VSX2_HUMAN
ID VSX2_HUMAN Reviewed; 361 AA.
AC P58304; A1A4X6;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Visual system homeobox 2;
DE AltName: Full=Ceh-10 homeodomain-containing homolog;
DE AltName: Full=Homeobox protein CHX10;
GN Name=VSX2; Synonyms=CHX10, HOX10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MCOPCTI GLN-200 AND
RP PRO-200.
RX PubMed=10932181; DOI=10.1038/78071;
RA Percin E.F., Ploder L.A., Yu J.J., Arici K., Horsford D.J., Rutherford A.,
RA Bapat B., Cox D.W., Duncan A.M.V., Kalnins V.I., Kocak-Altintas A.,
RA Sowden J.C., Traboulsi E., Sarfarazi M., McInnes R.R.;
RT "Human microphthalmia associated with mutations in the retinal homeobox
RT gene CHX10.";
RL Nat. Genet. 25:397-401(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Shan Y.X., Yu L.;
RT "Cloning and characterization of human CHX10 (Ceh-10 homeodomain containing
RT homolog) gene.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INVOLVEMENT IN MCOPCB3, AND VARIANT MCOP2 TRP-227.
RX PubMed=15257456; DOI=10.1007/s00439-004-1154-2;
RA Bar-Yosef U., Abuelaish I., Harel T., Hendler N., Ofir R., Birk O.S.;
RT "CHX10 mutations cause non-syndromic microphthalmia/ anophthalmia in Arab
RT and Jewish kindreds.";
RL Hum. Genet. 115:302-309(2004).
RN [7]
RP MUTAGENESIS OF ASN-198.
RX PubMed=16236706; DOI=10.1074/jbc.m509470200;
RA Dorval K.M., Bobechko B.P., Fujieda H., Chen S., Zack D.J., Bremner R.;
RT "CHX10 targets a subset of photoreceptor genes.";
RL J. Biol. Chem. 281:744-751(2006).
RN [8]
RP FUNCTION, AND CHARACTERIZATION OF VARIANT MCOPCTI GLN-200.
RX PubMed=17919464; DOI=10.1016/j.brainres.2007.06.007;
RA Clark A.M., Yun S., Veien E.S., Wu Y.Y., Chow R.L., Dorsky R.I.,
RA Levine E.M.;
RT "Negative regulation of Vsx1 by its paralog Chx10/Vsx2 is conserved in the
RT vertebrate retina.";
RL Brain Res. 1192:99-113(2008).
RN [9]
RP VARIANT MCOP2 ALA-223.
RX PubMed=21976963;
RA Reis L.M., Khan A., Kariminejad A., Ebadi F., Tyler R.C., Semina E.V.;
RT "VSX2 mutations in autosomal recessive microphthalmia.";
RL Mol. Vis. 17:2527-2532(2011).
RN [10]
RP VARIANT MCOPCB3 ARG-223.
RX PubMed=24033328; DOI=10.1111/cge.12275;
RA Chassaing N., Causse A., Vigouroux A., Delahaye A., Alessandri J.L.,
RA Boespflug-Tanguy O., Boute-Benejean O., Dollfus H., Duban-Bedu B.,
RA Gilbert-Dussardier B., Giuliano F., Gonzales M., Holder-Espinasse M.,
RA Isidor B., Jacquemont M.L., Lacombe D., Martin-Coignard D.,
RA Mathieu-Dramard M., Odent S., Picone O., Pinson L., Quelin C., Sigaudy S.,
RA Toutain A., Thauvin-Robinet C., Kaplan J., Calvas P.;
RT "Molecular findings and clinical data in a cohort of 150 patients with
RT anophthalmia/microphthalmia.";
RL Clin. Genet. 86:326-334(2014).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF ASN-198.
RX PubMed=27477290; DOI=10.1016/j.celrep.2016.06.100;
RA Clovis Y.M., Seo S.Y., Kwon J.S., Rhee J.C., Yeo S., Lee J.W., Lee S.,
RA Lee S.K.;
RT "Chx10 Consolidates V2a Interneuron Identity through Two Distinct Gene
RT Repression Modes.";
RL Cell Rep. 16:1642-1652(2016).
RN [12]
RP FUNCTION, AND CHARACTERIZATION OF VARIANT MCOPCTI GLN-200.
RX PubMed=27301076; DOI=10.1002/stem.2414;
RA Capowski E.E., Wright L.S., Liang K., Phillips M.J., Wallace K.,
RA Petelinsek A., Hagstrom A., Pinilla I., Borys K., Lien J., Min J.H.,
RA Keles S., Thomson J.A., Gamm D.M.;
RT "Regulation of WNT Signaling by VSX2 During Optic Vesicle Patterning in
RT Human Induced Pluripotent Stem Cells.";
RL Stem Cells 34:2625-2634(2016).
CC -!- FUNCTION: Acts as a transcriptional regulator through binding to DNA at
CC the consensus sequence 5'-[TC]TAATT[AG][AG]-3' upstream of gene
CC promoters (PubMed:27301076). Plays a significant role in the
CC specification and morphogenesis of the sensory retina (By similarity).
CC Mediates differentiation of V2a interneurons by repression of motor
CC neuron gene transcription, via competitively binding to response
CC elements that are activated by the ISL1-LHX3 complex, such as VSX1
CC (PubMed:17919464, PubMed:27477290). Acts as a positive transcriptional
CC regulator of NXNL1; regulation is significantly increased in synergy
CC with VSX1 (By similarity). Acts as a negative transcriptional regulator
CC of MITF (By similarity). Represses SAG transcription by competitive
CC inhibition of ISL1-LHX3 response elements (PubMed:16236706,
CC PubMed:27477290). Binds to the photoreceptor conserved element-1 (PCE-
CC 1) in the promoter of rod photoreceptor arrestin SAG and acts as a
CC transcriptional repressor (By similarity). Plays a significant role in
CC the specification and morphogenesis of the sensory retina (By
CC similarity). Involved in the development of retinal ganglion cells
CC (RGCs) which leads to release of SHH by RGCs, promoting Hedgehog
CC signaling and subsequent proliferation of retinal progenitor cells (By
CC similarity). Participates in the development of the cells of the inner
CC nuclear layer, by promoting postnatal differentiation of bipolar cells
CC with a comparable inhibition of rod cell differentiation (By
CC similarity). May play a role in the maintenance of neural retina
CC identity during development by regulation of canonical Wnt genes and
CC CTNNB1 localization, suggesting a role in the regulation of canonical
CC Wnt signaling (PubMed:27301076). {ECO:0000250|UniProtKB:Q61412,
CC ECO:0000269|PubMed:16236706, ECO:0000269|PubMed:17919464,
CC ECO:0000269|PubMed:27301076, ECO:0000269|PubMed:27477290}.
CC -!- SUBUNIT: Interacts with MITF. {ECO:0000250|UniProtKB:Q61412}.
CC -!- INTERACTION:
CC P58304; Q92870-2: APBB2; NbExp=3; IntAct=EBI-6427899, EBI-21535880;
CC P58304; P46379-2: BAG6; NbExp=3; IntAct=EBI-6427899, EBI-10988864;
CC P58304; Q9NX09: DDIT4; NbExp=3; IntAct=EBI-6427899, EBI-715104;
CC P58304; O14645: DNALI1; NbExp=3; IntAct=EBI-6427899, EBI-395638;
CC P58304; P50570-2: DNM2; NbExp=3; IntAct=EBI-6427899, EBI-10968534;
CC P58304; Q01658: DR1; NbExp=3; IntAct=EBI-6427899, EBI-750300;
CC P58304; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-6427899, EBI-21603100;
CC P58304; P14136: GFAP; NbExp=3; IntAct=EBI-6427899, EBI-744302;
CC P58304; P28799: GRN; NbExp=3; IntAct=EBI-6427899, EBI-747754;
CC P58304; Q00403: GTF2B; NbExp=3; IntAct=EBI-6427899, EBI-389564;
CC P58304; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-6427899, EBI-1054873;
CC P58304; P04792: HSPB1; NbExp=3; IntAct=EBI-6427899, EBI-352682;
CC P58304; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-6427899, EBI-1055254;
CC P58304; O60333-2: KIF1B; NbExp=3; IntAct=EBI-6427899, EBI-10975473;
CC P58304; O14901: KLF11; NbExp=3; IntAct=EBI-6427899, EBI-948266;
CC P58304; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-6427899, EBI-473196;
CC P58304; P19404: NDUFV2; NbExp=3; IntAct=EBI-6427899, EBI-713665;
CC P58304; P07196: NEFL; NbExp=3; IntAct=EBI-6427899, EBI-475646;
CC P58304; P35240-4: NF2; NbExp=3; IntAct=EBI-6427899, EBI-1014514;
CC P58304; P29474: NOS3; NbExp=3; IntAct=EBI-6427899, EBI-1391623;
CC P58304; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-6427899, EBI-2811583;
CC P58304; D3DTS7: PMP22; NbExp=3; IntAct=EBI-6427899, EBI-25882629;
CC P58304; P60891: PRPS1; NbExp=3; IntAct=EBI-6427899, EBI-749195;
CC P58304; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-6427899, EBI-396669;
CC P58304; Q13148: TARDBP; NbExp=6; IntAct=EBI-6427899, EBI-372899;
CC P58304; P02766: TTR; NbExp=3; IntAct=EBI-6427899, EBI-711909;
CC P58304; O76024: WFS1; NbExp=3; IntAct=EBI-6427899, EBI-720609;
CC P58304; Q96BH6; NbExp=3; IntAct=EBI-6427899, EBI-25872486;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61412}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in retinal neuroblasts during
CC eye development and in the inner nuclear layer of the adult retina.
CC Within this layer, expression is stronger in the outer margin where
CC bipolar cells predominate.
CC -!- DISEASE: Microphthalmia, isolated, 2 (MCOP2) [MIM:610093]: A disorder
CC of eye formation, ranging from small size of a single eye to complete
CC bilateral absence of ocular tissues. Ocular abnormalities like
CC opacities of the cornea and lens, scaring of the retina and choroid,
CC and other abnormalities may also be present.
CC {ECO:0000269|PubMed:15257456, ECO:0000269|PubMed:21976963}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Microphthalmia with cataracts and iris abnormalities (MCOPCTI)
CC [MIM:610092]: A disorder of eye formation, ranging from small size of a
CC single eye to complete bilateral absence of ocular tissues. Ocular
CC abnormalities like opacities of the cornea and lens, scaring of the
CC retina and choroid, cataract and other abnormalities like cataract may
CC also be present. {ECO:0000269|PubMed:10932181,
CC ECO:0000269|PubMed:17919464, ECO:0000269|PubMed:27301076}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Microphthalmia, isolated, with coloboma, 3 (MCOPCB3)
CC [MIM:610092]: A disorder of eye formation, ranging from small size of a
CC single eye to complete bilateral absence of ocular tissues. Ocular
CC abnormalities like opacities of the cornea and lens, scaring of the
CC retina and choroid, and other abnormalities may also be present. Ocular
CC colobomas are a set of malformations resulting from abnormal
CC morphogenesis of the optic cup and stalk, and the fusion of the fetal
CC fissure (optic fissure). {ECO:0000269|PubMed:15257456,
CC ECO:0000269|PubMed:24033328}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the paired homeobox family. {ECO:0000305}.
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DR EMBL; AY336059; AAQ01593.1; -; mRNA.
DR EMBL; AC005519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81164.1; -; Genomic_DNA.
DR EMBL; BC128153; AAI28154.1; -; mRNA.
DR CCDS; CCDS9827.1; -.
DR RefSeq; NP_878314.1; NM_182894.2.
DR AlphaFoldDB; P58304; -.
DR SMR; P58304; -.
DR BioGRID; 130813; 14.
DR IntAct; P58304; 40.
DR STRING; 9606.ENSP00000261980; -.
DR iPTMnet; P58304; -.
DR PhosphoSitePlus; P58304; -.
DR BioMuta; VSX2; -.
DR DMDM; 17374365; -.
DR MassIVE; P58304; -.
DR PaxDb; P58304; -.
DR PeptideAtlas; P58304; -.
DR PRIDE; P58304; -.
DR ProteomicsDB; 57058; -.
DR Antibodypedia; 190; 189 antibodies from 32 providers.
DR DNASU; 338917; -.
DR Ensembl; ENST00000261980.3; ENSP00000261980.2; ENSG00000119614.3.
DR GeneID; 338917; -.
DR KEGG; hsa:338917; -.
DR MANE-Select; ENST00000261980.3; ENSP00000261980.2; NM_182894.3; NP_878314.1.
DR UCSC; uc001xpq.3; human.
DR CTD; 338917; -.
DR DisGeNET; 338917; -.
DR GeneCards; VSX2; -.
DR HGNC; HGNC:1975; VSX2.
DR HPA; ENSG00000119614; Tissue enriched (retina).
DR MalaCards; VSX2; -.
DR MIM; 142993; gene.
DR MIM; 610092; phenotype.
DR MIM; 610093; phenotype.
DR neXtProt; NX_P58304; -.
DR OpenTargets; ENSG00000119614; -.
DR Orphanet; 98938; Colobomatous microphthalmia.
DR PharmGKB; PA26511; -.
DR VEuPathDB; HostDB:ENSG00000119614; -.
DR eggNOG; KOG0494; Eukaryota.
DR GeneTree; ENSGT00940000157776; -.
DR HOGENOM; CLU_049243_0_0_1; -.
DR InParanoid; P58304; -.
DR OMA; QDVHLQP; -.
DR OrthoDB; 1575904at2759; -.
DR PhylomeDB; P58304; -.
DR TreeFam; TF350743; -.
DR PathwayCommons; P58304; -.
DR SignaLink; P58304; -.
DR SIGNOR; P58304; -.
DR BioGRID-ORCS; 338917; 16 hits in 1090 CRISPR screens.
DR ChiTaRS; VSX2; human.
DR GeneWiki; VSX2; -.
DR GenomeRNAi; 338917; -.
DR Pharos; P58304; Tbio.
DR PRO; PR:P58304; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P58304; protein.
DR Bgee; ENSG00000119614; Expressed in lymph node and 7 other tissues.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR023339; CVC.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR003654; OAR_dom.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF03826; OAR; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51496; CVC; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS50803; OAR; 1.
PE 1: Evidence at protein level;
KW Activator; Cataract; Developmental protein; Disease variant; DNA-binding;
KW Homeobox; Microphthalmia; Nucleus; Reference proteome; Repressor;
KW Sensory transduction; Transcription; Transcription regulation; Vision.
FT CHAIN 1..361
FT /note="Visual system homeobox 2"
FT /id="PRO_0000049362"
FT DOMAIN 208..261
FT /note="CVC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00829"
FT DNA_BIND 148..207
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 304..317
FT /note="OAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00138"
FT COMPBIAS 112..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 100
FT /note="P -> Q (in dbSNP:rs35214083)"
FT /id="VAR_049593"
FT VARIANT 200
FT /note="R -> P (in MCOPCTI; loss of DNA binding capacity;
FT dbSNP:rs121912543)"
FT /evidence="ECO:0000269|PubMed:10932181"
FT /id="VAR_011618"
FT VARIANT 200
FT /note="R -> Q (in MCOPCTI; loss of DNA binding capacity at
FT consensus sequences; abnormal and prolonged expression of
FT MITF and WLS; mislocalization of CTNNB1;
FT dbSNP:rs121912543)"
FT /evidence="ECO:0000269|PubMed:10932181,
FT ECO:0000269|PubMed:17919464, ECO:0000269|PubMed:27301076"
FT /id="VAR_011619"
FT VARIANT 223
FT /note="G -> A (in MCOP2)"
FT /evidence="ECO:0000269|PubMed:21976963"
FT /id="VAR_067269"
FT VARIANT 223
FT /note="G -> R (in MCOPCB3; the patient also has cataracts;
FT dbSNP:rs755799430)"
FT /evidence="ECO:0000269|PubMed:24033328"
FT /id="VAR_075633"
FT VARIANT 227
FT /note="R -> W (in MCOP2; dbSNP:rs121912545)"
FT /evidence="ECO:0000269|PubMed:15257456"
FT /id="VAR_029357"
FT MUTAGEN 198
FT /note="N->A: Loss of SAG repressor activity. Loss of
FT competitive inhibition of ISL1-LHX3 binding to common
FT response elements."
FT /evidence="ECO:0000269|PubMed:16236706,
FT ECO:0000269|PubMed:27477290"
SQ SEQUENCE 361 AA; 39411 MW; 19EF3E8E783375F8 CRC64;
MTGKAGEALS KPKSETVAKS TSGGAPARCT GFGIQEILGL NKEPPSSHPR AALDGLAPGH
LLAARSVLSP AGVGGMGLLG PGGLPGFYTQ PTFLEVLSDP QSVHLQPLGR ASGPLDTSQT
ASSDSEDVSS SDRKMSKSAL NQTKKRKKRR HRTIFTSYQL EELEKAFNEA HYPDVYAREM
LAMKTELPED RIQVWFQNRR AKWRKREKCW GRSSVMAEYG LYGAMVRHSI PLPESILKSA
KDGIMDSCAP WLLGMHKKSL EAAAESGRKP EGERQALPKL DKMEQDERGP DAQAAISQEE
LRENSIAVLR AKAQEHSTKV LGTVSGPDSL ARSTEKPEEE EAMDEDRPAE RLSPPQLEDM
A
