRAEQKKV
KLENELSSYR TNLIKESIRM GYNDFGDFYY ACGMLGDAFK NYIRTRDYCT TTKHIIHMCM
NAILVSIEMG QFTHVTSYVN KAEQNPETLE PMVNAKLRCA SGLAHLELKK YKLAARKFLD
VNPELGNSYN EVIAPQDIAT YGGLCALASF DRSELKQKVI DNINFRNFLE LVPDVRELIN
DFYSSRYASC LEYLASLKSN LLLDIHLHDH VDTLYDQIRK KALIQYTLPF VSVDLSRMAD
AFKTSVSGLE KELEALITDN QIQARIDSHN KILYARHADQ RNATFQKVLQ MGNEFDRDVR
AMLLRANLLK HEYHARSARK L
