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LHX1_XENLA
ID   LHX1_XENLA              Reviewed;         403 AA.
AC   P29674; Q9PSU2;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=LIM/homeobox protein Lhx1;
DE            Short=LIM homeobox protein 1;
DE   AltName: Full=Homeobox protein Lim-1;
DE            Short=Xlim1;
DE            Short=x-Lhx1;
DE            Short=xLIM-1;
GN   Name=lhx1; Synonyms=lim-1, lim1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND INDUCTION.
RX   PubMed=1347750; DOI=10.1101/gad.6.3.356;
RA   Taira M., Jamrich M., Good P.J., Dawid I.B.;
RT   "The LIM domain-containing homeo box gene Xlim-1 is expressed specifically
RT   in the organizer region of Xenopus gastrula embryos.";
RL   Genes Dev. 6:356-366(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112, AND INDUCTION.
RX   PubMed=9275190; DOI=10.1073/pnas.94.18.9717;
RA   Rebbert M.L., Dawid I.B.;
RT   "Transcriptional regulation of the Xlim-1 gene by activin is mediated by an
RT   element in intron I.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9717-9722(1997).
RN   [3]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=7914163; DOI=10.1242/dev.120.6.1525;
RA   Taira M., Otani H., Jamrich M., Dawid I.B.;
RT   "Expression of the LIM class homeobox gene Xlim-1 in pronephros and CNS
RT   cell lineages of Xenopus embryos is affected by retinoic acid and
RT   exogastrulation.";
RL   Development 120:1525-1536(1994).
RN   [4]
RP   FUNCTION.
RX   PubMed=7990959; DOI=10.1038/372677a0;
RA   Taira M., Otani H., Saint-Jeannet J.P., Dawid I.B.;
RT   "Role of the LIM class homeodomain protein Xlim-1 in neural and muscle
RT   induction by the Spemann organizer in Xenopus.";
RL   Nature 372:677-679(1994).
RN   [5]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=8793615;
RA   Karavanov A.A., Saint-Jeannet J.P., Karavanova I., Taira M., Dawid I.B.;
RT   "The LIM homeodomain protein Lim-1 is widely expressed in neural, neural
RT   crest and mesoderm derivatives in vertebrate development.";
RL   Int. J. Dev. Biol. 40:453-461(1996).
RN   [6]
RP   FUNCTION, INTERACTION WITH LDB1, AND MUTAGENESIS OF CYS-28 AND CYS-88.
RX   PubMed=8918878; DOI=10.1038/384270a0;
RA   Agulnick A.D., Taira M., Breen J.J., Tanaka T., Dawid I.B., Westphal H.;
RT   "Interactions of the LIM-domain-binding factor Ldb1 with LIM homeodomain
RT   proteins.";
RL   Nature 384:270-272(1996).
RN   [7]
RP   FUNCTION, INDUCTION, AND MUTAGENESIS OF ILE-223.
RX   PubMed=9023353; DOI=10.1073/pnas.94.3.895;
RA   Taira M., Saint-Jeannet J.P., Dawid I.B.;
RT   "Role of the Xlim-1 and Xbra genes in anteroposterior patterning of neural
RT   tissue by the head and trunk organizer.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:895-900(1997).
RN   [8]
RP   INTERACTION WITH LDB1, DOMAIN, AND MUTAGENESIS OF CYS-28 AND CYS-88.
RX   PubMed=9468533; DOI=10.1074/jbc.273.8.4712;
RA   Breen J.J., Agulnick A.D., Westphal H., Dawid I.B.;
RT   "Interactions between LIM domains and the LIM domain-binding protein
RT   Ldb1.";
RL   J. Biol. Chem. 273:4712-4717(1998).
RN   [9]
RP   INDUCTION.
RX   PubMed=10068640; DOI=10.1242/dev.126.7.1467;
RA   Sun B.I., Bush S.M., Collins-Racie L.A., LaVallie E.R.,
RA   DiBlasio-Smith E.A., Wolfman N.M., McCoy J.M., Sive H.L.;
RT   "derriere: a TGF-beta family member required for posterior development in
RT   Xenopus.";
RL   Development 126:1467-1482(1999).
RN   [10]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10491256; DOI=10.1006/dbio.1999.9414;
RA   Carroll T.J., Vize P.D.;
RT   "Synergism between Pax-8 and lim-1 in embryonic kidney development.";
RL   Dev. Biol. 214:46-59(1999).
RN   [11]
RP   TISSUE SPECIFICITY.
RX   PubMed=10322628;
RX   DOI=10.1002/(sici)1520-6408(1999)24:3/4<199::aid-dvg3>3.0.co;2-d;
RA   Carroll T.J., Wallingford J.B., Vize P.D.;
RT   "Dynamic patterns of gene expression in the developing pronephros of
RT   Xenopus laevis.";
RL   Dev. Genet. 24:199-207(1999).
RN   [12]
RP   FUNCTION.
RX   PubMed=10913356; DOI=10.1006/bbrc.2000.3178;
RA   Nakano H., Amemiya S., Shiokawa K., Taira M.;
RT   "RNA interference for the organizer-specific gene Xlim-1 in Xenopus
RT   embryos.";
RL   Biochem. Biophys. Res. Commun. 274:434-439(2000).
RN   [13]
RP   FUNCTION.
RX   PubMed=10926781; DOI=10.1006/dbio.2000.9778;
RA   Mochizuki T., Karavanov A.A., Curtiss P.E., Ault K.T., Sugimoto N.,
RA   Watabe T., Shiokawa K., Jamrich M., Cho K.W.Y., Dawid I.B., Taira M.;
RT   "Xlim-1 and LIM domain binding protein 1 cooperate with various
RT   transcription factors in the regulation of the goosecoid promoter.";
RL   Dev. Biol. 224:470-485(2000).
RN   [14]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=11112328; DOI=10.1006/dbio.2000.9951;
RA   Chan T.-C., Takahashi S., Asashima M.;
RT   "A role for Xlim-1 in pronephros development in Xenopus laevis.";
RL   Dev. Biol. 228:256-269(2000).
RN   [15]
RP   DOMAIN, AND MUTAGENESIS OF TYR-278; TYR-281; TYR-285; TYR-286 AND TYR-292.
RX   PubMed=11203702; DOI=10.1006/dbio.2000.9986;
RA   Hiratani I., Mochizuki T., Tochimoto N., Taira M.;
RT   "Functional domains of the LIM homeodomain protein Xlim-1 involved in
RT   negative regulation, transactivation, and axis formation in Xenopus
RT   embryos.";
RL   Dev. Biol. 229:456-467(2001).
RN   [16]
RP   FUNCTION.
RX   PubMed=11291848;
RA   Kodjabachian L., Karavanov A.A., Hikasa H., Hukriede N.A., Aoki T.,
RA   Taira M., Dawid I.B.;
RT   "A study of Xlim1 function in the Spemann-Mangold organizer.";
RL   Int. J. Dev. Biol. 45:209-218(2001).
RN   [17]
RP   TISSUE SPECIFICITY.
RX   PubMed=11567052; DOI=10.1523/jneurosci.21-19-07620.2001;
RA   Bachy I., Vernier P., Retaux S.;
RT   "The LIM-homeodomain gene family in the developing Xenopus brain:
RT   conservation and divergences with the mouse related to the evolution of the
RT   forebrain.";
RL   J. Neurosci. 21:7620-7629(2001).
RN   [18]
RP   FUNCTION.
RX   PubMed=12381786; DOI=10.1073/pnas.212532399;
RA   Chen L., Segal D., Hukriede N.A., Podtelejnikov A.V., Bayarsaihan D.,
RA   Kennison J.A., Ogryzko V.V., Dawid I.B., Westphal H.;
RT   "Ssdp proteins interact with the LIM-domain-binding protein Ldb1 to
RT   regulate development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14320-14325(2002).
RN   [19]
RP   FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH LDB1 AND RNF12.
RX   PubMed=12874135; DOI=10.1242/dev.00621;
RA   Hiratani I., Yamamoto N., Mochizuki T., Ohmori S.-Y., Taira M.;
RT   "Selective degradation of excess Ldb1 by Rnf12/RLIM confers proper Ldb1
RT   expression levels and Xlim-1/Ldb1 stoichiometry in Xenopus organizer
RT   functions.";
RL   Development 130:4161-4175(2003).
RN   [20]
RP   FUNCTION.
RX   PubMed=12710967; DOI=10.1016/s0012-1606(03)00034-4;
RA   Yamamoto S., Hikasa H., Ono H., Taira M.;
RT   "Molecular link in the sequential induction of the Spemann organizer:
RT   direct activation of the cerberus gene by Xlim-1, Xotx2, Mix.1, and
RT   Siamois, immediately downstream from Nodal and Wnt signaling.";
RL   Dev. Biol. 257:190-204(2003).
RN   [21]
RP   FUNCTION.
RX   PubMed=12530965; DOI=10.1016/s1534-5807(02)00398-2;
RA   Hukriede N.A., Tsang T.E., Habas R., Khoo P.L., Steiner K., Weeks D.L.,
RA   Tam P.P., Dawid I.B.;
RT   "Conserved requirement of Lim1 function for cell movements during
RT   gastrulation.";
RL   Dev. Cell 4:83-94(2003).
RN   [22]
RP   TISSUE SPECIFICITY.
RX   PubMed=15024752; DOI=10.1002/cne.20046;
RA   Moreno N., Bachy I., Retaux S., Gonzalez A.;
RT   "LIM-homeodomain genes as developmental and adult genetic markers of
RT   Xenopus forebrain functional subdivisions.";
RL   J. Comp. Neurol. 472:52-72(2004).
RN   [23]
RP   TISSUE SPECIFICITY.
RX   PubMed=15791640; DOI=10.1002/cne.20498;
RA   Moreno N., Bachy I., Retaux S., Gonzalez A.;
RT   "LIM-homeodomain genes as territory markers in the brainstem of adult and
RT   developing Xenopus laevis.";
RL   J. Comp. Neurol. 485:240-254(2005).
CC   -!- FUNCTION: Involved in the establishment of the body plan via the
CC       Spemann organizer during gastrulation. Transcriptional activator
CC       required to induce organizer gene expression downstream of siamois.
CC       Promotes head formation by binding to 5'-TAAT'-3' elements in the
CC       promoters of head organizer genes cer1 and gsc to stimulate expression.
CC       Binds as a complex with siamois and mix-A/mix.1 to the cer1 promoter,
CC       and with ldb1 and otx2 to the gsc promoter. Also involved in neural
CC       induction via the organizer, including a role in notochord formation.
CC       Acts synergistically with ldb1 and ssbp in subsequent axis formation.
CC       Involved in kidney development, acting synergistically with pax8 to
CC       establish the pronephric primordium in late gastrulae/early neurulae
CC       and with pax2 during pronephric morphogenesis in tailbud stages. Has a
CC       later role in mediating the activity of inhibitors of ventralization.
CC       {ECO:0000269|PubMed:10491256, ECO:0000269|PubMed:10913356,
CC       ECO:0000269|PubMed:10926781, ECO:0000269|PubMed:11112328,
CC       ECO:0000269|PubMed:11291848, ECO:0000269|PubMed:12381786,
CC       ECO:0000269|PubMed:12530965, ECO:0000269|PubMed:12710967,
CC       ECO:0000269|PubMed:12874135, ECO:0000269|PubMed:1347750,
CC       ECO:0000269|PubMed:7990959, ECO:0000269|PubMed:8918878,
CC       ECO:0000269|PubMed:9023353}.
CC   -!- SUBUNIT: Interacts with ldb1 via the tandem LIM domains. Both LIM
CC       domains are required for optimal binding and binding relieves the
CC       inhibitory effect of the LIM domains and activates lhx1. Binding to
CC       ldb1 also prevents degradation of ldb1 by rnf12. The stoichiometry of
CC       lhx1 and ldb1 is important for their function and an excess of ldb1 can
CC       inhibit lhx1 function. Interacts with the N-terminal region of rnf12 by
CC       a homeobox-dependent mechanism. {ECO:0000269|PubMed:12874135,
CC       ECO:0000269|PubMed:8918878, ECO:0000269|PubMed:9468533}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC       ECO:0000269|PubMed:8793615}.
CC   -!- TISSUE SPECIFICITY: Exhibits a biphasic expression pattern. Initially
CC       localized to the Spemann organizer region of gastrulae, leading to
CC       expression in prechordal mesoderm and notochord. In the second phase,
CC       expressed in the lateral mesoderm and neural plate, eventually
CC       concentrating in the pronephros and the CNS. Expressed in the
CC       pronephros primordium by late gastrula (stage 12.5) and becomes
CC       restricted to the tips of the tubules and ducts as kidney development
CC       progresses. In the CNS, becomes progressively recognizable in
CC       anatomically distinct structures during larval development. Within the
CC       forebrain, shows almost identical expression to lhx5 in the
CC       diencephalon, being expressed in alternating stripes to lhx2 and lhx9.
CC       Expressed in the diencephalic pretectum within prosomere 1,
CC       hypothalamus, ventral thalamus and zona limitans intrathalamica. In the
CC       telencephalon, the expression pattern is distinct from lhx5, being
CC       localized in the pallium and subpallium. Also expressed in the ventral
CC       territories of midbrain (mesencephalon) and hindbrain
CC       (rhombencephalon), being expressed in the mesencephalic tegmentum and
CC       hindbrain reticular formation. Also shows intense expression in the
CC       cerebellum including Purkinje cells. {ECO:0000269|PubMed:10322628,
CC       ECO:0000269|PubMed:10491256, ECO:0000269|PubMed:11112328,
CC       ECO:0000269|PubMed:11567052, ECO:0000269|PubMed:12874135,
CC       ECO:0000269|PubMed:1347750, ECO:0000269|PubMed:15024752,
CC       ECO:0000269|PubMed:15791640, ECO:0000269|PubMed:7914163,
CC       ECO:0000269|PubMed:8793615}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed at a low level in the unfertilized egg. Expression is highest
CC       at the gastrula stage, then declines before rising again during the
CC       tadpole stage. {ECO:0000269|PubMed:1347750}.
CC   -!- INDUCTION: By retinoic acid and by dorsal mesoderm-inducers including
CC       activin, derriere, dvr1/vg-1 and nodal. {ECO:0000269|PubMed:10068640,
CC       ECO:0000269|PubMed:11112328, ECO:0000269|PubMed:1347750,
CC       ECO:0000269|PubMed:7914163, ECO:0000269|PubMed:9023353,
CC       ECO:0000269|PubMed:9275190}.
CC   -!- DOMAIN: The LIM domains exert a negative regulatory function and
CC       disruption of the LIM domains produces an activated form. In addition,
CC       two activation domains and a negative regulatory domain exist C-
CC       terminally to the homeobox. {ECO:0000269|PubMed:11203702,
CC       ECO:0000269|PubMed:9468533}.
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DR   EMBL; X63889; CAA45353.1; -; mRNA.
DR   EMBL; AF013242; AAB70190.1; -; Genomic_DNA.
DR   PIR; S23802; S23802.
DR   RefSeq; NP_001084128.1; NM_001090659.1.
DR   AlphaFoldDB; P29674; -.
DR   SMR; P29674; -.
DR   GeneID; 399323; -.
DR   KEGG; xla:399323; -.
DR   CTD; 399323; -.
DR   Xenbase; XB-GENE-856460; lhx1.L.
DR   OMA; SPMTETC; -.
DR   OrthoDB; 1070389at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 399323; Expressed in gastrula and 8 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:UniProtKB.
DR   GO; GO:0009798; P:axis specification; IMP:UniProtKB.
DR   GO; GO:0042074; P:cell migration involved in gastrulation; IMP:UniProtKB.
DR   GO; GO:0043009; P:chordate embryonic development; IMP:UniProtKB.
DR   GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
DR   GO; GO:0072080; P:nephron tubule development; IGI:UniProtKB.
DR   GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR   GO; GO:0030903; P:notochord development; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0039003; P:pronephric field specification; IGI:UniProtKB.
DR   GO; GO:0039020; P:pronephric nephron tubule development; IGI:UniProtKB.
DR   GO; GO:0048793; P:pronephros development; IMP:UniProtKB.
DR   GO; GO:0003002; P:regionalization; IMP:UniProtKB.
DR   GO; GO:0035565; P:regulation of pronephros size; IGI:UniProtKB.
DR   GO; GO:0032526; P:response to retinoic acid; TAS:AgBase.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR001781; Znf_LIM.
DR   Pfam; PF00046; Homeodomain; 1.
DR   Pfam; PF00412; LIM; 2.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00132; LIM; 2.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   Activator; Developmental protein; Differentiation; DNA-binding;
KW   Gastrulation; Homeobox; LIM domain; Metal-binding; Neurogenesis; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..403
FT                   /note="LIM/homeobox protein Lhx1"
FT                   /id="PRO_0000075777"
FT   DOMAIN          4..54
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          63..117
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DNA_BIND        179..238
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          130..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         28
FT                   /note="C->G: Disrupts ldb1-binding. Produces an active
FT                   form; when associated with G-88."
FT                   /evidence="ECO:0000269|PubMed:8918878,
FT                   ECO:0000269|PubMed:9468533"
FT   MUTAGEN         88
FT                   /note="C->G: Disrupts ldb1-binding. Produces an active
FT                   form; when associated with G-28."
FT                   /evidence="ECO:0000269|PubMed:8918878,
FT                   ECO:0000269|PubMed:9468533"
FT   MUTAGEN         223
FT                   /note="I->P: Fails to induce chrd."
FT                   /evidence="ECO:0000269|PubMed:9023353"
FT   MUTAGEN         278
FT                   /note="Y->A: Abolishes transcriptional activity and axis-
FT                   inducing activity; when associated with A-281; A-285; A-286
FT                   and A-292."
FT                   /evidence="ECO:0000269|PubMed:11203702"
FT   MUTAGEN         278
FT                   /note="Y->F: No effect on axis-inducing activity; when
FT                   associated with F-281; F-285; F-286 and F-292."
FT                   /evidence="ECO:0000269|PubMed:11203702"
FT   MUTAGEN         281
FT                   /note="Y->A: Abolishes transcriptional activity and axis-
FT                   inducing activity; when associated with A-278; A-285; A-286
FT                   and A-292."
FT                   /evidence="ECO:0000269|PubMed:11203702"
FT   MUTAGEN         281
FT                   /note="Y->F: No effect on axis-inducing activity; when
FT                   associated with F-278; F-285; F-286 and F-292."
FT                   /evidence="ECO:0000269|PubMed:11203702"
FT   MUTAGEN         285
FT                   /note="Y->A: Abolishes transcriptional activity and axis-
FT                   inducing activity; when associated with A-278; A-281; A-286
FT                   and A-292."
FT                   /evidence="ECO:0000269|PubMed:11203702"
FT   MUTAGEN         285
FT                   /note="Y->F: No effect on axis-inducing activity; when
FT                   associated with F-278; F-281; F-286 and F-292."
FT                   /evidence="ECO:0000269|PubMed:11203702"
FT   MUTAGEN         286
FT                   /note="Y->A: Abolishes transcriptional activity and axis-
FT                   inducing activity; when associated with A-278; A-281; A-285
FT                   and A-292."
FT                   /evidence="ECO:0000269|PubMed:11203702"
FT   MUTAGEN         286
FT                   /note="Y->F: No effect on axis-inducing activity; when
FT                   associated with F-278; F-281; F-285 and F-292."
FT                   /evidence="ECO:0000269|PubMed:11203702"
FT   MUTAGEN         292
FT                   /note="Y->A: Abolishes transcriptional activity and axis-
FT                   inducing activity; when associated with A-278; A-281; A-285
FT                   and A-286."
FT                   /evidence="ECO:0000269|PubMed:11203702"
FT   MUTAGEN         292
FT                   /note="Y->F: No effect on axis-inducing activity; when
FT                   associated with F-278; F-281; F-285 and F-286."
FT                   /evidence="ECO:0000269|PubMed:11203702"
SQ   SEQUENCE   403 AA;  44935 MW;  4147EB3A2774C110 CRC64;
     MVHCAGCERP ILDRFLLNVL DRAWHVKCVQ CCECKCNLTE KCFSREGKLY CKNDFFRRFG
     TKCAGCAQGI SPSDLVRRAR SKVFHLNCFT CMMCNKQLST GEELYIIDEN KFVCKEDYLN
     NNNAAKENSF ISVTGSDPSL SPESQDPLQD DAKDSESANV SDKEAGINEN DDQNLGAKRR
     GPRTTIKAKQ LETLKAAFAA TPKPTRHIRE QLAQETGLNM RVIQVWFQNR RSKERRMKQL
     SALGARRHAF FRSPRRMRPL VDRLEPGELI PNGPFAFYGD YQSEYYGPGS NYDFFPQGPP
     SSQAQTPVDL PFVPSSVPAG TPLGAMDHPI PGHHPSSDAQ RFTDIMSHPP GDSPSPEPNL
     PGSMHSMSAE VFGQSPPFSS LSVNGGYGNH LSHPPEMNET AVW
 
 
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