NRG3_MOUSE
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 03-AUG-2022, entry version 166.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., Hillan K.,
RA Crowley C., Brush J., Godowski P.J.;
RT "Neuregulin-3 (NRG3): a novel neural tissue-enriched protein that binds and
RT activates ErbB4.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9562-9567(1997).
CC -!- FUNCTION: Direct ligand for the ERBB4 tyrosine kinase receptor. Binding
CC results in ligand-stimulated tyrosine phosphorylation and activation of
CC the receptor. Does not bind to the EGF receptor, ERBB2 or ERBB3
CC receptors. {ECO:0000269|PubMed:9275162}.
CC -!- SUBUNIT: Interacts with ERBB4. {ECO:0000269|PubMed:9275162}.
CC -!- SUBCELLULAR LOCATION: [Pro-neuregulin-3, membrane-bound isoform]: Cell
CC 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 detected
CC mainly in the nervous system. At 16 dpc, detected in the brain, spinal
CC cord, trigeminal, vestibular-cochlear, and spinal ganglia. In adults,
CC expressed in spinal cord, and numerous brain regions.
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 (By
CC 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 external
CC face leads to the release of the soluble growth factor form.
CC {ECO:0000250}.
CC -!- PTM: Extensive glycosylation precedes the proteolytic cleavage.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neuregulin family. {ECO:0000305}.
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DR EMBL; AF010130; AAB70914.1; -; mRNA.
DR CCDS; CCDS26954.1; -.
DR PIR; T44447; T44447.
DR RefSeq; NP_032760.1; NM_008734.3.
DR AlphaFoldDB; O35181; -.
DR SMR; O35181; -.
DR STRING; 10090.ENSMUSP00000136884; -.
DR iPTMnet; O35181; -.
DR PhosphoSitePlus; O35181; -.
DR PaxDb; O35181; -.
DR PRIDE; O35181; -.
DR Antibodypedia; 30013; 226 antibodies from 36 providers.
DR DNASU; 18183; -.
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 VEuPathDB; HostDB:ENSMUSG00000041014; -.
DR eggNOG; ENOG502QS97; Eukaryota.
DR GeneTree; ENSGT00940000156754; -.
DR InParanoid; O35181; -.
DR OMA; QSYSKAE; -.
DR OrthoDB; 583156at2759; -.
DR PhylomeDB; O35181; -.
DR TreeFam; TF336537; -.
DR BioGRID-ORCS; 18183; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Nrg3; mouse.
DR PRO; PR:O35181; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O35181; protein.
DR Bgee; ENSMUSG00000041014; Expressed in lateral mesenchyme derived from mesoderm and 87 other tissues.
DR ExpressionAtlas; O35181; baseline and differential.
DR Genevisible; O35181; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
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:0048018; F:receptor ligand activity; IPI:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR GO; GO:0021842; P:chemorepulsion involved in interneuron migration from the subpallium to the cortex; IMP:MGI.
DR GO; GO:0038130; P:ERBB4 signaling pathway; IPI:MGI.
DR GO; GO:0038138; P:ERBB4-ERBB4 signaling pathway; IPI: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; IPR000742; EGF-like_dom.
DR InterPro; IPR040180; Neuregulin.
DR PANTHER; PTHR11100; PTHR11100; 2.
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; Disulfide bond; EGF-like domain; Growth factor; Membrane;
KW Reference proteome; Secreted; Transmembrane; Transmembrane helix.
FT CHAIN 1..713
FT /note="Pro-neuregulin-3, membrane-bound isoform"
FT /id="PRO_0000019483"
FT CHAIN 1..361
FT /note="Neuregulin-3"
FT /id="PRO_0000019484"
FT TOPO_DOM 1..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical; Note=Internal signal sequence"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 288..331
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 28..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 292..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 300..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 321..330
FT /evidence="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
