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   27-MAR-2024, entry version 185.
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). Interacts with NRDC and
CC       BACE1 (By similarity). {ECO:0000250|UniProtKB:Q02297,
CC       ECO:0000250|UniProtKB:Q6DR98, 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   AlphaFoldDB; P43322; -.
DR   SMR; P43322; -.
DR   STRING; 10116.ENSRNOP00000072731; -.
DR   GlyCosmos; P43322; 3 sites, No reported glycans.
DR   GlyGen; P43322; 3 sites.
DR   iPTMnet; P43322; -.
DR   PhosphoSitePlus; P43322; -.
DR   PaxDb; 10116-ENSRNOP00000014268; -.
DR   Ensembl; ENSRNOT00065003631; ENSRNOP00065002514; ENSRNOG00065002671. [P43322-1]
DR   UCSC; RGD:621341; rat. [P43322-1]
DR   AGR; RGD:621341; -.
DR   RGD; 621341; Nrg1.
DR   eggNOG; ENOG502QRUM; Eukaryota.
DR   InParanoid; P43322; -.
DR   OrthoDB; 3025258at2759; -.
DR   PhylomeDB; P43322; -.
DR   Reactome; R-RNO-1227986; Signaling by ERBB2.
DR   Reactome; R-RNO-1236394; Signaling by ERBB4.
DR   Reactome; R-RNO-1250196; SHC1 events in ERBB2 signaling.
DR   Reactome; R-RNO-1250342; PI3K events in ERBB4 signaling.
DR   Reactome; R-RNO-1250347; SHC1 events in ERBB4 signaling.
DR   Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-RNO-1306955; GRB7 events in ERBB2 signaling.
DR   Reactome; R-RNO-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR   Reactome; R-RNO-1963640; GRB2 events in ERBB2 signaling.
DR   Reactome; R-RNO-1963642; PI3K events in ERBB2 signaling.
DR   Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-RNO-6785631; ERBB2 Regulates Cell Motility.
DR   Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-RNO-8847993; ERBB2 Activates PTK6 Signaling.
DR   Reactome; R-RNO-8863795; Downregulation of ERBB2 signaling.
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:0097471; C:mossy fiber rosette; ISO:RGD.
DR   GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0098794; C:postsynapse; ISO:RGD.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:RGD.
DR   GO; GO:0048787; C:presynaptic active zone membrane; ISO:RGD.
DR   GO; GO:0045202; C:synapse; ISO: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:0003712; F:transcription coregulator activity; ISO:RGD.
DR   GO; GO:0032148; P:activation of protein kinase B activity; ISS:UniProtKB.
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: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:0050965; P:detection of temperature stimulus involved in sensory perception of pain; 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:0042552; P:myelination; 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:0045892; P:negative regulation of DNA-templated transcription; ISO: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:0007399; P:nervous system development; ISO:RGD.
DR   GO; GO:0048663; P:neuron fate commitment; ISO:RGD.
DR   GO; GO:0001764; P:neuron migration; ISO:RGD.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; ISO:RGD.
DR   GO; GO:0007422; P:peripheral nervous system development; ISO:RGD.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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:0030163; P:protein catabolic process; 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:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR   GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR   GO; GO:0014044; P:Schwann cell development; ISO:RGD.
DR   GO; GO:0014037; P:Schwann cell differentiation; ISO:RGD.
DR   GO; GO:0019233; P:sensory perception of pain; ISO: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   CDD; cd00053; EGF; 1.
DR   CDD; cd05895; Ig_Pro_neuregulin-1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.10.25.10; Laminin; 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; HEREGULIN-NEUREGULIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR11100:SF7; PRO-NEUREGULIN-1, MEMBRANE-BOUND ISOFORM; 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; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 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
//