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Reviewed, UniProtKB/Swiss-Prot Q62799 (ERBB3_RAT)

Last modified February 9, 2010. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Receptor tyrosine-protein kinase erbB-3
    EC=2.7.10.1
Alternative name(s):
    c-erbB-3
Gene names
Name: Erbb3
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length1339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Binds and is activated by neuregulins and NTAK. May also be activated by CSPG5.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Heterodimer with each of the other ERBB receptors Potential. Interacts with CSPG5, PA2G4 and MUC1 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Domain

The cytoplasmic part of the receptor may interact with the SH2 or SH3 domains of many signal-transducing proteins.

Post-translational modification

Ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.

Contains 1 protein kinase domain.

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Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Gene Ontology (GO)
   Biological processaxonogenesis Ref.3

Inferred from expression pattern. Source: RGD

cellular response to insulin stimulus

Inferred from expression pattern. Source: RGD

circadian rhythm

Inferred from expression pattern. Source: RGD

mammary gland involution

Inferred from expression pattern. Source: RGD

odontogenesis

Inferred from expression pattern. Source: RGD

positive regulation of glucose import

Inferred from mutant phenotype. Source: RGD

protein amino acid phosphorylation

Inferred from electronic annotation. Source: InterPro

response to drug

Inferred from expression pattern. Source: RGD

response to wounding Ref.3

Inferred from expression pattern. Source: RGD

skeletal muscle tissue development

Inferred from expression pattern. Source: RGD

tongue development

Inferred from expression pattern. Source: RGD

transmembrane receptor protein tyrosine kinase signaling pathway Ref.3

Traceable author statement. Source: RGD

   Cellular componentintegral to membrane Ref.3

Traceable author statement. Source: RGD

nucleus

Inferred from direct assay. Source: RGD

postsynaptic membrane

Inferred from direct assay. Source: RGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

receptor signaling protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

transmembrane receptor protein tyrosine kinase activity Ref.3

Traceable author statement. Source: RGD

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 13391320Receptor tyrosine-protein kinase erbB-3
PRO_0000016673

Regions

Topological domain20 – 643624Extracellular Potential
Transmembrane644 – 66219 Potential
Topological domain663 – 1339677Cytoplasmic Potential
Domain707 – 964258Protein kinase
Nucleotide binding713 – 7219ATP By similarity
Compositional bias183 – 25977Cys-rich

Sites

Active site8321Proton acceptor By similarity
Binding site7401ATP By similarity

Amino acid modifications

Modified residue6781Phosphotyrosine By similarity
Modified residue6841Phosphoserine By similarity
Modified residue13251Phosphotyrosine By similarity
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Glycosylation4081N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Glycosylation4371N-linked (GlcNAc...) Potential
Glycosylation4691N-linked (GlcNAc...) Potential
Glycosylation5221N-linked (GlcNAc...) Potential
Glycosylation5661N-linked (GlcNAc...) Potential
Glycosylation6161N-linked (GlcNAc...) Potential
Disulfide bond186 ↔ 194 By similarity
Disulfide bond190 ↔ 202 By similarity
Disulfide bond210 ↔ 218 By similarity
Disulfide bond214 ↔ 226 By similarity
Disulfide bond227 ↔ 235 By similarity
Disulfide bond231 ↔ 243 By similarity
Disulfide bond246 ↔ 255 By similarity
Disulfide bond259 ↔ 286 By similarity
Disulfide bond290 ↔ 301 By similarity
Disulfide bond305 ↔ 320 By similarity
Disulfide bond323 ↔ 327 By similarity
Disulfide bond500 ↔ 509 By similarity
Disulfide bond504 ↔ 517 By similarity
Disulfide bond520 ↔ 529 By similarity
Disulfide bond533 ↔ 549 By similarity
Disulfide bond556 ↔ 573 By similarity
Disulfide bond576 ↔ 585 By similarity
Disulfide bond589 ↔ 610 By similarity
Disulfide bond613 ↔ 621 By similarity
Disulfide bond617 ↔ 629 By similarity

Experimental info

Sequence conflict10281L → P in AAC53050. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Q62799-1 [UniParc].

Last modified June 6, 2002. Version 3.
Checksum: 0AA5F2402BBFDF1E

FASTA1,339147,546
        10         20         30         40         50         60 
MRATGTLQVL CFLLSLARGS EMGNSQAVCP GTLNGLSVTG DADNQYQTLY KLYEKCEVVM 

        70         80         90        100        110        120 
GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSVLPLP NLRVVRGTQV YDGKFAIFVM 

       130        140        150        160        170        180 
LNYNTNSSHA LRQLKFTQLT EILSGGVYIE KNDKLCHMDT IDWRDIVRVR GAEIVVKNNG 

       190        200        210        220        230        240 
ANCPPCHEVC KGRCWGPGPD DCQILTKTIC APQCNGRCFG PNPNQCCHDE CAGGCSGPQD 

       250        260        270        280        290        300 
TDCFACRRFN DSGACVPRCP EPLVYNKLTF QLEPNPHTKY QYGGVCVASC PHNFVVDQTF 

       310        320        330        340        350        360 
CVRACPPDKM EVDKHGLKMC EPCGGLCPKA CEGTGSGSRY QTVDSSNIDG FVNCTKILGN 

       370        380        390        400        410        420 
LDFLITGLNV DPWHKIPALD PEKLNVFRTV REITGYLNIQ SWPPHMHNFS VFSNLTTIGG 

       430        440        450        460        470        480 
RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS AGRVYISANQ QLCYHHSLNW TRLLRGPSEE 

       490        500        510        520        530        540 
RLDIKYDRPL GECLAEGKVC DPLCSSGGCW GPGPGQCLSC RNYSREGVCV THCNFLQGEP 

       550        560        570        580        590        600 
REFVHEAQCF SCHPECLPME GTSTCNGSGS DACARCAHFR DGPHCVNSCP HGILGAKGPI 

       610        620        630        640        650        660 
YKYPDAQNEC RPCHENCTQG CNGPELQDCL GQAEVLMSKP HLVIAVTVGL AVILMILGGS 

       670        680        690        700        710        720 
FLYWRGRRIQ NKRAMRRYLE RGESIEPLDP SEKANKVLAR IFKETELRKL KVLGSGVFGT 

       730        740        750        760        770        780 
VHKGIWIPEG ESIKIPVCIK VIEDKSGRQS FQAVTDHMLA VGSLDHAHIV RLLGLCPGSS 

       790        800        810        820        830        840 
LQLVTQYLPL GSLLDHVKQH RETLGPQLLL NWGVQIAKGM YYLEEHSMVH RDLALRNVML 

       850        860        870        880        890        900 
KSPSQVQVAD FGVADLLPPD DKQLLHSEAK TPIKWMALES IHFGKYTHQS DVWSYGVTVW 

       910        920        930        940        950        960 
ELMTFGAEPY AGLRLAEIPD LLEKGERLAQ PQICTIDVYM VMVKCWMIDE NIRPTFKELA 

       970        980        990       1000       1010       1020 
NEFTRMARDP PRYLVIKRAS GPGTPPAAEP SVLTTKELQE AELEPELDLD LDLEAEEEGL 

      1030       1040       1050       1060       1070       1080 
ATSLGSALSL PTGTLTRPRG SQSLLSPSSG YMPMNQSSLG EACLDSAVLG GREQFSRPIS 

      1090       1100       1110       1120       1130       1140 
LHPIPRGRPA SESSEGHVTG SEAELQEKVS VCRSRSRSRS PRPRGDSAYH SQRHSLLTPV 

      1150       1160       1170       1180       1190       1200 
TPLSPPGLEE EDGNGYVMPD THLRGASSSR EGTLSSVGLS SVLGTEEEDE DEEYEYMNRK 

      1210       1220       1230       1240       1250       1260 
RRGSPPRPPR PGSLEELGYE YMDVGSDLSA SLGSTQSCPL HPMAIVPSAG TTPDEDYEYM 

      1270       1280       1290       1300       1310       1320 
NRRRGAGGAG GDYAAMGACP AAEQGYEEMR AFQGPGHHAP HVRYARLKTL RSLEATDSAF 

      1330 
DNPDYWHSRL FPKANAQRT

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References

[1]"Cloning of the rat ErbB3 cDNA and characterization of the recombinant protein."
Hellyer N.J., Kim H.-H., Greaves C.H., Sierke S.L., Koland J.G.
Gene 165:279-284(1995) [PubMed: 8522190] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]Hellyer N.J., Koland J.G.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 85; 513 AND 565.
[3]"Expression of neuregulins and their putative receptors, ErbB2 and ErbB3, is induced during Wallerian degeneration."
Carroll S.L., Miller M.L., Frohnert P.W., Kim S.S., Corbett J.A.
J. Neurosci. 17:1642-1659(1997) [PubMed: 9030624] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 922-1097.
Strain: Sprague-Dawley.
Tissue: Sciatic nerve.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U29339 mRNA. Translation: AAC28498.2.
U52530 mRNA. Translation: AAC53050.1.
IPIIPI00208301.
PIRJC4387.
RefSeqNP_058914.2.
UniGeneRn.10228

3D structure databases

SMRQ62799. Positions 25-630, 665-716, 695-977, 702-1009.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ62799.

PTM databases

PhosphoSiteQ62799.

Proteomic databases

PRIDEQ62799.

Genome annotation databases

EnsemblENSRNOT00000006796; ENSRNOP00000006796; ENSRNOG00000004964; Rattus norvegicus. [Genome view]
GeneID29496.
KEGGrno:29496.
UCSCNM_017218. rat.

Organism-specific databases

CTD29496.
RGD69323. Erbb3.

Phylogenomic databases

eggNOGroNOG13529.
HOVERGENQ62799.
InParanoidQ62799.

Enzyme and pathway databases

BRENDA2.7.10.1. 248.

Gene expression databases

ArrayExpressQ62799.
GenevestigatorQ62799.
GermOnlineENSRNOG00000004964. Rattus norvegicus.

Family and domain databases

InterProIPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]
PANTHERPTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF00757. Furin-like. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000619. TyrPK_EGF-R. 1 hit.
SMARTSM00261. FU. 5 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio609384.

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Entry information

Entry nameERBB3_RAT
AccessionPrimary (citable) accession number: Q62799
Secondary accession number(s): Q62955
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 6, 2002
Last modified: February 9, 2010
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents