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Protein

Pro-neuregulin-3, membrane-bound isoform

Gene

Nrg3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Direct ligand for the ERBB4 tyrosine kinase receptor. Binding results in ligand-stimulated tyrosine phosphorylation and activation of the receptor. Does not bind to the EGF receptor, ERBB2 or ERBB3 receptors.1 Publication

GO - Molecular functioni

  1. receptor binding Source: GO_Central

GO - Biological processi

  1. intracellular signal transduction Source: MGI
  2. mammary gland development Source: MGI
  3. mammary placode formation Source: MGI
  4. pattern specification process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Names & Taxonomyi

Protein namesi
Recommended name:
Pro-neuregulin-3, membrane-bound isoform
Short name:
Pro-NRG3
Cleaved into the following chain:
Neuregulin-3
Short name:
NRG-3
Gene namesi
Name:Nrg3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1097165. Nrg3.

Subcellular locationi

Chain Pro-neuregulin-3, membrane-bound isoform : Cell membrane By similarity; Single-pass type I membrane protein By similarity
Note: Does not seem to be active.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 362362ExtracellularSequence AnalysisAdd
BLAST
Transmembranei363 – 38321Helical; Note=Internal signal sequenceSequence AnalysisAdd
BLAST
Topological domaini384 – 713330CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular space Source: GO_Central
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 713713Pro-neuregulin-3, membrane-bound isoformPRO_0000019483Add
BLAST
Chaini1 – 361361Neuregulin-3PRO_0000019484Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi292 ↔ 306PROSITE-ProRule annotation
Disulfide bondi300 ↔ 319PROSITE-ProRule annotation
Disulfide bondi321 ↔ 330PROSITE-ProRule annotation

Post-translational modificationi

Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form.By similarity
Extensive glycosylation precedes the proteolytic cleavage.By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiO35181.

PTM databases

PhosphoSiteiO35181.

Expressioni

Tissue specificityi

Expressed in sympathetic, motor, and sensory neurons.

Developmental stagei

Detected as early as 11 dpc. At 13 dpc detected mainly in the nervous system. At 16 dpc, detected in the brain, spinal cord, trigeminal, vestibular-cochlear, and spinal ganglia. In adults, expressed in spinal cord, and numerous brain regions.

Gene expression databases

BgeeiO35181.
CleanExiMM_NRG3.
ExpressionAtlasiO35181. baseline and differential.
GenevestigatoriO35181.

Interactioni

Subunit structurei

Interacts with ERBB4.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO35181.
SMRiO35181. Positions 288-335.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini288 – 33144EGF-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 219Poly-Ala
Compositional biasi26 – 349Poly-Ala
Compositional biasi105 – 287183Ser/Thr-richAdd
BLAST
Compositional biasi127 – 1359Poly-Thr
Compositional biasi250 – 2534Poly-Ala
Compositional biasi254 – 26310Poly-Ser
Compositional biasi264 – 2674Poly-Thr

Domaini

The cytoplasmic domain may be involved in the regulation of trafficking and proteolytic processing. Regulation of the proteolytic processing involves initial intracellular domain dimerization (By similarity).By similarity
ERBB receptor binding is elicited entirely by the EGF-like domain.By similarity

Sequence similaritiesi

Belongs to the neuregulin family.Curated
Contains 1 EGF-like domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG40523.
GeneTreeiENSGT00760000119412.
HOVERGENiHBG006532.
InParanoidiO35181.
KOiK05457.
OMAiKFRTTTY.
OrthoDBiEOG7SR4KZ.
PhylomeDBiO35181.
TreeFamiTF336537.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35181-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEGAAGASP PGAASAAAAS AEEGTAAAAA AAAAGGGPDG GGEGAAEPPR
60 70 80 90 100
ELRCSDCIVW NRQQTWLCVV PLFIGFIGLG LSLMLLKWIV VGSVKEYVPT
110 120 130 140 150
DLVDSKGMGQ DPFFLSKPSS FPKAMETTTT TTSTTSPATP SAGGAASSRT
160 170 180 190 200
PNRISTRLTT ITRAPTRFPG HRVPIRASPR STTARNTAAP PTVLSTTAPF
210 220 230 240 250
FSSSTPGSRP PMPGAPSTQA MPSWPTAAYA TSSYLHDSTP SWTLSPFQDA
260 270 280 290 300
AAASSSSPSS TSSTTTTPET STSPKFHTTT YSTERSEHFK PCRDKDLAYC
310 320 330 340 350
LNDGECFVIE TLTGSHKHCR CKEGYQGVRC DQFLPKTDSI LSDPTDHLGI
360 370 380 390 400
EFMESEDVYQ RQVLSISCII FGIVIVGMFC AAFYFKSKKQ AKQIQEHLKE
410 420 430 440 450
SQNGKNYSLK ASSTKSESLM KSHVHLQNYS KADRHPVTAL EKIMESSFSA
460 470 480 490 500
PQSFPEVTSP DRGSQPIKHH SPGQRSGMLH RNTFRRAPPS PRSRLGGIVG
510 520 530 540 550
PAYQQLEESR IPDQDTIPCQ GIEVRKTISH LPIQLWCVER PLDLKYVSNG
560 570 580 590 600
LRTQQNASIN MQLPSRETNP YFNSLDQKDL VGYLSPRANS VPIIPSMGLE
610 620 630 640 650
ETCMQMPGIS DVKSIKWCKN SYSADIVNAS MPVSDCLLEE QQEVKILLET
660 670 680 690 700
VQEQIRILTD ARRSEDFELA SMETEDSASE NTAFLPLSPT AKSEREAQFV
710
LRNEIQRDSV LTK
Length:713
Mass (Da):77,370
Last modified:December 31, 1997 - v1
Checksum:i9F7D1D5E7FC8DCF0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010130 mRNA. Translation: AAB70914.1.
CCDSiCCDS26954.1.
PIRiT44447.
RefSeqiNP_032760.1. NM_008734.3.
UniGeneiMm.258705.

Genome annotation databases

EnsembliENSMUST00000166968; ENSMUSP00000136884; ENSMUSG00000041014.
GeneIDi18183.
KEGGimmu:18183.
UCSCiuc007tbz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF010130 mRNA. Translation: AAB70914.1.
CCDSiCCDS26954.1.
PIRiT44447.
RefSeqiNP_032760.1. NM_008734.3.
UniGeneiMm.258705.

3D structure databases

ProteinModelPortaliO35181.
SMRiO35181. Positions 288-335.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiO35181.

Proteomic databases

PRIDEiO35181.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000166968; ENSMUSP00000136884; ENSMUSG00000041014.
GeneIDi18183.
KEGGimmu:18183.
UCSCiuc007tbz.2. mouse.

Organism-specific databases

CTDi10718.
MGIiMGI:1097165. Nrg3.

Phylogenomic databases

eggNOGiNOG40523.
GeneTreeiENSGT00760000119412.
HOVERGENiHBG006532.
InParanoidiO35181.
KOiK05457.
OMAiKFRTTTY.
OrthoDBiEOG7SR4KZ.
PhylomeDBiO35181.
TreeFamiTF336537.

Miscellaneous databases

NextBioi293498.
PROiO35181.
SOURCEiSearch...

Gene expression databases

BgeeiO35181.
CleanExiMM_NRG3.
ExpressionAtlasiO35181. baseline and differential.
GenevestigatoriO35181.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Neuregulin-3 (NRG3): a novel neural tissue-enriched protein that binds and activates ErbB4."
    Zhang D., Sliwkowski M.X., Mark M., Frantz G., Akita R., Sun Y., Hillan K., Crowley C., Brush J., Godowski P.J.
    Proc. Natl. Acad. Sci. U.S.A. 94:9562-9567(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ERBB4.
    Tissue: Brain.

Entry informationi

Entry nameiNRG3_MOUSE
AccessioniPrimary (citable) accession number: O35181
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2000
Last sequence update: December 31, 1997
Last modified: February 3, 2015
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.