NRG1_RAT
ID NRG1_RAT Reviewed; 662 AA.
AC P43322; P43323; P43324; P43325; P43326; P43327; P43328;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Pro-neuregulin-1, membrane-bound isoform;
DE Short=Pro-NRG1;
DE Contains:
DE RecName: Full=Neuregulin-1;
DE AltName: Full=Acetylcholine receptor-inducing activity;
DE Short=ARIA;
DE AltName: Full=Glial growth factor;
DE AltName: Full=Heregulin;
DE Short=HRG;
DE AltName: Full=Neu differentiation factor;
DE AltName: Full=Sensory and motor neuron-derived factor;
DE Flags: Precursor;
GN Name=Nrg1; Synonyms=Ndf;
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], AND ALTERNATIVE SPLICING.
RC TISSUE=Fibroblast;
RX PubMed=7509448; DOI=10.1128/mcb.14.3.1909-1919.1994;
RA Wen D., Suggs S.V., Karunagaran D., Liu N., Cupples R.L., Luo Y.,
RA Janssen A.M., Ben-Baruch N., Trollinger D.B., Jacobsen V.L., Meng S.-Y.,
RA Lu H.S., Hu S., Chang D., Yang W., Yanigahara D., Koski R.A., Yarden Y.;
RT "Structural and functional aspects of the multiplicity of Neu
RT differentiation factors.";
RL Mol. Cell. Biol. 14:1909-1919(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA2C), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fibroblast;
RX PubMed=1349853; DOI=10.1016/0092-8674(92)90456-m;
RA Wen D., Peles E., Cupples R., Suggs S.V., Bacus S.S., Luo Y., Trail G.,
RA Hu S., Silbiger S.M., Levy R.B., Koski R.A., Lu H.S., Yarden Y.;
RT "Neu differentiation factor: a transmembrane glycoprotein containing an EGF
RT domain and an immunoglobulin homology unit.";
RL Cell 69:559-572(1992).
RN [3]
RP PROTEIN SEQUENCE OF 14-36.
RX PubMed=1348215; DOI=10.1016/0092-8674(92)90131-u;
RA Peles E., Bacus S.S., Koski R.A., Lu H.S., Wen D., Ogden S.G., Levy R.B.,
RA Yarden Y.;
RT "Isolation of the neu/HER-2 stimulatory ligand: a 44 kd glycoprotein that
RT induces differentiation of mammary tumor cells.";
RL Cell 69:205-216(1992).
RN [4]
RP REGULATION OF PROCESSING (ISOFORM ALPHA2C).
RX PubMed=9852099; DOI=10.1074/jbc.273.51.34335;
RA Liu X., Hwang H., Cao L., Wen D., Liu N., Graham R.M., Zhou M.;
RT "Release of the neuregulin functional polypeptide requires its cytoplasmic
RT tail.";
RL J. Biol. Chem. 273:34335-34340(1998).
RN [5]
RP INTERACTION WITH LIMK1.
RX PubMed=9685409; DOI=10.1074/jbc.273.32.20525;
RA Wang J.Y., Frenzel K.E., Wen D., Falls D.L.;
RT "Transmembrane neuregulins interact with LIM kinase 1, a cytoplasmic
RT protein kinase implicated in development of visuospatial cognition.";
RL J. Biol. Chem. 273:20525-20534(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [7]
RP FUNCTION.
RX PubMed=17250808; DOI=10.1016/j.bbrc.2007.01.009;
RA Liu Y., Tao Y.M., Woo R.S., Xiong W.C., Mei L.;
RT "Stimulated ErbB4 internalization is necessary for neuregulin signaling in
RT neurons.";
RL Biochem. Biophys. Res. Commun. 354:505-510(2007).
CC -!- FUNCTION: Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors.
CC Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in
CC ligand-stimulated tyrosine phosphorylation and activation of the ERBB
CC receptors. The multiple isoforms perform diverse functions such as
CC inducing growth and differentiation of epithelial, glial, neuronal, and
CC skeletal muscle cells; inducing expression of acetylcholine receptor in
CC synaptic vesicles during the formation of the neuromuscular junction;
CC stimulating lobuloalveolar budding and milk production in the mammary
CC gland and inducing differentiation of mammary tumor cells; stimulating
CC Schwann cell proliferation; implication in the development of the
CC myocardium such as trabeculation of the developing heart. Binds to
CC ERBB4 and ERBB3. Acts as a ligand for integrins and binds (via EGF
CC domain) to integrins ITGAV:ITGB3 or ITGA6:ITGB4. Its binding to
CC integrins and subsequent ternary complex formation with integrins and
CC ERRB3 are essential for NRG1-ERBB signaling (By similarity). Induces
CC the phosphorylation and activation of MAPK3/ERK1, MAPK1/ERK2 and AKT1,
CC and ligand-dependent ERBB4 endocytosis is essential for the NRG1-
CC mediated activation of these kinases in neurons (PubMed:17250808).
CC {ECO:0000250|UniProtKB:Q02297, ECO:0000269|PubMed:17250808}.
CC -!- SUBUNIT: The cytoplasmic domain interacts with the LIM domain region of
CC LIMK1 (PubMed:9685409). Forms a ternary complex with ERBB3 and
CC ITGAV:ITGB3 or ITGA6:ITGB4 (By similarity).
CC {ECO:0000250|UniProtKB:Q02297, ECO:0000269|PubMed:9685409}.
CC -!- SUBCELLULAR LOCATION: [Pro-neuregulin-1, membrane-bound isoform]: Cell
CC membrane; Single-pass type I membrane protein. Note=Does not seem to be
CC active.
CC -!- SUBCELLULAR LOCATION: [Neuregulin-1]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Additional isoforms seem to exist.;
CC Name=Beta4; Synonyms=NDF42A;
CC IsoId=P43322-1; Sequence=Displayed;
CC Name=Alpha2A; Synonyms=NDF38;
CC IsoId=P43322-2; Sequence=VSP_003436;
CC Name=Alpha2B; Synonyms=NDF19;
CC IsoId=P43322-3; Sequence=VSP_003436, VSP_003443, VSP_003444;
CC Name=Alpha2C; Synonyms=NDF44;
CC IsoId=P43322-4; Sequence=VSP_003436, VSP_003442;
CC Name=Beta1;
CC IsoId=P43322-5; Sequence=VSP_003437;
CC Name=Beta2; Synonyms=NDF40;
CC IsoId=P43322-6; Sequence=VSP_003440, VSP_003441;
CC Name=BetA2A; Synonyms=NDF22;
CC IsoId=P43322-7; Sequence=VSP_003440;
CC Name=Beta3; Synonyms=NDF4;
CC IsoId=P43322-8; Sequence=VSP_003438, VSP_003439;
CC -!- TISSUE SPECIFICITY: Widely expressed. Most tissues contain isoform
CC alpha2A and isoform alpha2B. Isoform Alpha2 and isoform beta2 are the
CC predominant forms in mesenchymal and non-neuronal organs. Isoform Beta1
CC is enriched in brain and spinal cord, but not in muscle and heart.
CC Isoform Alpha2C is highly expressed in spinal cord, moderately in lung,
CC brain, ovary, and stomach, in low amounts in the kidney, skin and heart
CC and not detected in the liver, spleen, and placenta.
CC -!- DOMAIN: The cytoplasmic domain may be involved in the regulation of
CC trafficking and proteolytic processing. Regulation of the proteolytic
CC processing involves initial intracellular domain dimerization.
CC -!- DOMAIN: ERBB receptor binding is elicited entirely by the EGF-like
CC domain.
CC -!- PTM: Proteolytic cleavage close to the plasma membrane on the external
CC face leads to the release of the soluble growth factor form.
CC -!- PTM: N- and O-glycosylated (By similarity). Extensive glycosylation
CC precedes the proteolytic cleavage. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neuregulin family. {ECO:0000305}.
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DR EMBL; U02315; AAA19940.1; -; mRNA.
DR EMBL; U02316; AAA19941.1; -; mRNA.
DR EMBL; U02317; AAA19942.1; -; mRNA.
DR EMBL; U02318; AAA19943.1; -; mRNA.
DR EMBL; U02319; AAA19944.1; -; mRNA.
DR EMBL; U02320; AAA19945.1; -; mRNA.
DR EMBL; U02321; AAA19946.1; -; mRNA.
DR EMBL; U02322; AAA19947.1; -; mRNA.
DR EMBL; U02323; AAA19948.1; -; mRNA.
DR EMBL; U02324; AAA19949.1; -; mRNA.
DR EMBL; M92430; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; I61718; I61718.
DR PIR; I61719; I61719.
DR PIR; I61722; I61722.
DR RefSeq; NP_001258052.1; NM_001271123.1. [P43322-8]
DR AlphaFoldDB; P43322; -.
DR STRING; 10116.ENSRNOP00000014268; -.
DR GlyGen; P43322; 3 sites.
DR iPTMnet; P43322; -.
DR PhosphoSitePlus; P43322; -.
DR PaxDb; P43322; -.
DR PRIDE; P43322; -.
DR GeneID; 112400; -.
DR KEGG; rno:112400; -.
DR UCSC; RGD:621341; rat. [P43322-1]
DR CTD; 3084; -.
DR RGD; 621341; Nrg1.
DR eggNOG; ENOG502QRUM; Eukaryota.
DR InParanoid; P43322; -.
DR OrthoDB; 313400at2759; -.
DR PhylomeDB; P43322; -.
DR PRO; PR:P43322; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0045499; F:chemorepellent activity; ISO:RGD.
DR GO; GO:0005176; F:ErbB-2 class receptor binding; ISO:RGD.
DR GO; GO:0043125; F:ErbB-3 class receptor binding; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; ISO:RGD.
DR GO; GO:0048018; F:receptor ligand activity; ISO:RGD.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; ISO:RGD.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISS:UniProtKB.
DR GO; GO:0007171; P:activation of transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR GO; GO:0003161; P:cardiac conduction system development; ISO:RGD.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; ISO:RGD.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; ISO:RGD.
DR GO; GO:0048738; P:cardiac muscle tissue development; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0021842; P:chemorepulsion involved in interneuron migration from the subpallium to the cortex; ISO:RGD.
DR GO; GO:0060956; P:endocardial cell differentiation; ISO:RGD.
DR GO; GO:0038127; P:ERBB signaling pathway; ISS:UniProtKB.
DR GO; GO:0038133; P:ERBB2-ERBB3 signaling pathway; ISO:RGD.
DR GO; GO:0038135; P:ERBB2-ERBB4 signaling pathway; ISO:RGD.
DR GO; GO:0038129; P:ERBB3 signaling pathway; ISO:RGD.
DR GO; GO:0038130; P:ERBB4 signaling pathway; ISO:RGD.
DR GO; GO:0038138; P:ERBB4-ERBB4 signaling pathway; ISO:RGD.
DR GO; GO:0010001; P:glial cell differentiation; ISO:RGD.
DR GO; GO:0021781; P:glial cell fate commitment; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0000165; P:MAPK cascade; ISO:RGD.
DR GO; GO:0007613; P:memory; IMP:RGD.
DR GO; GO:0007517; P:muscle organ development; ISO:RGD.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISO:RGD.
DR GO; GO:2000853; P:negative regulation of corticosterone secretion; IMP:RGD.
DR GO; GO:2001223; P:negative regulation of neuron migration; ISO:RGD.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0051048; P:negative regulation of secretion; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0048663; P:neuron fate commitment; ISO:RGD.
DR GO; GO:0045213; P:neurotransmitter receptor metabolic process; ISO:RGD.
DR GO; GO:0042476; P:odontogenesis; IEP:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; ISO:RGD.
DR GO; GO:0007422; P:peripheral nervous system development; ISO:RGD.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IDA:RGD.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:RGD.
DR GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:RGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:0010625; P:positive regulation of Schwann cell proliferation; IMP:RGD.
DR GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; ISO:RGD.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; ISO:RGD.
DR GO; GO:0045595; P:regulation of cell differentiation; ISO:RGD.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:RGD.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR040180; Neuregulin.
DR InterPro; IPR002154; Neuregulin_C.
DR InterPro; IPR018250; NRG1.
DR PANTHER; PTHR11100; PTHR11100; 1.
DR PANTHER; PTHR11100:SF25; PTHR11100:SF25; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF02158; Neuregulin; 1.
DR PRINTS; PR01089; NEUREGULIN.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Glycoprotein; Growth factor;
KW Immunoglobulin domain; Membrane; Reference proteome; Secreted;
KW Transmembrane; Transmembrane helix.
FT PROPEP 1..13
FT /evidence="ECO:0000269|PubMed:1348215"
FT /id="PRO_0000019465"
FT CHAIN 14..662
FT /note="Pro-neuregulin-1, membrane-bound isoform"
FT /id="PRO_0000019466"
FT CHAIN 14..264
FT /note="Neuregulin-1"
FT /id="PRO_0000019467"
FT TOPO_DOM 14..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..288
FT /note="Helical; Note=Internal signal sequence"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..128
FT /note="Ig-like C2-type"
FT DOMAIN 178..222
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..112
FT DISULFID 182..196
FT /evidence="ECO:0000250"
FT DISULFID 190..210
FT /evidence="ECO:0000250"
FT DISULFID 212..221
FT /evidence="ECO:0000250"
FT VAR_SEQ 213..256
FT /note="PNEFTGDRCQNYVMASFYMTSRRKRQETEKPLERKLDHSLVKES -> QPGF
FT TGARCTENVPMKVQTQE (in isoform Alpha2A, isoform Alpha2B and
FT isoform Alpha2C)"
FT /evidence="ECO:0000303|PubMed:1349853"
FT /id="VSP_003436"
FT VAR_SEQ 231..257
FT /note="MTSRRKRQETEKPLERKLDHSLVKESK -> KHLGIEFME (in isoform
FT Beta1)"
FT /evidence="ECO:0000305"
FT /id="VSP_003437"
FT VAR_SEQ 231..256
FT /note="Missing (in isoform Beta2 and isoform BetA2A)"
FT /evidence="ECO:0000305"
FT /id="VSP_003440"
FT VAR_SEQ 231..241
FT /note="MTSRRKRQETE -> STSTPFLSLPE (in isoform Beta3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003438"
FT VAR_SEQ 242..662
FT /note="Missing (in isoform Beta3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003439"
FT VAR_SEQ 325..330
FT /note="PPENVQ -> RVRTRG (in isoform Beta2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003441"
FT VAR_SEQ 446..662
FT /note="Missing (in isoform Alpha2C)"
FT /evidence="ECO:0000303|PubMed:1349853"
FT /id="VSP_003442"
FT VAR_SEQ 446..484
FT /note="YVSAMTTPARMSPVDFHTPSSPKSPPSEMSPPVSSMTVS -> HNLIAELRR
FT NKAYRSKCMQIQLSATHLRPSSITHLGFIL (in isoform Alpha2B)"
FT /evidence="ECO:0000305"
FT /id="VSP_003443"
FT VAR_SEQ 485..662
FT /note="Missing (in isoform Alpha2B)"
FT /evidence="ECO:0000305"
FT /id="VSP_003444"
FT CONFLICT 90
FT /note="K -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="T -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="Y -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 73288 MW; 1C31ABCF2A8EB1D5 CRC64;
MSERKEGRGK GKGKKKDRGS RGKPGPAEGD PSPALPPRLK EMKSQESAAG SKLVLRCETS
SEYSSLRFKW FKNGNELNRK NKPENIKIQK KPGKSELRIN KASLADSGEY MCKVISKLGN
DSASANITIV ESNEFITGMP ASTETAYVSS ESPIRISVST EGANTSSSTS TSTTGTSHLI
KCAEKEKTFC VNGGECFTVK DLSNPSRYLC KCPNEFTGDR CQNYVMASFY MTSRRKRQET
EKPLERKLDH SLVKESKAEE LYQKRVLTIT GICIALLVVG IMCVVAYCKT KKQRQKLHDR
LRQSLRSERS NLVNIANGPH HPNPPPENVQ LVNQYVSKNV ISSEHIVERE VETSFSTSHY
TSTAHHSTTV TQTPSHSWSN GHTESVISES NSVIMMSSVE NSRHSSPAGG PRGRLHGLGG
PRDNSFLRHA RETPDSYRDS PHSERYVSAM TTPARMSPVD FHTPSSPKSP PSEMSPPVSS
MTVSMPSVAV SPFVEEERPL LLVTPPRLRE KKYDHHPQQL NSFHHNPAHQ STSLPPSPLR
IVEDEEYETT QEYESVQEPV KKVTNSRRAK RTKPNGHIAN RLEMDSNTSS VSSNSESETE
DERVGEDTPF LGIQNPLAAS LEVAPAFRLA ESRTNPAGRF STQEELQARL SSVIANQDPI
AV
