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Database: UniProt
Entry: O35181
LinkDB: O35181
Original site: O35181 
ID   NRG3_MOUSE              Reviewed;         713 AA.
AC   O35181;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   13-FEB-2019, entry version 151.
DE   RecName: Full=Pro-neuregulin-3, membrane-bound isoform;
DE            Short=Pro-NRG3;
DE   Contains:
DE     RecName: Full=Neuregulin-3;
DE              Short=NRG-3;
DE   Flags: Precursor;
GN   Name=Nrg3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH ERBB4.
RC   TISSUE=Brain;
RX   PubMed=9275162; DOI=10.1073/pnas.94.18.9562;
RA   Zhang D., Sliwkowski M.X., Mark M., Frantz G., Akita R., Sun Y.,
RA   Hillan K., Crowley C., Brush J., Godowski P.J.;
RT   "Neuregulin-3 (NRG3): a novel neural tissue-enriched protein that
RT   binds and activates ErbB4.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9562-9567(1997).
CC   -!- FUNCTION: Direct ligand for the ERBB4 tyrosine kinase receptor.
CC       Binding results in ligand-stimulated tyrosine phosphorylation and
CC       activation of the receptor. Does not bind to the EGF receptor,
CC       ERBB2 or ERBB3 receptors. {ECO:0000269|PubMed:9275162}.
CC   -!- SUBUNIT: Interacts with ERBB4. {ECO:0000269|PubMed:9275162}.
CC   -!- SUBCELLULAR LOCATION: Pro-neuregulin-3, 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-3: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in sympathetic, motor, and sensory
CC       neurons.
CC   -!- DEVELOPMENTAL STAGE: Detected as early as 11 dpc. At 13 dpc
CC       detected mainly in the nervous system. At 16 dpc, detected in the
CC       brain, spinal cord, trigeminal, vestibular-cochlear, and spinal
CC       ganglia. In adults, expressed in spinal cord, and numerous brain
CC       regions.
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. {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- PTM: Extensive glycosylation precedes the proteolytic cleavage.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the neuregulin family. {ECO:0000305}.
DR   EMBL; AF010130; AAB70914.1; -; mRNA.
DR   CCDS; CCDS26954.1; -.
DR   PIR; T44447; T44447.
DR   RefSeq; NP_032760.1; NM_008734.3.
DR   UniGene; Mm.258705; -.
DR   ProteinModelPortal; O35181; -.
DR   SMR; O35181; -.
DR   STRING; 10090.ENSMUSP00000136884; -.
DR   iPTMnet; O35181; -.
DR   PhosphoSitePlus; O35181; -.
DR   PaxDb; O35181; -.
DR   PRIDE; O35181; -.
DR   Ensembl; ENSMUST00000166968; ENSMUSP00000136884; ENSMUSG00000041014.
DR   GeneID; 18183; -.
DR   KEGG; mmu:18183; -.
DR   UCSC; uc007tbz.2; mouse.
DR   CTD; 10718; -.
DR   MGI; MGI:1097165; Nrg3.
DR   eggNOG; ENOG410IMQB; Eukaryota.
DR   eggNOG; ENOG4111KAZ; LUCA.
DR   GeneTree; ENSGT00940000156754; -.
DR   HOVERGEN; HBG006532; -.
DR   InParanoid; O35181; -.
DR   KO; K05457; -.
DR   OrthoDB; 583156at2759; -.
DR   PhylomeDB; O35181; -.
DR   TreeFam; TF336537; -.
DR   Reactome; R-MMU-1227986; Signaling by ERBB2.
DR   Reactome; R-MMU-1236394; Signaling by ERBB4.
DR   Reactome; R-MMU-1250196; SHC1 events in ERBB2 signaling.
DR   Reactome; R-MMU-1250342; PI3K events in ERBB4 signaling.
DR   Reactome; R-MMU-1250347; SHC1 events in ERBB4 signaling.
DR   Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-MMU-1963640; GRB2 events in ERBB2 signaling.
DR   Reactome; R-MMU-1963642; PI3K events in ERBB2 signaling.
DR   Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-MMU-6785631; ERBB2 Regulates Cell Motility.
DR   Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-MMU-8847993; ERBB2 Activates PTK6 Signaling.
DR   Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling.
DR   PRO; PR:O35181; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   Bgee; ENSMUSG00000041014; Expressed in 93 organ(s), highest expression level in brain.
DR   ExpressionAtlas; O35181; baseline and differential.
DR   Genevisible; O35181; MM.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
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:0045499; F:chemorepellent activity; IDA:MGI.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0021842; P:chemorepulsion involved in interneuron migration from the subpallium to the cortex; IMP:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
DR   GO; GO:0030879; P:mammary gland development; IDA:MGI.
DR   GO; GO:0060596; P:mammary placode formation; IMP:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR   GO; GO:2001223; P:negative regulation of neuron migration; IDA:MGI.
DR   GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR040180; Neuregulin.
DR   PANTHER; PTHR11100; PTHR11100; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Disulfide bond; EGF-like domain;
KW   Growth factor; Membrane; Reference proteome; Secreted; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    713       Pro-neuregulin-3, membrane-bound isoform.
FT                                /FTId=PRO_0000019483.
FT   CHAIN         1    361       Neuregulin-3.
FT                                /FTId=PRO_0000019484.
FT   TOPO_DOM      1    362       Extracellular. {ECO:0000255}.
FT   TRANSMEM    363    383       Helical; Note=Internal signal sequence.
FT                                {ECO:0000255}.
FT   TOPO_DOM    384    713       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      288    331       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS     13     21       Poly-Ala.
FT   COMPBIAS     26     34       Poly-Ala.
FT   COMPBIAS    105    287       Ser/Thr-rich.
FT   COMPBIAS    127    135       Poly-Thr.
FT   COMPBIAS    250    253       Poly-Ala.
FT   COMPBIAS    254    263       Poly-Ser.
FT   COMPBIAS    264    267       Poly-Thr.
FT   DISULFID    292    306       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    300    319       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    321    330       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   713 AA;  77370 MW;  9F7D1D5E7FC8DCF0 CRC64;
     MSEGAAGASP PGAASAAAAS AEEGTAAAAA AAAAGGGPDG GGEGAAEPPR ELRCSDCIVW
     NRQQTWLCVV PLFIGFIGLG LSLMLLKWIV VGSVKEYVPT DLVDSKGMGQ DPFFLSKPSS
     FPKAMETTTT TTSTTSPATP SAGGAASSRT PNRISTRLTT ITRAPTRFPG HRVPIRASPR
     STTARNTAAP PTVLSTTAPF FSSSTPGSRP PMPGAPSTQA MPSWPTAAYA TSSYLHDSTP
     SWTLSPFQDA AAASSSSPSS TSSTTTTPET STSPKFHTTT YSTERSEHFK PCRDKDLAYC
     LNDGECFVIE TLTGSHKHCR CKEGYQGVRC DQFLPKTDSI LSDPTDHLGI EFMESEDVYQ
     RQVLSISCII FGIVIVGMFC AAFYFKSKKQ AKQIQEHLKE SQNGKNYSLK ASSTKSESLM
     KSHVHLQNYS KADRHPVTAL EKIMESSFSA PQSFPEVTSP DRGSQPIKHH SPGQRSGMLH
     RNTFRRAPPS PRSRLGGIVG PAYQQLEESR IPDQDTIPCQ GIEVRKTISH LPIQLWCVER
     PLDLKYVSNG LRTQQNASIN MQLPSRETNP YFNSLDQKDL VGYLSPRANS VPIIPSMGLE
     ETCMQMPGIS DVKSIKWCKN SYSADIVNAS MPVSDCLLEE QQEVKILLET VQEQIRILTD
     ARRSEDFELA SMETEDSASE NTAFLPLSPT AKSEREAQFV LRNEIQRDSV LTK
//
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