HAT4_ARATH
ID HAT4_ARATH Reviewed; 284 AA.
AC Q05466; A5Y7H1; A5Y7H2; A5Y7H3; A5Y7H4; A5Y7H5; A5Y7H6; A5Y7H7; A5Y7H8;
AC A5Y7H9; A5Y7I0; A5Y7I1; A5Y7I2; A5Y7I3; A5Y7I4; A5Y7I5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 174.
DE RecName: Full=Homeobox-leucine zipper protein HAT4;
DE AltName: Full=HD-ZIP protein ATHB-2;
DE AltName: Full=Homeodomain transcription factor ATHB-2;
DE AltName: Full=Homeodomain-leucine zipper protein HAT4;
DE Short=HD-ZIP protein 4;
GN Name=HAT4; Synonyms=ATHB-2; OrderedLocusNames=At4g16780;
GN ORFNames=dl4415w, FCAALL.101;
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].
RC STRAIN=cv. Columbia;
RX PubMed=1349174; DOI=10.1073/pnas.89.9.3894;
RA Schena M., Davis R.W.;
RT "HD-Zip proteins: members of an Arabidopsis homeodomain protein
RT superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3894-3898(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8449400; DOI=10.1101/gad.7.3.367;
RA Schena M., Lloyd A.M., Davis R.W.;
RT "The HAT4 gene of Arabidopsis encodes a developmental regulator.";
RL Genes Dev. 7:367-379(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=8106086; DOI=10.1046/j.1365-313x.1993.04030469.x;
RA Carabelli M., Sessa G., Baima S., Morelli G., Ruberti I.;
RT "The Arabidopsis Athb-2 and -4 genes are strongly induced by far-red-rich
RT light.";
RL Plant J. 4:469-479(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [5]
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-217, AND VARIANTS PRO-35; ILE-79;
RP VAL-88; TYR-123 AND LYS-162.
RC STRAIN=cv. An-2, cv. Bla-6, cv. Br-0, cv. Bu-2, cv. Columbia, cv. Di-1,
RC cv. Et-0, cv. Kl-1, cv. Li-5:3, cv. Ma-2, cv. Mt-0, cv. Pa-2, cv. Pi-0,
RC cv. Su-0, and cv. Tsu-1;
RX PubMed=17614917; DOI=10.1111/j.1365-294x.2007.03298.x;
RA Brock M.T., Tiffin P., Weinig C.;
RT "Sequence diversity and haplotype associations with phenotypic responses to
RT crowding: GIGANTEA affects fruit set in Arabidopsis thaliana.";
RL Mol. Ecol. 16:3050-3062(2007).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-238.
RC STRAIN=cv. CIBC-10, cv. GB, cv. KNO-1, and cv. NA-A;
RX PubMed=12694288; DOI=10.1046/j.1365-294x.2003.01743.x;
RA Wright S.I., Lauga B., Charlesworth D.;
RT "Subdivision and haplotype structure in natural populations of Arabidopsis
RT lyrata.";
RL Mol. Ecol. 12:1247-1263(2003).
RN [10]
RP DNA-BINDING.
RX PubMed=8253077; DOI=10.1002/j.1460-2075.1993.tb06025.x;
RA Sessa G., Morelli G., Ruberti I.;
RT "The Athb-1 and -2 HD-Zip domains homodimerize forming complexes of
RT different DNA binding specificities.";
RL EMBO J. 12:3507-3517(1993).
RN [11]
RP DNA-BINDING, AND MUTAGENESIS OF VAL-172; ASN-176 AND ARG-180.
RX PubMed=9405140; DOI=10.1006/jmbi.1997.1408;
RA Sessa G., Morelli G., Ruberti I.;
RT "DNA-binding specificity of the homeodomain-leucine zipper domain.";
RL J. Mol. Biol. 274:303-309(1997).
RN [12]
RP FUNCTION.
RX PubMed=10477292; DOI=10.1242/dev.126.19.4235;
RA Steindler C., Matteucci A., Sessa G., Weimar T., Ohgishi M., Aoyama T.,
RA Morelli G., Ruberti I.;
RT "Shade avoidance responses are mediated by the ATHB-2 HD-zip protein, a
RT negative regulator of gene expression.";
RL Development 126:4235-4245(1999).
RN [13]
RP FUNCTION.
RX PubMed=11260495; DOI=10.1046/j.1365-313x.2001.00966.x;
RA Ohgishi M., Oka A., Morelli G., Ruberti I., Aoyama T.;
RT "Negative autoregulation of the Arabidopsis homeobox gene ATHB-2.";
RL Plant J. 25:389-398(2001).
RN [14]
RP GENE FAMILY.
RX PubMed=16055682; DOI=10.1104/pp.105.063461;
RA Henriksson E., Olsson A.S.B., Johannesson H., Johansson H., Hanson J.,
RA Engstroem P., Soederman E.;
RT "Homeodomain leucine zipper class I genes in Arabidopsis. Expression
RT patterns and phylogenetic relationships.";
RL Plant Physiol. 139:509-518(2005).
CC -!- FUNCTION: Probable transcription factor involved in the negative
CC regulation of cell elongation and specific cell proliferation processes
CC such as lateral root formation and secondary growth of the vascular
CC system. Acts as mediator of the red/far-red light effects on leaf cell
CC expansion in the shading response. Binds to the DNA sequence 5'-
CC CAAT[GC]ATTG-3'. Negatively regulates its own expression.
CC {ECO:0000269|PubMed:10477292, ECO:0000269|PubMed:11260495,
CC ECO:0000269|PubMed:8449400}.
CC -!- SUBUNIT: Interacts with DNA as homodimer.
CC -!- INTERACTION:
CC Q05466; Q8GXM7: ATHB-X; NbExp=5; IntAct=EBI-4428728, EBI-3133795;
CC Q05466; Q9SU72: EDS1; NbExp=3; IntAct=EBI-4428728, EBI-1390454;
CC Q05466; P46600: HAT1; NbExp=3; IntAct=EBI-4428728, EBI-15195911;
CC Q05466; P46601: HAT2; NbExp=4; IntAct=EBI-4428728, EBI-4448195;
CC Q05466; P46604: HAT22; NbExp=3; IntAct=EBI-4428728, EBI-4448318;
CC Q05466; P46602: HAT3; NbExp=3; IntAct=EBI-4428728, EBI-4450405;
CC Q05466; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-4428728, EBI-4424877;
CC Q05466; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-4428728, EBI-15192325;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in leaves and stems.
CC {ECO:0000269|PubMed:8106086}.
CC -!- INDUCTION: Rapidly and strongly induced by lowering the ratio of red to
CC far-red light. {ECO:0000269|PubMed:8106086}.
CC -!- SIMILARITY: Belongs to the HD-ZIP homeobox family. Class II subfamily.
CC {ECO:0000305}.
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DR EMBL; M90394; AAA32815.1; -; mRNA.
DR EMBL; Z19602; CAA79670.1; -; Genomic_DNA.
DR EMBL; X68145; CAA48246.1; -; mRNA.
DR EMBL; X68146; CAA48248.1; -; Genomic_DNA.
DR EMBL; Z97342; CAB10452.1; -; Genomic_DNA.
DR EMBL; AL161544; CAB78720.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83803.1; -; Genomic_DNA.
DR EMBL; AF375453; AAK53037.1; -; mRNA.
DR EMBL; AY081747; AAL87400.1; -; mRNA.
DR EMBL; EF193551; ABP96504.1; -; Genomic_DNA.
DR EMBL; EF193552; ABP96505.1; -; Genomic_DNA.
DR EMBL; EF193553; ABP96506.1; -; Genomic_DNA.
DR EMBL; EF193554; ABP96507.1; -; Genomic_DNA.
DR EMBL; EF193555; ABP96508.1; -; Genomic_DNA.
DR EMBL; EF193556; ABP96509.1; -; Genomic_DNA.
DR EMBL; EF193557; ABP96510.1; -; Genomic_DNA.
DR EMBL; EF193558; ABP96511.1; -; Genomic_DNA.
DR EMBL; EF193559; ABP96512.1; -; Genomic_DNA.
DR EMBL; EF193560; ABP96513.1; -; Genomic_DNA.
DR EMBL; EF193561; ABP96514.1; -; Genomic_DNA.
DR EMBL; EF193562; ABP96515.1; -; Genomic_DNA.
DR EMBL; EF193563; ABP96516.1; -; Genomic_DNA.
DR EMBL; EF193564; ABP96517.1; -; Genomic_DNA.
DR EMBL; EF193565; ABP96518.1; -; Genomic_DNA.
DR EMBL; AY174653; AAO19435.1; -; Genomic_DNA.
DR EMBL; AY174654; AAO19436.1; -; Genomic_DNA.
DR EMBL; AY174655; AAO19437.1; -; Genomic_DNA.
DR EMBL; AY174656; AAO19438.1; -; Genomic_DNA.
DR PIR; S31424; S31424.
DR RefSeq; NP_193411.1; NM_117780.4.
DR AlphaFoldDB; Q05466; -.
DR SMR; Q05466; -.
DR BioGRID; 12677; 34.
DR IntAct; Q05466; 37.
DR STRING; 3702.AT4G16780.1; -.
DR iPTMnet; Q05466; -.
DR PaxDb; Q05466; -.
DR PRIDE; Q05466; -.
DR ProteomicsDB; 247214; -.
DR EnsemblPlants; AT4G16780.1; AT4G16780.1; AT4G16780.
DR GeneID; 827384; -.
DR Gramene; AT4G16780.1; AT4G16780.1; AT4G16780.
DR KEGG; ath:AT4G16780; -.
DR Araport; AT4G16780; -.
DR TAIR; locus:2129136; AT4G16780.
DR eggNOG; KOG0483; Eukaryota.
DR HOGENOM; CLU_049516_2_1_1; -.
DR InParanoid; Q05466; -.
DR OMA; PSCEHVS; -.
DR OrthoDB; 1388148at2759; -.
DR PhylomeDB; Q05466; -.
DR PRO; PR:Q05466; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q05466; baseline and differential.
DR Genevisible; Q05466; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0010311; P:lateral root formation; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0010017; P:red or far-red light signaling pathway; IEP:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IEP:TAIR.
DR GO; GO:0010218; P:response to far red light; IEP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0080191; P:secondary thickening; IMP:TAIR.
DR GO; GO:0009641; P:shade avoidance; IEP:TAIR.
DR GO; GO:0010016; P:shoot system morphogenesis; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR006712; HD-ZIP_N.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR000047; HTH_motif.
DR InterPro; IPR003106; Leu_zip_homeo.
DR Pfam; PF02183; HALZ; 1.
DR Pfam; PF04618; HD-ZIP_N; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00031; HTHREPRESSR.
DR SMART; SM00340; HALZ; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; DNA-binding; Homeobox; Nucleus;
KW Phytochrome signaling pathway; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..284
FT /note="Homeobox-leucine zipper protein HAT4"
FT /id="PRO_0000048901"
FT DNA_BIND 126..185
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 48..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..214
FT /note="Leucine-zipper"
FT COMPBIAS 48..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 35
FT /note="S -> P (in strain: cv. Tsu-1)"
FT /evidence="ECO:0000269|PubMed:17614917"
FT VARIANT 79
FT /note="T -> I (in strain: cv. Kl-1)"
FT /evidence="ECO:0000269|PubMed:17614917"
FT VARIANT 88
FT /note="G -> V (in strain: cv. Bla-6, cv. Bu-2, cv. Di-1 and
FT cv. Pi-0)"
FT /evidence="ECO:0000269|PubMed:17614917"
FT VARIANT 123
FT /note="D -> Y (in strain: cv. Tsu-1)"
FT /evidence="ECO:0000269|PubMed:17614917"
FT VARIANT 162
FT /note="Q -> K (in strain: cv. Bla-6)"
FT /evidence="ECO:0000269|PubMed:17614917"
FT MUTAGEN 172
FT /note="V->A: Abolishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:9405140"
FT MUTAGEN 176
FT /note="N->A: Abolishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:9405140"
FT MUTAGEN 180
FT /note="R->A: Abolishes DNA-binding."
FT /evidence="ECO:0000269|PubMed:9405140"
FT CONFLICT 216
FT /note="A -> V (in Ref. 1; AAA32815 and 2; CAA79670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 31853 MW; 4BBC0D069E9D56F7 CRC64;
MMFEKDDLGL SLGLNFPKKQ INLKSNPSVS VTPSSSSFGL FRRSSWNESF TSSVPNSDSS
QKETRTFIRG IDVNRPPSTA EYGDEDAGVS SPNSTVSSST GKRSEREEDT DPQGSRGISD
DEDGDNSRKK LRLSKDQSAI LEETFKDHST LNPKQKQALA KQLGLRARQV EVWFQNRRAR
TKLKQTEVDC EFLRRCCENL TEENRRLQKE VTELRALKLS PQFYMHMSPP TTLTMCPSCE
HVSVPPPQPQ AATSAHHRSL PVNAWAPATR ISHGLTFDAL RPRS
