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Protein

Ephrin type-A receptor 7

Gene

Epha7

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

Functioni

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 EPHA7.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei665ATPPROSITE-ProRule annotation1
Active sitei758Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi639 – 647ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • axon guidance receptor activity Source: UniProtKB
  • chemorepellent activity Source: UniProtKB
  • ephrin receptor activity Source: RGD
  • ephrin receptor binding Source: RGD
  • GPI-linked ephrin receptor activity Source: UniProtKB
  • protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis, Neurogenesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.
ReactomeiR-RNO-2682334. EPH-Ephrin signaling.
R-RNO-3928663. EPHA-mediated growth cone collapse.
R-RNO-3928665. EPH-ephrin mediated repulsion of cells.

Names & Taxonomyi

Protein namesi
Recommended name:
Ephrin type-A receptor 7 (EC:2.7.10.1)
Alternative name(s):
EPH homology kinase 3
Short name:
EHK-3
Gene namesi
Name:Epha7
Synonyms:Ehk-3, Ehk3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi70957. Epha7.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 555ExtracellularSequence analysisAdd BLAST528
Transmembranei556 – 576HelicalSequence analysisAdd BLAST21
Topological domaini577 – 998CytoplasmicSequence analysisAdd BLAST422

GO - Cellular componenti

  • dendrite Source: RGD
  • integral component of plasma membrane Source: InterPro
  • neuromuscular junction Source: RGD
  • neuronal cell body Source: RGD
  • postsynaptic membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000001682028 – 998Ephrin type-A receptor 7Add BLAST971

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi343N-linked (GlcNAc...)Sequence analysis1
Glycosylationi410N-linked (GlcNAc...)Sequence analysis1
Modified residuei608Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei614Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei791Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei940Phosphotyrosine; by autocatalysisSequence analysis1

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP54759.
PRIDEiP54759.

PTM databases

iPTMnetiP54759.
PhosphoSitePlusiP54759.

Expressioni

Tissue specificityi

Restricted to the nervous system.

Gene expression databases

BgeeiENSRNOG00000007030.
GenevisibleiP54759. RN.

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

GO - Molecular functioni

  • ephrin receptor binding Source: RGD

Protein-protein interaction databases

IntActiP54759. 3 interactors.
STRINGi10116.ENSRNOP00000009899.

Structurei

3D structure databases

ProteinModelPortaliP54759.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 210Eph LBDPROSITE-ProRule annotationAdd BLAST179
Domaini331 – 441Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini442 – 537Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST96
Domaini633 – 894Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini923 – 987SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi996 – 998PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi192 – 328Cys-richAdd BLAST137

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

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54759.
KOiK05108.
OMAiTRHPSWI.
OrthoDBiEOG091G00W0.
PhylomeDBiP54759.
TreeFamiTF315608.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
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.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 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. 1 hit.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: P54759-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVVQTRYPSW IILCYIWLLG FAHTGEAQAA KEVLLLDSKA QQTELEWISS
60 70 80 90 100
PPSGWEEISG LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV
110 120 130 140 150
ELKFTLRDCN SLPGVLGTCK ETFNLYYYET DYDTGRNIRE NLYVKIDTIA
160 170 180 190 200
ADESFTQGDL GERKMKLNTE VREIGPLSKK GFYLAFQDVG ACIALVSVKV
210 220 230 240 250
YYKKCWSIIE NLAVFPDTVT GSEFSSLVEV RGTCVSSAEE EAENSPRMHC
260 270 280 290 300
SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RRFYKSSSQD LQCSRCPTHS
310 320 330 340 350
FSDREGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE
360 370 380 390 400
WSPPADNGGR NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV
410 420 430 440 450
TVMDLLAHAN YTFEVEAVNG VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM
460 470 480 490 500
KERVLQRSVE LSWQEPEHPN GVITEYEIKY YEKDQRERTY STLKTKSTSA
510 520 530 540 550
SINNLKPGTV YVFQIRAFTA AGYGNYSPRL DVATLEEASG KMFEATAVSS
560 570 580 590 600
EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF
610 620 630 640 650
KFPGTKTYID PETYEDPNRA VHQFAKELDA SCIKIERVIG AGEFGEVCSG
660 670 680 690 700
RLKLPGKRDV AVAIKTLKVG YTEKQRRDFL CEASIMGQFD HPNVVHLEGV
710 720 730 740 750
VTRGKPVMIV IEFMENGALD AFLRKHDGQF TVIQLVGMLR GIAAGMRYLA
760 770 780 790 800
DMGYVHRDLA ARNILVNSNL VCKVSDFGLS RVIEDDPEAV YTTTGGKIPV
810 820 830 840 850
RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM SNQDVIKAIE
860 870 880 890 900
EGYRLPAPMD CPAGLHQLML DCWQKERAER PKFEQIVGIL DKMIRNPSSL
910 920 930 940 950
KTPLGTCSRP ISPLLDQSTP DFTAFCSVGE WLQAIKMERY KDNFTAAGYN
960 970 980 990
SLESVARMTI DDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV
Note: More widely expressed in the embryo.
Length:998
Mass (Da):111,953
Last modified:October 1, 1996 - v1
Checksum:iA7A82A698924876C
GO
Isoform Short (identifier: P54759-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     600-610: FKFPGTKTYID → SLVTNEHLSVL

Note: Lacks the kinase domain.
Show »
Length:998
Mass (Da):111,848
Checksum:iB87536EA0D7CB919
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003012600 – 610FKFPGTKTYID → SLVTNEHLSVL in isoform Short. 1 PublicationAdd BLAST11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21954 mRNA. Translation: AAA86830.1.
U21955 mRNA. Translation: AAA86831.1.
RefSeqiNP_599158.1. NM_134331.1. [P54759-1]
XP_006238026.1. XM_006237964.3.
UniGeneiRn.10181.

Genome annotation databases

EnsembliENSRNOT00000009899; ENSRNOP00000009899; ENSRNOG00000007030. [P54759-1]
GeneIDi171287.
KEGGirno:171287.
UCSCiRGD:70957. rat. [P54759-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U21954 mRNA. Translation: AAA86830.1.
U21955 mRNA. Translation: AAA86831.1.
RefSeqiNP_599158.1. NM_134331.1. [P54759-1]
XP_006238026.1. XM_006237964.3.
UniGeneiRn.10181.

3D structure databases

ProteinModelPortaliP54759.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP54759. 3 interactors.
STRINGi10116.ENSRNOP00000009899.

PTM databases

iPTMnetiP54759.
PhosphoSitePlusiP54759.

Proteomic databases

PaxDbiP54759.
PRIDEiP54759.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009899; ENSRNOP00000009899; ENSRNOG00000007030. [P54759-1]
GeneIDi171287.
KEGGirno:171287.
UCSCiRGD:70957. rat. [P54759-1]

Organism-specific databases

CTDi2045.
RGDi70957. Epha7.

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiP54759.
KOiK05108.
OMAiTRHPSWI.
OrthoDBiEOG091G00W0.
PhylomeDBiP54759.
TreeFamiTF315608.

Enzyme and pathway databases

BRENDAi2.7.10.1. 5301.
ReactomeiR-RNO-2682334. EPH-Ephrin signaling.
R-RNO-3928663. EPHA-mediated growth cone collapse.
R-RNO-3928665. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

PROiP54759.

Gene expression databases

BgeeiENSRNOG00000007030.
GenevisibleiP54759. RN.

Family and domain databases

CDDicd00063. FN3. 2 hits.
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. FN3_dom.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
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.
PF07714. Pkinase_Tyr. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00615. EPH_lbd. 1 hit.
SM01411. Ephrin_rec_like. 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. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiEPHA7_RAT
AccessioniPrimary (citable) accession number: P54759
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 164 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

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 one 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.