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P54759 (EPHA7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ephrin type-A receptor 7
EC=2.7.10.1
Alternative name(s):
EPH homology kinase 3
Short name=EHK-3
Gene names
Name:Epha7
Synonyms:Ehk-3, Ehk3
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length998 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A 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. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 AND MAPK3 which are phosphorylated upon activation of EPHA7. Ref.2

Catalytic activity

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

Subunit structure

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 By similarity. Interacts (via PDZ-binding motif) with GRIP1 and PICK1 (via PDZ domain) By similarity.

Subcellular location

Cell membrane By similarity; Single-pass type I membrane protein By similarity.

Tissue specificity

Restricted to the nervous system.

Post-translational modification

Phosphorylated By similarity.

Sequence similarities

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

Contains 1 Eph LBD (Eph ligand-binding) domain.

Contains 2 fibronectin type-III domains.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
   Biological processApoptosis
Neurogenesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processbrain development

Inferred from sequence or structural similarity. Source: UniProtKB

branching morphogenesis of a nerve

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neuron apoptosis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell-cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentdendrite

Inferred from direct assay. Source: RGD

integral to plasma membrane

Inferred from electronic annotation. Source: InterPro

neuromuscular junction

Inferred from direct assay. Source: RGD

neuronal cell body

Inferred from direct assay. Source: RGD

postsynaptic membrane

Inferred from direct assay. Source: RGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GPI-linked ephrin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

axon guidance receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

chemorepellent activity

Inferred from sequence or structural similarity. Source: UniProtKB

ephrin receptor binding

Inferred from direct assay. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P54759-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: More widely expressed in the embryo.
Isoform Short (identifier: P54759-2)

The sequence of this isoform differs from the canonical sequence as follows:
     600-610: FKFPGTKTYID → SLVTNEHLSVL
Note: Lacks the kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 998971Ephrin type-A receptor 7
PRO_0000016820

Regions

Topological domain28 – 555528Extracellular Potential
Transmembrane556 – 57621Helical; Potential
Topological domain577 – 998422Cytoplasmic Potential
Domain32 – 210179Eph LBD
Domain331 – 433103Fibronectin type-III 1
Domain443 – 53593Fibronectin type-III 2
Domain633 – 894262Protein kinase
Domain923 – 98765SAM
Nucleotide binding639 – 6479ATP By similarity
Motif996 – 9983PDZ-binding Potential
Compositional bias192 – 328137Cys-rich

Sites

Active site7581Proton acceptor By similarity
Binding site6651ATP By similarity

Amino acid modifications

Modified residue6081Phosphotyrosine; by autocatalysis Potential
Modified residue6141Phosphotyrosine; by autocatalysis Potential
Modified residue7911Phosphotyrosine; by autocatalysis Potential
Modified residue9401Phosphotyrosine; by autocatalysis Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence600 – 61011FKFPGTKTYID → SLVTNEHLSVL in isoform Short.
VSP_003012

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A7A82A698924876C

FASTA998111,953
        10         20         30         40         50         60 
MVVQTRYPSW IILCYIWLLG FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPSGWEEISG 

        70         80         90        100        110        120 
LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK 

       130        140        150        160        170        180 
ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK 

       190        200        210        220        230        240 
GFYLAFQDVG ACIALVSVKV YYKKCWSIIE NLAVFPDTVT GSEFSSLVEV RGTCVSSAEE 

       250        260        270        280        290        300 
EAENSPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RRFYKSSSQD LQCSRCPTHS 

       310        320        330        340        350        360 
FSDREGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR 

       370        380        390        400        410        420 
NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG 

       430        440        450        460        470        480 
VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVE LSWQEPEHPN GVITEYEIKY 

       490        500        510        520        530        540 
YEKDQRERTY STLKTKSTSA SINNLKPGTV YVFQIRAFTA AGYGNYSPRL DVATLEEASG 

       550        560        570        580        590        600 
KMFEATAVSS EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF 

       610        620        630        640        650        660 
KFPGTKTYID PETYEDPNRA VHQFAKELDA SCIKIERVIG AGEFGEVCSG RLKLPGKRDV 

       670        680        690        700        710        720 
AVAIKTLKVG YTEKQRRDFL CEASIMGQFD HPNVVHLEGV VTRGKPVMIV IEFMENGALD 

       730        740        750        760        770        780 
AFLRKHDGQF TVIQLVGMLR GIAAGMRYLA DMGYVHRDLA ARNILVNSNL VCKVSDFGLS 

       790        800        810        820        830        840 
RVIEDDPEAV YTTTGGKIPV RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM 

       850        860        870        880        890        900 
SNQDVIKAIE EGYRLPAPMD CPAGLHQLML DCWQKERAER PKFEQIVGIL DKMIRNPSSL 

       910        920        930        940        950        960 
KTPLGTCSRP ISPLLDQSTP DFTAFCSVGE WLQAIKMERY KDNFTAAGYN SLESVARMTI 

       970        980        990 
DDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV

« Hide

Isoform Short [UniParc].

Checksum: B87536EA0D7CB919
Show »

FASTA998111,848

References

[1]"Identification of full-length and truncated forms of Ehk-3, a novel member of the Eph receptor tyrosine kinase family."
Valenzuela D.M., Rojas E., Griffiths J.A., Compton D.L., Gisser M., Ip N.Y., Goldfarb M., Yancopoulos G.D.
Oncogene 10:1573-1580(1995) [PubMed: 7731712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
[2]"Inhibition of EphA7 up-regulation after spinal cord injury reduces apoptosis and promotes locomotor recovery."
Figueroa J.D., Benton R.L., Velazquez I., Torrado A.I., Ortiz C.M., Hernandez C.M., Diaz J.J., Magnuson D.S., Whittemore S.R., Miranda J.D.
J. Neurosci. Res. 84:1438-1451(2006) [PubMed: 16983667] [Abstract]
Cited for: FUNCTION IN APOPTOSIS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U21954 mRNA. Translation: AAA86830.1.
U21955 mRNA. Translation: AAA86831.1.
IPIIPI00188223.
IPI00231026.
RefSeqNP_599158.1. NM_134331.1.
UniGeneRn.10181.

3D structure databases

ProteinModelPortalP54759.
SMRP54759. Positions 32-205, 607-899, 922-993.
ModBaseSearch...

Protein-protein interaction databases

IntActP54759. 3 interactions.
STRINGP54759.

PTM databases

PhosphoSiteP54759.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000009899; ENSRNOP00000009899; ENSRNOG00000007030.
ENSRNOT00000061033; ENSRNOP00000057749; ENSRNOG00000007030.
GeneID171287.
KEGGrno:171287.
UCSCNM_134331. rat.

Organism-specific databases

CTD2045.
RGD70957. Epha7.

Phylogenomic databases

eggNOGmaNOG08784.
GeneTreeENSGT00600000084150.
HOVERGENHBG062180.
InParanoidP54759.
OMAGYQQKGD.
OrthoDBEOG4H19TZ.
PhylomeDBP54759.

Enzyme and pathway databases

BRENDA2.7.10.1. 5301.

Gene expression databases

ArrayExpressP54759.
GenevestigatorP54759.
GermOnlineENSRNOG00000007030. Rattus norvegicus.

Family and domain databases

InterProIPR001090. Ephrin_rcpt_lig-bd.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 2 hits.
G3DSA:1.10.150.50. SAM_type. 1 hit.
KOK05108.
PfamPF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. FN_III-like. 2 hits.
SSF49785. Gal_bind_like. 1 hit.
SSF57184. Grow_fac_recept. 1 hit.
SSF56112. Kinase_like. 1 hit.
SSF47769. SAM_homology. 1 hit.
PROSITEPS01186. EGF_2. 1 hit. Uncertain.
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]
ProtoNetSearch...

Other

NextBio622031.

Entry information

Entry nameEPHA7_RAT
AccessionPrimary (citable) accession number: P54759
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 14, 2011
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents