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O08680

- EPHA3_RAT

UniProt

O08680 - EPHA3_RAT

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Protein

Ephrin type-A receptor 3

Gene

Epha3

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei654 – 6541ATPPROSITE-ProRule annotation
Active sitei747 – 7471Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi629 – 6346ATPPROSITE-ProRule annotation
Nucleotide bindingi701 – 7077ATPPROSITE-ProRule annotation
Nucleotide bindingi751 – 7522ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. GPI-linked ephrin receptor activity Source: UniProtKB

GO - Biological processi

  1. cell migration Source: UniProtKB
  2. ephrin receptor signaling pathway Source: UniProtKB
  3. fasciculation of motor neuron axon Source: UniProtKB
  4. fasciculation of sensory neuron axon Source: UniProtKB
  5. fever generation Source: RGD
  6. regulation of actin cytoskeleton organization Source: UniProtKB
  7. regulation of epithelial to mesenchymal transition Source: UniProtKB
  8. regulation of focal adhesion assembly Source: UniProtKB
  9. regulation of microtubule cytoskeleton organization Source: UniProtKB
  10. regulation of Rho GTPase activity Source: UniProtKB
  11. response to cytokine Source: RGD
  12. response to lipopolysaccharide Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-A receptor 3 (EC:2.7.10.1)
Alternative name(s):
EPH-like kinase 4
Short name:
EK4
Short name:
rEK4
Tyrosine-protein kinase TYRO4
Gene namesi
Name:Epha3
Synonyms:Rek4, Tyro4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi68389. Epha3.

Subcellular locationi

GO - Cellular componenti

  1. early endosome Source: UniProtKB
  2. integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020By similarityAdd
BLAST
Chaini21 – 984964Ephrin type-A receptor 3PRO_0000016804Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi493 – 4931N-linked (GlcNAc...)Sequence Analysis
Modified residuei597 – 5971Phosphotyrosine; by autocatalysisBy similarity
Modified residuei603 – 6031Phosphotyrosine; by autocatalysisBy similarity
Modified residuei702 – 7021Phosphotyrosine; by autocatalysisBy similarity
Modified residuei780 – 7801Phosphotyrosine; by autocatalysisBy similarity
Modified residuei938 – 9381PhosphotyrosineBy similarity

Post-translational modificationi

Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-603 mediates interaction with NCK1. Dephosphorylated by PTPN1 (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO08680.
PRIDEiO08680.

PTM databases

PhosphoSiteiO08680.

Expressioni

Tissue specificityi

Most abundant in the heart, brain and lung.

Inductioni

Down-regulated by IL1-beta in neonatal cardiac myocytes.

Gene expression databases

GenevestigatoriO08680.

Interactioni

Subunit structurei

Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses. Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function. Interacts (phosphorylated) with PTPN1; dephosphorylates EPHA3 and may regulate its trafficking and function. Interacts (phosphorylated) with CRK; mediates EFNA5-EPHA3 signaling through RHOA GTPase activation. Interacts with NCK1 (via SH2 domain); mediates EFNA5-EPHA3 signaling (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000043263.

Structurei

3D structure databases

ProteinModelPortaliO08680.
SMRiO08680. Positions 29-203, 614-907.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 541521ExtracellularSequence AnalysisAdd
BLAST
Topological domaini566 – 984419CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei542 – 56524HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 207179Eph LBDPROSITE-ProRule annotationAdd
BLAST
Domaini325 – 435111Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini436 – 53297Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini622 – 883262Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini912 – 97665SAMPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi982 – 9843PDZ-bindingSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi189 – 322134Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiO08680.
KOiK05104.
PhylomeDBiO08680.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProiIPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamiPF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07699. GCC2_GCC3. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS01186. EGF_2. 1 hit.
PS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O08680-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDCHLSILIL FGCCVLSCSR ELSPQPSNEV NLLDSKTIQG ELGWISYPSH
60 70 80 90 100
GWEEISGVDE HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK
110 120 130 140 150
FTLRDCNSIP LVLGTCKETF NLYYMESDDD HGVKFLEHQF TKIDTIAADE
160 170 180 190 200
SFTQMDLGDR ILKLNTEIRE VGPVNKKGFY LAFQDVGACV ALVSVRVYFK
210 220 230 240 250
KCPFTVKNLA MFPDTVPMDS QSLVEVRGSC VNNSKEEDPP RMYCSTEGEW
260 270 280 290 300
LVPIGKCTCN AGYEERGFIC QACRPGFYKA LDGVAKCTKC PPHSSTQEDG
310 320 330 340 350
SMNCRCENNY FRAEKDPPSM ACTRPPSAPR NVISNINETS VILDWSWPLD
360 370 380 390 400
TGGRKDITFN IICKKCGWNV RQCEPCSPNV RFLPRQLGLT NTTVTVTDLL
410 420 430 440 450
AHTNYTFEID AINGVSELSS PPRQFAAVSI TTNQAAPSPV MTIKKDRTSR
460 470 480 490 500
NSISLSWQEP EHPNGIILDY EVKYYEKQEQ ETSYTILRAR GTNVTISSLK
510 520 530 540 550
PDTTYVFQIR ARTAAGYGTN SRKFEFENSP DSFSISGENS HVVMIAISAA
560 570 580 590 600
VAIIVLTVVT YVLVGRFCGY HKSKHSSDEK RLHFGNGHLR LPGLRTYVDP
610 620 630 640 650
HTYEDPTQAV HEFAKELDAT NIAIDKVVGA GEFGEVCSGR LKLPSKKEIS
660 670 680 690 700
VAIKTLKVGY TEKQRRDFLG EASIMGQFDH PNIIRLEGVV TKSKPVMIVT
710 720 730 740 750
EYMENGSLDS FLRKHDAQFT VIQLVGMLRG IASGMKYLSD MGYVHRDLAA
760 770 780 790 800
RNILINSNLV CKVSDFGLSR VLEDDPEAAY TTRGGKIPVR WTSPEATAYR
810 820 830 840 850
KFTSASDVWS YGIVLWEVMS YGERPYWEMS NQDVIKAVDE GYRLPLPMDC
860 870 880 890 900
PAALYQLMLD CWQKDRNNRP KFEQIVSILD KLIRNPGSLK IITSAAARPS
910 920 930 940 950
NLLLDQSNVD IATFHTTGDW LNGMRTAHCK EIFTGVEYSS CDTIAKISTD
960 970 980
DMKKVGVTVV GPQKKIISSI KALETQSKNG PVPV
Length:984
Mass (Da):110,228
Last modified:July 1, 1997 - v1
Checksum:iF170C49312F7A0AB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U69278 mRNA. Translation: AAC06273.1.
PIRiPT0186.
RefSeqiNP_113752.1. NM_031564.1.
UniGeneiRn.10713.

Genome annotation databases

GeneIDi29210.
KEGGirno:29210.
UCSCiRGD:68389. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U69278 mRNA. Translation: AAC06273.1 .
PIRi PT0186.
RefSeqi NP_113752.1. NM_031564.1.
UniGenei Rn.10713.

3D structure databases

ProteinModelPortali O08680.
SMRi O08680. Positions 29-203, 614-907.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000043263.

PTM databases

PhosphoSitei O08680.

Proteomic databases

PaxDbi O08680.
PRIDEi O08680.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29210.
KEGGi rno:29210.
UCSCi RGD:68389. rat.

Organism-specific databases

CTDi 2042.
RGDi 68389. Epha3.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233856.
HOVERGENi HBG062180.
InParanoidi O08680.
KOi K05104.
PhylomeDBi O08680.

Enzyme and pathway databases

BRENDAi 2.7.10.1. 5301.

Miscellaneous databases

NextBioi 608380.
PROi O08680.

Gene expression databases

Genevestigatori O08680.

Family and domain databases

Gene3Di 1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProi IPR027936. Eph_TM.
IPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_N_dom.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR011510. SAM_2.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view ]
Pfami PF14575. EphA2_TM. 1 hit.
PF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07699. GCC2_GCC3. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF07647. SAM_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEi PS01186. EGF_2. 1 hit.
PS51550. EPH_LBD. 1 hit.
PS50853. FN3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "IL-1 beta alters the expression of the receptor tyrosine kinase gene r-EphA3 in neonatal rat cardiomyocytes."
    Li Y.Y., McTiernan C.F., Feldman A.M.
    Am. J. Physiol. 274:H331-H341(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.

Entry informationi

Entry nameiEPHA3_RAT
AccessioniPrimary (citable) accession number: O08680
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: October 1, 2014
This is version 133 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3