DDB1A_ARATH
ID DDB1A_ARATH Reviewed; 1088 AA.
AC Q9M0V3; Q0WL42; Q8VY31;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=DNA damage-binding protein 1a {ECO:0000303|PubMed:12225661};
DE AltName: Full=UV-damaged DNA-binding protein 1a {ECO:0000303|PubMed:12225661};
DE Short=DDB1a {ECO:0000303|PubMed:12225661};
GN Name=DDB1A {ECO:0000303|PubMed:12225661};
GN OrderedLocusNames=At4g05420 {ECO:0000312|Araport:AT4G05420};
GN ORFNames=C6L9.100 {ECO:0000312|EMBL:CAB81084.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-1088.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH DET1.
RX PubMed=12225661; DOI=10.1016/s0960-9822(02)01106-5;
RA Schroeder D.F., Gahrtz M., Maxwell B.B., Cook R.K., Kan J.M., Alonso J.M.,
RA Ecker J.R., Chory J.;
RT "De-etiolated 1 and damaged DNA binding protein 1 interact to regulate
RT Arabidopsis photomorphogenesis.";
RL Curr. Biol. 12:1462-1472(2002).
RN [6]
RP COMPONENT OF CDD COMPLEX WITH COP10 AND DET1.
RX PubMed=15342494; DOI=10.1101/gad.1229504;
RA Yanagawa Y., Sullivan J.A., Komatsu S., Gusmaroli G., Suzuki G., Yin J.,
RA Ishibashi T., Saijo Y., Rubio V., Kimura S., Wang J., Deng X.-W.;
RT "Arabidopsis COP10 forms a complex with DDB1 and DET1 in vivo and enhances
RT the activity of ubiquitin conjugating enzymes.";
RL Genes Dev. 18:2172-2181(2004).
RN [7]
RP INTERACTION WITH CUL4, AND IDENTIFICATION IN THE CUL4-RBX1-CDD E3 LIGASE
RP COMPLEX.
RX PubMed=16844902; DOI=10.1105/tpc.106.043224;
RA Chen H., Shen Y., Tang X., Yu L., Wang J., Guo L., Zhang Y., Zhang H.,
RA Feng S., Strickland E., Zheng N., Deng X.-W.;
RT "Arabidopsis CULLIN4 forms an E3 ubiquitin ligase with RBX1 and the CDD
RT complex in mediating light control of development.";
RL Plant Cell 18:1991-2004(2006).
RN [8]
RP INTERACTION WITH CUL4 AND WITH DDB2.
RX PubMed=16792691; DOI=10.1111/j.1365-313x.2006.02810.x;
RA Bernhardt A., Lechner E., Hano P., Schade V., Dieterle M., Anders M.,
RA Dubin M.J., Benvenuto G., Bowler C., Genschik P., Hellmann H.;
RT "CUL4 associates with DDB1 and DET1 and its downregulation affects diverse
RT aspects of development in Arabidopsis thaliana.";
RL Plant J. 47:591-603(2006).
RN [9]
RP COMPONENT OF THE UV-DDB COMPLEX.
RX PubMed=17409070; DOI=10.1534/genetics.107.070359;
RA Al Khateeb W.M., Schroeder D.F.;
RT "DDB2, DDB1A and DET1 exhibit complex interactions during Arabidopsis
RT development.";
RL Genetics 176:231-242(2007).
RN [10]
RP FUNCTION, INTERACTION WITH CUL4 AND DDB2, AND SUBCELLULAR LOCATION.
RX PubMed=18551167; DOI=10.1371/journal.pgen.1000093;
RA Molinier J., Lechner E., Dumbliauskas E., Genschik P.;
RT "Regulation and role of Arabidopsis CUL4-DDB1A-DDB2 in maintaining genome
RT integrity upon UV stress.";
RL PLoS Genet. 4:E1000093-E1000093(2008).
RN [11]
RP INTERACTION WITH PRL1 AND RAE1, AND COMPONENT OF THE CUL4-RBX1-DDB1-PRL1
RP COMPLEX.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [12]
RP INTERACTION WITH ATCSA-1.
RX PubMed=20128879; DOI=10.1111/j.1365-313x.2010.04157.x;
RA Biedermann S., Hellmann H.;
RT "The DDB1a interacting proteins ATCSA-1 and DDB2 are critical factors for
RT UV-B tolerance and genomic integrity in Arabidopsis thaliana.";
RL Plant J. 62:404-415(2010).
RN [13]
RP INTERACTION WITH KTN80.2/DWA3.
RC STRAIN=cv. Columbia;
RX PubMed=21421380; DOI=10.1016/j.plantsci.2010.10.008;
RA Lee J.-H., Terzaghi W., Deng X.W.;
RT "DWA3, an Arabidopsis DWD protein, acts as a negative regulator in ABA
RT signal transduction.";
RL Plant Sci. 180:352-357(2011).
RN [14]
RP INTERACTION WITH WDR55.
RX PubMed=22447688; DOI=10.1105/tpc.111.089425;
RA Bjerkan K.N., Jung-Romeo S., Jurgens G., Genschik P., Grini P.E.;
RT "Arabidopsis WD repeat domain55 Interacts with DNA damaged binding protein1
RT and is required for apical patterning in the embryo.";
RL Plant Cell 24:1013-1033(2012).
RN [15]
RP INTERACTION WITH HTD1.
RX PubMed=25358503; DOI=10.14348/molcells.2014.0224;
RA Kim S.-H., Lee J.-H., Seo K.-I., Ryu B., Sung Y., Chung T., Deng X.W.,
RA Lee J.-H.;
RT "Characterization of a novel DWD protein that participates in heat stress
RT response in Arabidopsis.";
RL Mol. Cells 37:833-840(2014).
RN [16]
RP IDENTIFICATION IN CDD COMPLEX WITH COP10 AND DET1, AND INTERACTION WITH
RP DDA1.
RX PubMed=24563205; DOI=10.1105/tpc.113.122234;
RA Irigoyen M.L., Iniesto E., Rodriguez L., Puga M.I., Yanagawa Y., Pick E.,
RA Strickland E., Paz-Ares J., Wei N., De Jaeger G., Rodriguez P.L.,
RA Deng X.W., Rubio V.;
RT "Targeted degradation of abscisic acid receptors is mediated by the
RT ubiquitin ligase substrate adaptor DDA1 in Arabidopsis.";
RL Plant Cell 26:712-728(2014).
RN [17]
RP INTERACTION WITH DHU1.
RC STRAIN=cv. Columbia;
RX PubMed=25193399; DOI=10.1007/s11103-014-0247-0;
RA Kim S.-H., Kim H., Seo K.-I., Kim S.-H., Chung S., Huang X., Yang P.,
RA Deng X.W., Lee J.-H.;
RT "DWD HYPERSENSITIVE TO UV-B 1 is negatively involved in UV-B mediated
RT cellular responses in Arabidopsis.";
RL Plant Mol. Biol. 86:571-583(2014).
RN [18]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ASG2.
RC STRAIN=cv. Columbia;
RX PubMed=26147561; DOI=10.1111/pce.12605;
RA Dutilleul C., Ribeiro I., Blanc N., Nezames C.D., Deng X.W., Zglobicki P.,
RA Palacio Barrera A.M., Atehortua L., Courtois M., Labas V.,
RA Giglioli-Guivarc'h N., Ducos E.;
RT "ASG2 is a farnesylated DWD protein that acts as ABA negative regulator in
RT Arabidopsis.";
RL Plant Cell Environ. 39:185-198(2016).
CC -!- FUNCTION: Component of light signal transduction machinery. Involved in
CC repression of photomorphogenesis in darkness by participating in the
CC CDD complex, a complex probably required to regulate the activity of
CC ubiquitin conjugating enzymes (E2s). Repression of photomorphogenesis
CC is probably mediated by ubiquitination and subsequent degradation of
CC photomorphogenesis-promoting factors such as HY5, HYH and LAF1. Plays a
CC role in DNA repair by forming with DDB2 the UV-damaged DNA-binding
CC protein complex (UV-DDB). Component of the CUL4-RBX1-DDB1-PRL1 E3
CC ubiquitin-protein ligase complex. {ECO:0000269|PubMed:18551167}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the CDD complex, at least composed of COP10, DET1
CC and DDB1A (PubMed:15342494, PubMed:24563205). Component of the CUL4-
CC RBX1-CDD complex (PubMed:16844902). Component of the CUL4-RBX1-DDB1-
CC PRL1 E3 ubiquitin-protein ligase complex (PubMed:18223036). Component
CC of the UV-DDB complex, which is composed of DDB1A and DDB2
CC (PubMed:17409070). Interacts with RAE1 (PubMed:16844902,
CC PubMed:18223036). Interacts with WDR55 (PubMed:22447688). Interacts
CC with ATCSA-1 (PubMed:20128879). Interacts with DDA1 (PubMed:24563205).
CC Binds to ASG2; the subcellular localization of this complex depends on
CC ASG2 farnesylation status (PubMed:26147561). Binds to KTN80.2/DWA3
CC (PubMed:21421380). Interacts with HTD1 (PubMed:25358503). Interacts
CC directly with DHU1 (PubMed:25193399). {ECO:0000269|PubMed:15342494,
CC ECO:0000269|PubMed:16844902, ECO:0000269|PubMed:17409070,
CC ECO:0000269|PubMed:18223036, ECO:0000269|PubMed:20128879,
CC ECO:0000269|PubMed:21421380, ECO:0000269|PubMed:22447688,
CC ECO:0000269|PubMed:24563205, ECO:0000269|PubMed:25193399,
CC ECO:0000269|PubMed:25358503, ECO:0000269|PubMed:26147561}.
CC -!- INTERACTION:
CC Q9M0V3; Q8H177: At1g65030; NbExp=2; IntAct=EBI-1632780, EBI-1632868;
CC Q9M0V3; Q9LJD7: COP10; NbExp=5; IntAct=EBI-1632780, EBI-2429853;
CC Q9M0V3; Q8LGH4: CUL4; NbExp=11; IntAct=EBI-1632780, EBI-541750;
CC Q9M0V3; Q9M086: DCAF1; NbExp=6; IntAct=EBI-1632780, EBI-2429941;
CC Q9M0V3; Q9M1E5: F9K21.200; NbExp=2; IntAct=EBI-1632780, EBI-1632891;
CC Q9M0V3; O22469: MSI3; NbExp=2; IntAct=EBI-1632780, EBI-1632794;
CC Q9M0V3; O22607: MSI4; NbExp=2; IntAct=EBI-1632780, EBI-9661079;
CC Q9M0V3; Q8L4M1: THO6; NbExp=2; IntAct=EBI-1632780, EBI-941035;
CC Q9M0V3; Q9SZQ5: VIP3; NbExp=2; IntAct=EBI-1632780, EBI-1632819;
CC Q9M0V3-1; Q6NQ88: DDB2; NbExp=2; IntAct=EBI-8565056, EBI-2028926;
CC Q9M0V3-1; O22467: MSI1; NbExp=3; IntAct=EBI-8565056, EBI-632891;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18551167,
CC ECO:0000269|PubMed:26147561}. Nucleus {ECO:0000269|PubMed:18551167,
CC ECO:0000269|PubMed:26147561}. Note=Translocates to the nucleus upon
CC exposure to UV (PubMed:18551167). Excluded from the nucleus when in
CC complex with farnesylated ASG2 (PubMed:26147561).
CC {ECO:0000269|PubMed:18551167, ECO:0000269|PubMed:26147561}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M0V3-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
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DR EMBL; AL161503; CAB81084.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82517.1; -; Genomic_DNA.
DR EMBL; AY074257; AAL66955.1; -; mRNA.
DR EMBL; BT001905; AAN71904.1; -; mRNA.
DR EMBL; AK230366; BAF02165.1; -; mRNA.
DR PIR; B85068; B85068.
DR RefSeq; NP_192451.1; NM_116781.3. [Q9M0V3-1]
DR AlphaFoldDB; Q9M0V3; -.
DR SMR; Q9M0V3; -.
DR BioGRID; 11201; 72.
DR DIP; DIP-40455N; -.
DR IntAct; Q9M0V3; 23.
DR MINT; Q9M0V3; -.
DR STRING; 3702.AT4G05420.1; -.
DR iPTMnet; Q9M0V3; -.
DR PaxDb; Q9M0V3; -.
DR PRIDE; Q9M0V3; -.
DR ProteomicsDB; 224042; -. [Q9M0V3-1]
DR EnsemblPlants; AT4G05420.1; AT4G05420.1; AT4G05420. [Q9M0V3-1]
DR GeneID; 825890; -.
DR Gramene; AT4G05420.1; AT4G05420.1; AT4G05420. [Q9M0V3-1]
DR KEGG; ath:AT4G05420; -.
DR Araport; AT4G05420; -.
DR TAIR; locus:2115909; AT4G05420.
DR eggNOG; KOG1897; Eukaryota.
DR HOGENOM; CLU_002893_0_1_1; -.
DR InParanoid; Q9M0V3; -.
DR OMA; CTEMEHE; -.
DR PhylomeDB; Q9M0V3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9M0V3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0V3; baseline and differential.
DR Genevisible; Q9M0V3; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IPI:TAIR.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IPI:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA damage; DNA repair; DNA-binding;
KW Nucleus; Phytochrome signaling pathway; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..1088
FT /note="DNA damage-binding protein 1a"
FT /id="PRO_0000079837"
SQ SEQUENCE 1088 AA; 121306 MW; 79071E5BC62A197E CRC64;
MSSWNYVVTA HKPTSVTHSC VGNFTSPQEL NLIVAKCTRI EIHLLTPQGL QPMLDVPIYG
RIATLELFRP HGEAQDFLFI ATERYKFCVL QWDPESSELI TRAMGDVSDR IGRPTDNGQI
GIIDPDCRLI GLHLYDGLFK VIPFDNKGQL KEAFNIRLEE LQVLDIKFLF GCAKPTIAVL
YQDNKDARHV KTYEVSLKDK DFVEGPWSQN SLDNGADLLI PVPPPLCGVL IIGEETIVYC
SASAFKAIPI RPSITKAYGR VDVDGSRYLL GDHAGMIHLL VITHEKEKVT GLKIELLGET
SIASTISYLD NAVVFVGSSY GDSQLVKLNL HPDAKGSYVE VLERYINLGP IVDFCVVDLE
RQGQGQVVTC SGAFKDGSLR VVRNGIGINE QASVELQGIK GMWSLKSSID EAFDTFLVVS
FISETRILAM NLEDELEETE IEGFLSQVQT LFCHDAVYNQ LVQVTSNSVR LVSSTTRELR
DEWHAPAGFT VNVATANASQ VLLATGGGHL VYLEIGDGKL TEVQHALLEY EVSCLDINPI
GDNPNYSQLA AVGMWTDISV RIFSLPELTL ITKEQLGGEI IPRSVLLCAF EGISYLLCAL
GDGHLLNFQM DTTTGQLKDR KKVSLGTQPI TLRTFSSKSA THVFAASDRP TVIYSSNKKL
LYSNVNLKEV SHMCPFNSAA FPDSLAIARE GELTIGTIDD IQKLHIRTIP LGEHARRICH
QEQTRTFGIC SLGNQSNSEE SEMHFVRLLD DQTFEFMSTY PLDSFEYGCS ILSCSFTEDK
NVYYCVGTAY VLPEENEPTK GRILVFIVED GRLQLIAEKE TKGAVYSLNA FNGKLLAAIN
QKIQLYKWML RDDGTRELQS ECGHHGHILA LYVQTRGDFI VVGDLMKSIS LLLYKHEEGA
IEERARDYNA NWMSAVEILD DDIYLGAENN FNLLTVKKNS EGATDEERGR LEVVGEYHLG
EFVNRFRHGS LVMRLPDSEI GQIPTVIFGT VNGVIGVIAS LPQEQYTFLE KLQSSLRKVI
KGVGGLSHEQ WRSFNNEKRT AEARNFLDGD LIESFLDLSR NKMEDISKSM NVQVEELCKR
VEELTRLH
