EPHA7_HUMAN » Ephrin type-A receptor 7

EPHA7_HUMAN » Ephrin type-A receptor 7
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
EPHA7_HUMAN » Ephrin type-A receptor 7 » EPH homology kinase 3;EHK-3; EPH-like kinase 11;EK11; hEK11;
Hydrophobic Thickness 34.0 ± 1.4 Å
Tilt Angle 0 ± 4°
ΔGtransfer -57.6 kcal/mol
ΔGfold -24.0 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 554-579 (554-581)
Pathways

Axon guidance (KEGG)

PDB 3nru (32-204), 2rei (590-899), 3dko (590-899), 3h8m (919-990)
OPM none
Complexes none
Interactions

EPHA2, Complex: EPHA2:EPHA7, PubMed

EPHA3, Complex: EPHA3:EPHA7, PubMed

Domains

AA: 33-205, PDBID: 3NRU, Subunit G, Seq Identity:100%, Ephrin receptor ligand binding domain

AA: 268-312, Putative ephrin-receptor like

AA: 333-427, PDBID: 4BK4, Subunit A, Seq Identity:46%, Fibronectin type III domain

AA: 444-527, PDBID: 1X5L, Subunit A, Seq Identity:55%, Fibronectin type III domain

AA: 557-630, PDBID: 2REI, Subunit A, Seq Identity:100%, Ephrin type-A receptor 2 transmembrane domain

AA: 633-890, PDBID: 2REI, Subunit A, Seq Identity:100%, Protein tyrosine kinase

AA: 920-985, PDBID: 3H8M, Subunit A, Seq Identity:100%, SAM domain (Sterile alpha motif)

UniProt annotation for EPHA7_HUMAN » Ephrin type-A receptor 7
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.

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

SUBUNIT: 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).

TISSUE SPECIFICITY: Widely expressed.

UniProt features for EPHA7_HUMAN » Ephrin type-A receptor 7
SIGNAL 1 27 Potential.
CHAIN 28 998 Ephrin type-A receptor 7.
DOMAIN 32 210 Eph LBD.
DOMAIN 331 433 Fibronectin type-III 1.
DOMAIN 443 535 Fibronectin type-III 2.
DOMAIN 633 894 Protein kinase.
DOMAIN 923 987 SAM.
MOTIF 996 998 PDZ-binding (Potential).
ACT_SITE 758 758 Proton acceptor (By similarity).
Amino Acid Sequence for EPHA7_HUMAN » Ephrin type-A receptor 7
MVFQTRYPSW IILCYIWLLR FAHTGEAQAA KEVLLLDSKA QQTELEWISS PPNGWEEISG LDENYTPIRT YQVCQVMEPN QNNWLRTNWI SKGNAQRIFV ELKFTLRDCN SLPGVLGTCK ETFNLYYYET DYDTGRNIRE NLYVKIDTIA ADESFTQGDL GERKMKLNTE VREIGPLSKK GFYLAFQDVG ACIALVSVKV YYKKCWSIIE NLAIFPDTVT GSEFSSLVEV RGTCVSSAEE EAENAPRMHC SAEGEWLVPI GKCICKAGYQ QKGDTCEPCG RGFYKSSSQD LQCSRCPTHS FSDKEGSSRC ECEDGYYRAP SDPPYVACTR PPSAPQNLIF NINQTTVSLE WSPPADNGGR NDVTYRILCK RCSWEQGECV PCGSNIGYMP QQTGLEDNYV TVMDLLAHAN YTFEVEAVNG VSDLSRSQRL FAAVSITTGQ AAPSQVSGVM KERVLQRSVE LSWQEPEHPN GVITEYEIKY YEKDQRERTY STVKTKSTSA SINNLKPGTV YVFQIRAFTA AGYGNYSPRL DVATLEEATG KMFEATAVSS EQNPVIIIAV VAVAGTIILV FMVFGFIIGR RHCGYSKADQ EGDEELYFHF KFPGTKTYID PETYEDPNRA VHQFAKELDA SCIKIERVIG AGEFGEVCSG RLKLPGKRDV AVAIKTLKVG YTEKQRRDFL CEASIMGQFD HPNVVHLEGV VTRGKPVMIV IEFMENGALD AFLRKHDGQF TVIQLVGMLR GIAAGMRYLA DMGYVHRDLA ARNILVNSNL VCKVSDFGLS RVIEDDPEAV YTTTGGKIPV RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM SNQDVIKAIE EGYRLPAPMD CPAGLHQLML DCWQKERAER PKFEQIVGIL DKMIRNPNSL KTPLGTCSRP ISPLLDQNTP DFTTFCSVGE WLQAIKMERY KDNFTAAGYN SLESVARMTI EDVMSLGITL VGHQKKIMSS IQTMRAQMLH LHGTGIQV