GenomeNet

Database: UniProt
Entry: O93383
LinkDB: O93383
Original site: O93383 
ID   NRG1_XENLA              Reviewed;         677 AA.
AC   O93383; Q9W6N0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   05-DEC-2018, entry version 106.
DE   RecName: Full=Pro-neuregulin-1, membrane-bound isoform;
DE            Short=Pro-NRG1;
DE   Contains:
DE     RecName: Full=Neuregulin-1;
DE   Flags: Precursor;
GN   Name=nrg1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA1), AND ALTERNATIVE SPLICING.
RX   PubMed=9685585; DOI=10.1016/S0169-328X(98)00085-0;
RA   Yang J.F., Zhou H., Pun S., Ip N.Y., Peng H.B., Tsim K.W.K.;
RT   "Cloning of cDNAs encoding Xenopus neuregulin: expression in myotomal
RT   muscle during embryo development.";
RL   Brain Res. Mol. Brain Res. 58:59-73(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CRD).
RX   PubMed=10383827; DOI=10.1006/mcne.1999.0759;
RA   Yang J.F., Zhou H., Choi R.C., Ip N.Y., Peng H.B., Tsim K.W.K.;
RT   "A cysteine-rich form of Xenopus neuregulin induces the expression of
RT   acetylcholine receptors in cultured myotubes.";
RL   Mol. Cell. Neurosci. 13:415-429(1999).
CC   -!- FUNCTION: Direct ligand for the ERBB tyrosine kinase receptors.
CC       Induces expression of acetylcholine receptor in synaptic nuclei.
CC   -!- SUBCELLULAR LOCATION: Pro-neuregulin-1, membrane-bound isoform:
CC       Cell membrane {ECO:0000250}; Single-pass type I membrane protein
CC       {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Neuregulin-1: Secreted {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist. Isoforms have
CC         alpha-or beta-type EGF-like domains.;
CC       Name=Alpha1;
CC         IsoId=O93383-1; Sequence=Displayed;
CC       Name=CRD; Synonyms=CRD-NRG1, Cysteine-rich domain;
CC         IsoId=O93383-2; Sequence=VSP_003449, VSP_003450;
CC   -!- TISSUE SPECIFICITY: Isoform alpha1 is expressed in brain and
CC       muscle. Isoform CRD is expressed in brain and spinal cord, but at
CC       very low level in muscle.
CC   -!- DEVELOPMENTAL STAGE: Strong expression in developing brain and
CC       spinal cord of the embryo. Also expressed in the myotomal muscle.
CC   -!- DOMAIN: The cytoplasmic domain may be involved in the regulation
CC       of trafficking and proteolytic processing. Regulation of the
CC       proteolytic processing involves initial intracellular domain
CC       dimerization (By similarity). {ECO:0000250}.
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
CC       external face leads to the release of the soluble growth factor
CC       form.
CC   -!- PTM: Extensive glycosylation precedes the proteolytic cleavage.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the neuregulin family. {ECO:0000305}.
DR   EMBL; AF076618; AAC26804.1; -; mRNA.
DR   EMBL; AF142632; AAD33893.1; -; mRNA.
DR   RefSeq; NP_001079063.1; NM_001085594.1. [O93383-2]
DR   UniGene; Xl.289; -.
DR   ProteinModelPortal; O93383; -.
DR   SMR; O93383; -.
DR   GeneID; 373595; -.
DR   KEGG; xla:373595; -.
DR   CTD; 373595; -.
DR   Xenbase; XB-GENE-1011454; nrg1.
DR   HOVERGEN; HBG006531; -.
DR   KO; K05455; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR013032; EGF-like_CS.
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:SF7; PTHR11100:SF7; 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; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Growth factor; Immunoglobulin domain; Membrane;
KW   Secreted; Transmembrane; Transmembrane helix.
FT   CHAIN         1    677       Pro-neuregulin-1, membrane-bound isoform.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000019470.
FT   CHAIN         1    259       Neuregulin-1. {ECO:0000250}.
FT                                /FTId=PRO_0000019471.
FT   TOPO_DOM      1    260       Extracellular. {ECO:0000255}.
FT   TRANSMEM    261    280       Helical; Note=Internal signal sequence.
FT                                {ECO:0000255}.
FT   TOPO_DOM    281    677       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       37    132       Ig-like C2-type.
FT   DOMAIN      188    232       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS      1     25       Lys-rich.
FT   CARBOHYD    124    124       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    130    130       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     57    116       {ECO:0000250}.
FT   DISULFID    192    206       {ECO:0000250}.
FT   DISULFID    200    220       {ECO:0000250}.
FT   DISULFID    222    231       {ECO:0000250}.
FT   VAR_SEQ       1    136       MAEKKKVKEGKGRKGKGKKDRKGKKAEGSDQGAAASPKLKE
FT                                IKTQSVQEGKKLVLKCQAVSEQPSLKFRWFKGEKEIGAKNK
FT                                PDSKPEHIKIRGKKKSSELQISKASSADNGEYKCMVSNQLG
FT                                NDTVTVNVTIVPK -> MSEDTAEGLQNQCSEQSSDPPSAE
FT                                LQNEESMPETQDEEETTHGITGLAITCCVCLEADRLRICLN
FT                                SEKICIIPILACLISLCLCIAGLKWVFVDKIFEYDSPTHLD
FT                                PGHRGQDLILYTDTAPSTLVPSSVRTLPVIIPTTDSKAAVT
FT                                FKFGTSLLPTE (in isoform CRD).
FT                                {ECO:0000303|PubMed:10383827}.
FT                                /FTId=VSP_003449.
FT   VAR_SEQ     223    252       KPGFTGARCTETDPLRVVRSEKHLGIEFME -> PNEFTGD
FT                                RCQNYVMASFYK (in isoform CRD).
FT                                {ECO:0000303|PubMed:10383827}.
FT                                /FTId=VSP_003450.
SQ   SEQUENCE   677 AA;  75795 MW;  49279E8F5BAE396F CRC64;
     MAEKKKVKEG KGRKGKGKKD RKGKKAEGSD QGAAASPKLK EIKTQSVQEG KKLVLKCQAV
     SEQPSLKFRW FKGEKEIGAK NKPDSKPEHI KIRGKKKSSE LQISKASSAD NGEYKCMVSN
     QLGNDTVTVN VTIVPKPTYN HLLLMKIYLK VTSVEKSVEP STLNLLESQK EVIFATTKRG
     DTTAGPGHLI KCSDKEKTYC VNGGECYVLN GITSSNQFMC KCKPGFTGAR CTETDPLRVV
     RSEKHLGIEF MEAEELYQKR VLTITGICID LLVVGDMCVV DAYCKTKKQR KKLNDRLRQS
     LRERNKNITN KDNRPHNPKN PPPRKNVQLV NQYVSKNVIS SEHVIERETE TSFSTSHYTS
     TTHHSTTVTQ TPSHSWSNGL SESMISEKSY SVIVTSSVEN SRHTSPTGPR GRLNGIGGPR
     DCSYLRHARD TPDSYRDSPH SERYVSAMTT PARMSPVEFK TPISPKSPCL ETSPPESSLA
     VSVPSVAVSP FIEEERPLLL VSPPRLREKR YDRKTPQKTP HKQHNSYHHN PGHDSSSLPP
     NPLRIVEDEE YETTQEYEPS LEPAKKLVNS RRQKRTKPNG HISNRLELDS DSSSESSTSE
     SETEDERIGE ETPFLSIQNP LAASLESASL YRHADSRTNP TSRFSTQEEL QARLSSIANQ
     ALCDQKKRKM TCKTLFI
//
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