ESR2_RAT
ID ESR2_RAT Reviewed; 530 AA.
AC Q62986; O35784; O35785; O55015; O55016; O70195; Q9R185;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Estrogen receptor beta;
DE Short=ER-beta;
DE AltName: Full=Nuclear receptor subfamily 3 group A member 2;
GN Name=Esr2; Synonyms=Erbeta, Nr3a2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-530 (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Prostate;
RX PubMed=8650195; DOI=10.1073/pnas.93.12.5925;
RA Kuiper G.G.J.M., Enmark E., Pelto-Huikko M., Nilsson S., Gustafsson J.-A.;
RT "Cloning of a novel receptor expressed in rat prostate and ovary.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5925-5930(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-530 (ISOFORM 2), AND FUNCTION (ISOFORMS 1
RP AND 2).
RC STRAIN=Wistar; TISSUE=Ovary;
RX PubMed=9600083; DOI=10.1006/bbrc.1998.8590;
RA Maruyama K., Endoh H., Sasaki-Iwaoka H., Kanou H., Shimaya E.,
RA Hashimoto S., Kato S., Kawashima H.;
RT "A novel isoform of rat estrogen receptor beta with 18 amino acid insertion
RT in the ligand binding domain as a putative dominant negative regular of
RT estrogen action.";
RL Biochem. Biophys. Res. Commun. 246:142-147(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC STRAIN=Wistar; TISSUE=Prostate;
RA Aldridge T.C.;
RT "Tissue specific responses to estrogen: an explanation based on
RT differential activation of multiple estrogen receptors with different
RT estrogen response elements.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE OF 46-530 (ISOFORMS 1; 3 AND 4), AND FUNCTION (ISOFORMS
RP 1; 3 AND 4).
RC STRAIN=Sprague-Dawley;
RX PubMed=9492041; DOI=10.1210/endo.139.3.5840;
RA Petersen D.N., Tkalcevic G.T., Koza-Taylor P.H., Turi T.G., Brown T.A.;
RT "Identification of estrogen receptor beta2, a functional variant of
RT estrogen receptor beta expressed in normal rat tissues.";
RL Endocrinology 139:1082-1092(1998).
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 5).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Price R., Handa R.J.;
RT "A novel splice variant of estrogen receptor beta found in rat brain.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH UBE1C.
RX PubMed=11818503; DOI=10.1210/mend.16.2.0778;
RA Fan M., Long X., Bailey J.A., Reed C.A., Osborne E., Gize E.A., Kirk E.A.,
RA Bigsby R.M., Nephew K.P.;
RT "The activating enzyme of NEDD8 inhibits steroid receptor function.";
RL Mol. Endocrinol. 16:315-330(2002).
RN [7]
RP INTERACTION WITH DNAAF4.
RX PubMed=19423554; DOI=10.1093/hmg/ddp215;
RA Massinen S., Tammimies K., Tapia-Paez I., Matsson H., Hokkanen M.E.,
RA Soederberg O., Landegren U., Castren E., Gustafsson J.A., Treuter E.,
RA Kere J.;
RT "Functional interaction of DYX1C1 with estrogen receptors suggests
RT involvement of hormonal pathways in dyslexia.";
RL Hum. Mol. Genet. 18:2802-2812(2009).
CC -!- FUNCTION: [Isoform 1]: Nuclear hormone receptor. Binds estrogens with
CC an affinity similar to that of ESR1/ER-alpha, and activates expression
CC of reporter genes containing estrogen response elements (ERE) in an
CC estrogen-dependent manner. {ECO:0000250|UniProtKB:Q92731,
CC ECO:0000269|PubMed:8650195, ECO:0000269|PubMed:9600083}.
CC -!- FUNCTION: [Isoform 2]: Lacks ligand binding affinity and suppresses
CC ESR1/ER-alpha and ESR2 isoform 1/ER-beta1 mediated transcriptional
CC activation and may act as a dominant negative regulator of estrogen
CC action. {ECO:0000269|PubMed:9600083}.
CC -!- FUNCTION: [Isoform 3]: Unable to bind DNA and activate transcription
CC due to the truncation of the DNA binding domain.
CC {ECO:0000269|PubMed:9492041}.
CC -!- FUNCTION: [Isoform 4]: Unable to bind DNA and activate transcription
CC due to the truncation of the DNA binding domain.
CC {ECO:0000269|PubMed:9492041}.
CC -!- SUBUNIT: Binds DNA as a homodimer. Can form a heterodimer with ESR1.
CC Interacts with NCOA1, NCOA3, NCOA5 and NCOA6 coactivators, leading to a
CC strong increase of transcription of target genes. Interacts with UBE1C
CC and AKAP13. Interacts with DNTTIP2 (By similarity). Interacts with
CC CCDC62 in the presence of estradiol/E2; this interaction seems to
CC enhance the transcription of target genes. Interacts with PRMT2.
CC Interacts with CCAR2 (via N-terminus) in a ligand-independent manner
CC (By similarity). Interacts with DNAAF4. Interacts with RBM39, in the
CC presence of estradiol (E2) (By similarity).
CC {ECO:0000250|UniProtKB:O08537, ECO:0000250|UniProtKB:Q92731,
CC ECO:0000269|PubMed:11818503, ECO:0000269|PubMed:19423554}.
CC -!- INTERACTION:
CC Q62986; P62989: Ubb; NbExp=2; IntAct=EBI-15938489, EBI-7038538;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92731}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Beta1;
CC IsoId=Q62986-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta2;
CC IsoId=Q62986-2; Sequence=VSP_003699;
CC Name=3; Synonyms=Beta1-delta3;
CC IsoId=Q62986-3; Sequence=VSP_003697;
CC Name=4; Synonyms=Beta2-delta3;
CC IsoId=Q62986-4; Sequence=VSP_003697, VSP_003699;
CC Name=5; Synonyms=Beta1-delta4;
CC IsoId=Q62986-5; Sequence=VSP_003698;
CC -!- TISSUE SPECIFICITY: Expressed in prostate, ovary, lung, liver, kidney,
CC fat, bone, brain, uterus and testis.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- PTM: Phosphorylation at Ser-87 and Ser-105 recruits NCOA1.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA05631.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U57439; AAC52602.1; -; mRNA.
DR EMBL; AB012721; BAA25431.1; -; mRNA.
DR EMBL; AJ002602; CAA05631.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ002603; CAA05632.1; -; Genomic_DNA.
DR EMBL; AF042058; AAB97424.1; -; mRNA.
DR EMBL; AF042059; AAB97425.1; -; mRNA.
DR EMBL; AF042060; AAB97426.1; -; mRNA.
DR EMBL; AF042061; AAB97427.1; -; mRNA.
DR EMBL; AF161187; AAD47637.1; -; mRNA.
DR PIR; JW0046; JW0046.
DR RefSeq; NP_036886.1; NM_012754.1.
DR PDB; 1HJ1; X-ray; 2.30 A; A=255-509.
DR PDB; 1QKN; X-ray; 2.25 A; A=255-509.
DR PDB; 2J7X; X-ray; 2.10 A; A=255-509.
DR PDB; 2J7Y; X-ray; 1.80 A; A=255-509.
DR PDBsum; 1HJ1; -.
DR PDBsum; 1QKN; -.
DR PDBsum; 2J7X; -.
DR PDBsum; 2J7Y; -.
DR AlphaFoldDB; Q62986; -.
DR SMR; Q62986; -.
DR BioGRID; 247214; 6.
DR DIP; DIP-60383N; -.
DR IntAct; Q62986; 2.
DR STRING; 10116.ENSRNOP00000043144; -.
DR BindingDB; Q62986; -.
DR ChEMBL; CHEMBL3021; -.
DR DrugCentral; Q62986; -.
DR GuidetoPHARMACOLOGY; 621; -.
DR GlyGen; Q62986; 1 site.
DR PhosphoSitePlus; Q62986; -.
DR PaxDb; Q62986; -.
DR PRIDE; Q62986; -.
DR GeneID; 25149; -.
DR KEGG; rno:25149; -.
DR UCSC; RGD:2582; rat. [Q62986-1]
DR CTD; 2100; -.
DR RGD; 2582; Esr2.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; Q62986; -.
DR OrthoDB; 487299at2759; -.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-RNO-8939211; ESR-mediated signaling.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR EvolutionaryTrace; Q62986; -.
DR PRO; PR:Q62986; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005929; C:cilium; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032993; C:protein-DNA complex; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:1903924; F:estradiol binding; IPI:RGD.
DR GO; GO:0099130; F:estrogen binding; IPI:RGD.
DR GO; GO:0034056; F:estrogen response element binding; IDA:RGD.
DR GO; GO:1901363; F:heterocyclic compound binding; IPI:RGD.
DR GO; GO:0042562; F:hormone binding; IDA:RGD.
DR GO; GO:0030284; F:nuclear estrogen receptor activity; IDA:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:RGD.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IDA:RGD.
DR GO; GO:0097159; F:organic cyclic compound binding; IPI:RGD.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:RGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0005496; F:steroid binding; IDA:UniProtKB.
DR GO; GO:1990239; F:steroid hormone binding; IPI:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0021764; P:amygdala development; IEP:RGD.
DR GO; GO:0001662; P:behavioral fear response; IDA:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
DR GO; GO:0071259; P:cellular response to magnetism; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; ISO:RGD.
DR GO; GO:0044849; P:estrous cycle; IMP:RGD.
DR GO; GO:0008585; P:female gonad development; IEP:RGD.
DR GO; GO:0008628; P:hormone-mediated apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0021854; P:hypothalamus development; IEP:RGD.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; ISO:RGD.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; IDA:RGD.
DR GO; GO:0007611; P:learning or memory; IMP:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:RGD.
DR GO; GO:0048521; P:negative regulation of behavior; IDA:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:RGD.
DR GO; GO:2000252; P:negative regulation of feeding behavior; IMP:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IDA:RGD.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:RGD.
DR GO; GO:0030850; P:prostate gland development; IEP:RGD.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; IDA:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:1903925; P:response to bisphenol A; IEP:RGD.
DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0033595; P:response to genistein; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0044752; P:response to human chorionic gonadotropin; IEP:RGD.
DR GO; GO:0017085; P:response to insecticide; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:1902074; P:response to salt; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IMP:RGD.
DR GO; GO:0009414; P:response to water deprivation; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0060009; P:Sertoli cell development; IEP:RGD.
DR GO; GO:0060011; P:Sertoli cell proliferation; IMP:RGD.
DR GO; GO:0060065; P:uterus development; ISO:RGD.
DR GO; GO:0060068; P:vagina development; ISO:RGD.
DR GO; GO:0042311; P:vasodilation; IMP:RGD.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR021064; ER-beta-like_N.
DR InterPro; IPR028355; ER-beta/gamma.
DR InterPro; IPR024178; Est_rcpt/est-rel_rcp.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF12497; ERbeta_N; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PIRSF; PIRSF500102; ER-b; 1.
DR PIRSF; PIRSF002527; ER-like_NR; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; DNA-binding; Glycoprotein;
KW Lipid-binding; Metal-binding; Nucleus; Phosphoprotein; Receptor;
KW Reference proteome; Steroid-binding; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..530
FT /note="Estrogen receptor beta"
FT /id="PRO_0000053646"
FT DOMAIN 264..498
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 149..214
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 149..169
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 185..209
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..148
FT /note="Modulating"
FT REGION 506..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 61
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O08537"
FT MOD_RES 87
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:O08537"
FT MOD_RES 105
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:O08537"
FT CARBOHYD 61
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 179..217
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003697"
FT VAR_SEQ 219..318
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003698"
FT VAR_SEQ 364
FT /note="R -> RSSEDPHWHVAQMKSAAPR (in isoform 2 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:9600083"
FT /id="VSP_003699"
FT CONFLICT 72
FT /note="L -> Q (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="P -> A (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="S -> P (in Ref. 3; CAA05631)"
FT /evidence="ECO:0000305"
FT CONFLICT 505
FT /note="S -> P (in Ref. 3; CAA05631)"
FT /evidence="ECO:0000305"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:2J7Y"
FT HELIX 291..315
FT /evidence="ECO:0007829|PDB:2J7Y"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2J7Y"
FT HELIX 324..347
FT /evidence="ECO:0007829|PDB:2J7Y"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:2J7Y"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:2J7Y"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:2J7Y"
FT HELIX 373..390
FT /evidence="ECO:0007829|PDB:2J7Y"
FT HELIX 394..405
FT /evidence="ECO:0007829|PDB:2J7Y"
FT TURN 406..409
FT /evidence="ECO:0007829|PDB:2J7Y"
FT HELIX 421..443
FT /evidence="ECO:0007829|PDB:2J7Y"
FT HELIX 448..481
FT /evidence="ECO:0007829|PDB:2J7Y"
FT HELIX 489..496
FT /evidence="ECO:0007829|PDB:2J7Y"
SQ SEQUENCE 530 AA; 59152 MW; 36F269D9FD773DA9 CRC64;
MEIKNSPSSL SSPASYNCSQ SILPLEHGPI YIPSSYVDNR HEYSAMTFYS PAVMNYSVPG
STSNLDGGPV RLSTSPNVLW PTSGHLSPLA THCQSSLLYA EPQKSPWCEA RSLEHTLPVN
RETLKRKLSG SSCASPVTSP NAKRDAHFCP VCSDYASGYH YGVWSCEGCK AFFKRSIQGH
NDYICPATNQ CTIDKNRRKS CQACRLRKCY EVGMVKCGSR RERCGYRIVR RQRSSSEQVH
CLSKAKRNGG HAPRVKELLL STLSPEQLVL TLLEAEPPNV LVSRPSMPFT EASMMMSLTK
LADKELVHMI GWAKKIPGFV ELSLLDQVRL LESCWMEVLM VGLMWRSIDH PGKLIFAPDL
VLDRDEGKCV EGILEIFDML LATTSRFREL KLQHKEYLCV KAMILLNSSM YPLASANQEA
ESSRKLTHLL NAVTDALVWV IAKSGISSQQ QSVRLANLLM LLSHVRHISN KGMEHLLSMK
CKNVVPVYDL LLEMLNAHTL RGYKSSISGS ECSSTEDSKN KESSQNLQSQ
