Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ephrin type-A receptor 7

Gene

EPHA7

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei660ATPPROSITE-ProRule annotation1
Active sitei753Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi634 – 642ATPPROSITE-ProRule annotation9

GO - Molecular functioni

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. 1306.
ReactomeiR-GGA-2682334. EPH-Ephrin signaling.
R-GGA-3928663. EPHA-mediated growth cone collapse.
R-GGA-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-like kinase 11
Short name:
EK11
Short name:
cEK11
Tyrosine-protein kinase receptor CEPHA7
Gene namesi
Name:EPHA7
Synonyms:CEK11
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 3

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini28 – 550ExtracellularSequence analysisAdd BLAST523
Transmembranei551 – 571HelicalSequence analysisAdd BLAST21
Topological domaini572 – 993CytoplasmicSequence analysisAdd BLAST422

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_000001682128 – 993Ephrin type-A receptor 7Add BLAST966

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi343N-linked (GlcNAc...)Sequence analysis1
Glycosylationi410N-linked (GlcNAc...)Sequence analysis1
Modified residuei603Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei609Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei786Phosphotyrosine; by autocatalysisSequence analysis1
Modified residuei935Phosphotyrosine; by autocatalysisSequence analysis1

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO42422.

Expressioni

Developmental stagei

Within the nervous system, expression is restricted to prosomeres 1 and 2 in the diencephalon and all the rhombomeres in the hindbrain during segmentation stages. Later on, a superimposed pattern appears that correlates with the formation of several axonal tracts. In the somitic mesoderm, the expression correlates with segmentation and the guidance of both neural crest and motor axons through the sclerotomes.1 Publication

Gene expression databases

BgeeiENSGALG00000015593.

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).By similarity

Protein-protein interaction databases

STRINGi9031.ENSGALP00000025098.

Structurei

3D structure databases

ProteinModelPortaliO42422.
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
Domaini628 – 889Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini918 – 982SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi991 – 993PDZ-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.
InParanoidiO42422.
KOiK05108.
OMAiTRHPSWI.
OrthoDBiEOG091G00W0.
PhylomeDBiO42422.
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.
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.
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.

O42422-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLRSRLPPW IMLCSVWLLR FAHTGEAQAA KEVILLDSKA QQTELEWISS
60 70 80 90 100
PPNGWEEISG LDENYTPIRT YQVCQVMESN QNNWLRTNWI AKSNAQRIFV
110 120 130 140 150
ELKFTLRDCN SLPGVLGTCK ETFNLYYYET DYDTGRNIRE NQYVKIDTIA
160 170 180 190 200
ADESFTQGDL GERKMKLNTE VREIGPLSKK GFYLAFQDVG ACIALVSVKV
210 220 230 240 250
YYKKCWSIIE NLAIFPDTVT GSEFSSLVEV RGTCVSSAEE EAENSPKMHC
260 270 280 290 300
SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RGFYKSSSQD LQCSRCPTHS
310 320 330 340 350
FSDKEGSSRC DCEDSYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE
360 370 380 390 400
WSPPADNGGR NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLVDNYV
410 420 430 440 450
TVMDLLAHAN YTFEVEAVNG VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM
460 470 480 490 500
KERVLQRSVE LSWQEPEHPN GVITEYEIKY YEKDQRERTY STVKTKSTSA
510 520 530 540 550
SINNLKPGTV YVFQIRAFTA AGYGNYSPRL DVATLEEATA TAVSSEQNPV
560 570 580 590 600
IIIAVVAVAG TIILVFMVFG FIIGRRHCGY SKADQEGDEE LYFHFKFPGT
610 620 630 640 650
KTYIDPETYE DPNRAVHQFA KELDASCIKI ERVIGAGEFG EVCSGRLKLP
660 670 680 690 700
GKRDVAVAIK TLKVGYTEKQ RRDFLCEASI MGQFDHPNVV HLEGVVTRGK
710 720 730 740 750
PVMIVIEYME NGALDAFLRK HDGQFTVIQL VGMLRGIAAG MRYLADMGYV
760 770 780 790 800
HRDLAARNIL VNSNLVCKVS DFGLSRVIED DPEAVYTTTG GKIPVRWTAP
810 820 830 840 850
EAIQYRKFTS ASDVWSYGIV MWEVMSYGER PYWDMSNQDV IKAIEEGYRL
860 870 880 890 900
PAPMDCPAGL HQLMLDCWQK ERGERPKFEQ IVGILDKMIR NPNSLKTPLG
910 920 930 940 950
TCSRPISPLL DQNTPDFTTF CSVGEWLQAI KMERYKDNFT AAGYNSLESV
960 970 980 990
ARMTIEDVMS LGITLVGHQK KIMSSIQTMR AQMLHLHGTG IQV
Length:993
Mass (Da):111,367
Last modified:January 1, 1998 - v1
Checksum:iEECF9603047606BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14271 mRNA. Translation: CAA74643.1.
RefSeqiNP_990414.1. NM_205083.1.
UniGeneiGga.4157.

Genome annotation databases

EnsembliENSGALT00000025144; ENSGALP00000025098; ENSGALG00000015593.
GeneIDi395967.
KEGGigga:395967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14271 mRNA. Translation: CAA74643.1.
RefSeqiNP_990414.1. NM_205083.1.
UniGeneiGga.4157.

3D structure databases

ProteinModelPortaliO42422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000025098.

Proteomic databases

PaxDbiO42422.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000025144; ENSGALP00000025098; ENSGALG00000015593.
GeneIDi395967.
KEGGigga:395967.

Organism-specific databases

CTDi2045.

Phylogenomic databases

eggNOGiKOG0196. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118975.
HOGENOMiHOG000233856.
HOVERGENiHBG062180.
InParanoidiO42422.
KOiK05108.
OMAiTRHPSWI.
OrthoDBiEOG091G00W0.
PhylomeDBiO42422.
TreeFamiTF315608.

Enzyme and pathway databases

BRENDAi2.7.10.1. 1306.
ReactomeiR-GGA-2682334. EPH-Ephrin signaling.
R-GGA-3928663. EPHA-mediated growth cone collapse.
R-GGA-3928665. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

PROiO42422.

Gene expression databases

BgeeiENSGALG00000015593.

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.
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.
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_CHICK
AccessioniPrimary (citable) accession number: O42422
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 150 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.