IDD10_ARATH
ID IDD10_ARATH Reviewed; 503 AA.
AC Q700D2; Q0WQ14; Q9FYN0; Q9LYX0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Zinc finger protein JACKDAW {ECO:0000303|PubMed:17785527};
DE AltName: Full=ID1-like zinc finger protein 3 {ECO:0000303|Ref.2};
DE AltName: Full=Protein indeterminate-domain 10 {ECO:0000303|PubMed:16784536};
GN Name=JKD {ECO:0000303|PubMed:17785527};
GN Synonyms=IDD10 {ECO:0000303|PubMed:16784536}, IDZ3 {ECO:0000303|Ref.2};
GN OrderedLocusNames=At5g03150 {ECO:0000312|Araport:AT5G03150};
GN ORFNames=F15A17.180 {ECO:0000312|EMBL:CAB86082.1},
GN MOK16.6 {ECO:0000312|EMBL:BAB08375.1};
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 [MRNA].
RX PubMed=15208423; DOI=10.1104/pp.104.042176;
RA Gong W., Shen Y.-P., Ma L.-G., Pan Y., Du Y.-L., Wang D.-H., Yang J.-Y.,
RA Hu L.-D., Liu X.-F., Dong C.-X., Ma L., Chen Y.-H., Yang X.-Y., Gao Y.,
RA Zhu D., Tan X., Mu J.-Y., Zhang D.-B., Liu Y.-L., Dinesh-Kumar S.P., Li Y.,
RA Wang X.-P., Gu H.-Y., Qu L.-J., Bai S.-N., Lu Y.-T., Li J.-Y., Zhao J.-D.,
RA Zuo J., Huang H., Deng X.-W., Zhu Y.-X.;
RT "Genome-wide ORFeome cloning and analysis of Arabidopsis transcription
RT factor genes.";
RL Plant Physiol. 135:773-782(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Dewald M., Fritz J., Merkle T.;
RT "INDETERMINATE1-like genes in Arabidopsis.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-503.
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 [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16784536; DOI=10.1186/1471-2164-7-158;
RA Colasanti J., Tremblay R., Wong A.Y., Coneva V., Kozaki A., Mable B.K.;
RT "The maize INDETERMINATE1 flowering time regulator defines a highly
RT conserved zinc finger protein family in higher plants.";
RL BMC Genomics 7:158-158(2006).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH SHR; SCR; MGP AND ITSELF.
RX PubMed=17785527; DOI=10.1101/gad.440307;
RA Welch D., Hassan H., Blilou I., Immink R., Heidstra R., Scheres B.;
RT "Arabidopsis JACKDAW and MAGPIE zinc finger proteins delimit asymmetric
RT cell division and stabilize tissue boundaries by restricting SHORT-ROOT
RT action.";
RL Genes Dev. 21:2196-2204(2007).
RN [9]
RP FUNCTION.
RX PubMed=20356954; DOI=10.1242/dev.048777;
RA Hassan H., Scheres B., Blilou I.;
RT "JACKDAW controls epidermal patterning in the Arabidopsis root meristem
RT through a non-cell-autonomous mechanism.";
RL Development 137:1523-1529(2010).
RN [10]
RP INTERACTION WITH SIEL.
RX PubMed=21924907; DOI=10.1016/j.cub.2011.08.013;
RA Koizumi K., Wu S., MacRae-Crerar A., Gallagher K.L.;
RT "An essential protein that interacts with endosomes and promotes movement
RT of the SHORT-ROOT transcription factor.";
RL Curr. Biol. 21:1559-1564(2011).
RN [11]
RP FUNCTION, AND INDUCTION.
RX PubMed=21935722; DOI=10.1007/s11103-011-9826-5;
RA Ogasawara H., Kaimi R., Colasanti J., Kozaki A.;
RT "Activity of transcription factor JACKDAW is essential for SHR/SCR-
RT dependent activation of SCARECROW and MAGPIE and is modulated by reciprocal
RT interactions with MAGPIE, SCARECROW and SHORT ROOT.";
RL Plant Mol. Biol. 77:489-499(2011).
RN [12]
RP FUNCTION, AND INTERACTION WITH RGA AND SCL3.
RX PubMed=24821766; DOI=10.1073/pnas.1321669111;
RA Yoshida H., Hirano K., Sato T., Mitsuda N., Nomoto M., Maeo K., Koketsu E.,
RA Mitani R., Kawamura M., Ishiguro S., Tada Y., Ohme-Takagi M., Matsuoka M.,
RA Ueguchi-Tanaka M.;
RT "DELLA protein functions as a transcriptional activator through the DNA
RT binding of the indeterminate domain family proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7861-7866(2014).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25829440; DOI=10.1105/tpc.114.132407;
RA Long Y., Smet W., Cruz-Ramirez A., Castelijns B., de Jonge W.,
RA Maehoenen A.P., Bouchet B.P., Perez G.S., Akhmanova A., Scheres B.,
RA Blilou I.;
RT "Arabidopsis BIRD zinc finger proteins jointly stabilize tissue boundaries
RT by confining the cell fate regulator SHORT-ROOT and contributing to fate
RT specification.";
RL Plant Cell 27:1185-1199(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 155-224 IN COMPLEX WITH ZINC; SCR
RP AND SHR, INTERACTION WITH SCR AND SHR, AND DNA BINDING.
RX PubMed=28211915; DOI=10.1038/nplants.2017.10;
RA Hirano Y., Nakagawa M., Suyama T., Murase K., Shirakawa M., Takayama S.,
RA Sun T.-P., Hakoshima T.;
RT "Structure of the SHR-SCR heterodimer bound to the BIRD/IDD transcriptional
RT factor JKD.";
RL Nat. Plants 3:17010-17010(2017).
CC -!- FUNCTION: Transcription factor that, together with BIB, regulates
CC tissue boundaries and asymmetric cell division by a rapid up-regulation
CC of 'SCARECROW' (SCR), thus controlling the nuclear localization of
CC 'SHORT-ROOT' (SHR) and restricting its action (PubMed:17785527,
CC PubMed:25829440). Binds DNA via its zinc fingers (PubMed:28211915,
CC PubMed:24821766). Recognizes and binds to SCL3 promoter sequence 5'-
CC AGACAA-3' to promotes its expression when in complex with RGA
CC (PubMed:24821766). Confines CYCD6 expression to the cortex-endodermis
CC initial/daughter (CEI/CEID) tissues (PubMed:25829440). Required for
CC radial patterning and stem cell maintenance (PubMed:17785527).
CC Counteracted by 'MAGPIE' (MGP) (PubMed:17785527). Binds to the SCR and
CC MGP promoter sequences (PubMed:21935722). Controls position-dependent
CC signals that regulate epidermal-cell-type patterning (PubMed:20356954).
CC {ECO:0000269|PubMed:17785527, ECO:0000269|PubMed:20356954,
CC ECO:0000269|PubMed:21935722, ECO:0000269|PubMed:24821766,
CC ECO:0000269|PubMed:25829440, ECO:0000269|PubMed:28211915}.
CC -!- SUBUNIT: Interacts with SHR, SCR, MGP and itself (PubMed:17785527,
CC PubMed:28211915). The heterodimer with SHR involves its zinc fingers
CC (PubMed:28211915). Interacts with SIEL (PubMed:21924907). Binds to RGA
CC and SCL3 competitively in the nucleus (PubMed:24821766).
CC {ECO:0000269|PubMed:17785527, ECO:0000269|PubMed:21924907,
CC ECO:0000269|PubMed:24821766, ECO:0000269|PubMed:28211915}.
CC -!- INTERACTION:
CC Q700D2; Q9ZWA6: MGP; NbExp=3; IntAct=EBI-1568562, EBI-1568600;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:17785527, ECO:0000269|PubMed:24821766,
CC ECO:0000269|PubMed:25829440}.
CC -!- TISSUE SPECIFICITY: Expressed in the quiescent center, the ground
CC tissue stem cells and to a lesser extent in mature cortex and
CC endodermis cells. {ECO:0000269|PubMed:17785527}.
CC -!- DEVELOPMENTAL STAGE: Start to accumulate during the 16- to 32-cell
CC stage of embryogenesis. {ECO:0000269|PubMed:17785527}.
CC -!- INDUCTION: Not regulated by SCR and SHR. {ECO:0000269|PubMed:21935722}.
CC -!- DISRUPTION PHENOTYPE: Ectopic divisions in the ground tissue (GT)
CC region leading to an additional layer at the root pole of mature
CC embryos and seedlings and associated with increased numbers of cells in
CC the circumference within each root layer. Impaired SCR expression in
CC the quiescent center (QC). A low level of SHR moves one extra layer
CC outward from the endodermis, correlating with ectopic divisions in the
CC cortex. This phenotype is stronger in the double mutant jkd bib, thus
CC resulting in roots with wider meristems and additional layers between
CC the central stele and the epidermis as well as an increased cell number
CC per layer leading to unclear morphological tissue distinctions; in root
CC meristems, only a dynamic subset of layers expresses SCR, restricted to
CC the stele-adjacent layer at the root pole, and specific to ectopic
CC dividing tissues. In the double mutant, SHR accumulates in the expanded
CC inner vascular tissue and in all surrounding cell layers, including
CC epidermis, with inefficient nuclear retention. The quadruple mutant
CC line jkd mgp nuc scr has short root meristems, lacks endodermis and
CC miss Casparian strip. {ECO:0000269|PubMed:25829440}.
CC -!- MISCELLANEOUS: Early initiation of expression in ground tissue is
CC SHR- and SCR-independent but later maintenance becomes dependent on
CC both.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08375.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB86082.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY568665; AAS79555.1; -; mRNA.
DR EMBL; AJ630493; CAG25866.1; -; mRNA.
DR EMBL; AJ621494; CAF18563.1; -; mRNA.
DR EMBL; AB005240; BAB08375.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL163002; CAB86082.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90561.1; -; Genomic_DNA.
DR EMBL; AK228895; BAF00785.1; -; mRNA.
DR PIR; T48336; T48336.
DR RefSeq; NP_195935.2; NM_120393.6.
DR PDB; 5B3H; X-ray; 2.70 A; C/F=155-224.
DR PDB; 6KPB; X-ray; 2.40 A; B=367-383.
DR PDBsum; 5B3H; -.
DR PDBsum; 6KPB; -.
DR AlphaFoldDB; Q700D2; -.
DR SMR; Q700D2; -.
DR BioGRID; 17195; 2.
DR IntAct; Q700D2; 3.
DR STRING; 3702.AT5G03150.1; -.
DR PaxDb; Q700D2; -.
DR PRIDE; Q700D2; -.
DR ProteomicsDB; 228775; -.
DR EnsemblPlants; AT5G03150.1; AT5G03150.1; AT5G03150.
DR GeneID; 831919; -.
DR Gramene; AT5G03150.1; AT5G03150.1; AT5G03150.
DR KEGG; ath:AT5G03150; -.
DR Araport; AT5G03150; -.
DR TAIR; locus:2143543; AT5G03150.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_014578_3_1_1; -.
DR InParanoid; Q700D2; -.
DR OMA; FFAGPTM; -.
DR OrthoDB; 802357at2759; -.
DR PhylomeDB; Q700D2; -.
DR PRO; PR:Q700D2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q700D2; baseline and differential.
DR Genevisible; Q700D2; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0008356; P:asymmetric cell division; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; IMP:TAIR.
DR GO; GO:0045604; P:regulation of epidermal cell differentiation; IMP:TAIR.
DR GO; GO:0010075; P:regulation of meristem growth; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..503
FT /note="Zinc finger protein JACKDAW"
FT /id="PRO_0000337840"
FT ZN_FING 82..104
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 124..154
FT /note="C2H2-type 2"
FT /evidence="ECO:0000305"
FT ZN_FING 159..182
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 186..209
FT /note="CCHC-type 2; atypical"
FT /evidence="ECO:0000305"
FT REGION 32..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..208
FT /note="SHR-binding"
FT /evidence="ECO:0000269|PubMed:28211915"
FT REGION 301..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 100..107
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 146..153
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 32..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28211915,
FT ECO:0007744|PDB:5B3H"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28211915,
FT ECO:0007744|PDB:5B3H"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28211915,
FT ECO:0007744|PDB:5B3H"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:28211915,
FT ECO:0007744|PDB:5B3H"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28211915,
FT ECO:0007744|PDB:5B3H"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28211915,
FT ECO:0007744|PDB:5B3H"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28211915,
FT ECO:0007744|PDB:5B3H"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28211915,
FT ECO:0007744|PDB:5B3H"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8GYC1"
FT CONFLICT 435
FT /note="H -> R (in Ref. 6; BAF00785)"
FT /evidence="ECO:0000305"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5B3H"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:5B3H"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:5B3H"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:5B3H"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5B3H"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:5B3H"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:6KPB"
SQ SEQUENCE 503 AA; 55201 MW; 49F387E021AB0A97 CRC64;
MQMIPGDPFS ISSSMGGFVH QETHLHHLQQ QIPDLNPNSN PNPNAKPNSS SAKKKRNQPG
TPDPDADVIA LSPTTLMATN RFVCEICNKG FQRDQNLQLH RRGHNLPWKL KQRSKQEVIK
KKVYICPIKT CVHHDASRAL GDLTGIKKHY SRKHGEKKWK CEKCSKKYAV QSDWKAHAKT
CGTREYKCDC GTLFSRKDSF ITHRAFCDAL TEEGARMSSL SNNNPVISTT NLNFGNESNV
MNNPNLPHGF VHRGVHHPDI NAAISQFGLG FGHDLSAMHA QGLSEMVQMA STGNHHLFPS
SSSSLPDFSG HHQFQIPMTS TNPSLTLSSS STSQQTSASL QHQTLKDSSF SPLFSSSSEN
KQNKPLSPMS ATALLQKAAQ MGSTRSNSST APSFFAGPTM TSSSATASPP PRSSSPMMIQ
QQLNNFNTNV LRENHNRAPP PLSGVSTSSV DNNPFQSNRS GLNPAQQMGL TRDFLGVSNE
HHPHQTGRRP FLPQELARFA PLG
