EPHB4_HUMAN » Ephrin type-B receptor 4

EPHB4_HUMAN » Ephrin type-B receptor 4
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
EPHB4_HUMAN » Ephrin type-B receptor 4 » Hepatoma transmembrane kinase;Tyrosine-protein kinase TYRO11;
Hydrophobic Thickness 37.6 ± 1.4 Å
Tilt Angle 0 ± 1°
ΔGtransfer -59.3 kcal/mol
ΔGfold -25.7 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 537-565 (530-567)
Pathways

Axon guidance (KEGG)

PDB 2e7h (434-529), 2vwu (598-887), 3zew (598-892), 2yn8 (598-892), 4bb4 (598-899), 2xvd (598-899), 2x9f (598-899), 2vx1 (598-899), 2vx0 (598-899), 2vwz (598-899), 2vwy (598-899), 2vwx (598-899), 2vww (598-899), 2vwv (598-899), 4aw5 (605-890), 2qkq (896-977), 2hle (A=17-196), 2bba (A=17-196)
OPM none
Complexes

EPHB4:Q96L35:EFNB2_HUMAN

Interactions

A4, Complex: A4:EPHB4, PubMed

EFNB2, Complex: EFNB2:EPHB4, PDBID: 2hle

EGFR, Complex: EGFR:EPHB4, PubMed

EPHB6, Complex: EPHB6:EPHB4, PubMed

SDC3, Complex: SDC3:EPHB4, PubMed

Domains

AA: 18-197, PDBID: 2BBA, Subunit A, Seq Identity:100%, Ephrin receptor ligand binding domain

AA: 258-304, Putative ephrin-receptor like

AA: 325-417, PDBID: 2X10, Subunit A, Seq Identity:34%, Fibronectin type III domain

AA: 435-519, PDBID: 2E7H, Subunit A, Seq Identity:100%, Fibronectin type III domain

AA: 541-612, PDBID: 2VWU, Subunit A, Seq Identity:100%, Ephrin type-A receptor 2 transmembrane domain

AA: 615-874, PDBID: 2VWU, Subunit A, Seq Identity:100%, Protein tyrosine kinase

AA: 905-969, PDBID: 2QKQ, Subunit B, Seq Identity:100%, SAM domain (Sterile alpha motif)

UniProt annotation for EPHB4_HUMAN » Ephrin type-B receptor 4
FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B 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. Together with its cognate ligand/functional ligand EFNB2 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4- mediated forward signaling controls cellular repulsion and segregation form EFNB2-expressing cells. Plays also a role in postnatal blood vessel remodeling, morphogenesis and permeability and is thus important in the context of tumor angiogenesis.

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).

TISSUE SPECIFICITY: Abundantly expressed in placenta but also detected in kidney, liver, lung, pancreas, skeletal muscle and heart. Expressed in primitive and myeloid, but not lymphoid, hematopoietic cells. Also observed in cell lines derived from liver, breast, colon, lung, melanocyte and cervix.

DEVELOPMENTAL STAGE: Expressed in fetal heart, lung, liver and to a lower extent in brain. Not expressed in adult brain.

UniProt features for EPHB4_HUMAN » Ephrin type-B receptor 4
SIGNAL 1 15 Potential.
CHAIN 16 987 Ephrin type-B receptor 4.
DOMAIN 17 202 Eph LBD.
DOMAIN 323 428 Fibronectin type-III 1.
DOMAIN 434 526 Fibronectin type-III 2.
DOMAIN 615 899 Protein kinase.
DOMAIN 907 971 SAM.
MOTIF 985 987 PDZ-binding (Potential).
ACT_SITE 740 740 Proton acceptor (By similarity).
DISULFID 61 184
DISULFID 97 107
Amino Acid Sequence for EPHB4_HUMAN » Ephrin type-B receptor 4
MELRVLLCWA SLAAALEETL LNTKLETADL KWVTFPQVDG QWEELSGLDE EQHSVRTYEV CDVQRAPGQA HWLRTGWVPR RGAVHVYATL RFTMLECLSL PRAGRSCKET FTVFYYESDA DTATALTPAW MENPYIKVDT VAAEHLTRKR PGAEATGKVN VKTLRLGPLS KAGFYLAFQD QGACMALLSL HLFYKKCAQL TVNLTRFPET VPRELVVPVA GSCVVDAVPA PGPSPSLYCR EDGQWAEQPV TGCSCAPGFE AAEGNTKCRA CAQGTFKPLS GEGSCQPCPA NSHSNTIGSA VCQCRVGYFR ARTDPRGAPC TTPPSAPRSV VSRLNGSSLH LEWSAPLESG GREDLTYALR CRECRPGGSC APCGGDLTFD PGPRDLVEPW VVVRGLRPDF TYTFEVTALN GVSSLATGPV PFEPVNVTTD REVPPAVSDI RVTRSSPSSL SLAWAVPRAP SGAVLDYEVK YHEKGAEGPS SVRFLKTSEN RAELRGLKRG ASYLVQVRAR SEAGYGPFGQ EHHSQTQLDE SEGWREQLAL IAGTAVVGVV LVLVVIVVAV LCLRKQSNGR EAEYSDKHGQ YLIGHGTKVY IDPFTYEDPN EAVREFAKEI DVSYVKIEEV IGAGEFGEVC RGRLKAPGKK ESCVAIKTLK GGYTERQRRE FLSEASIMGQ FEHPNIIRLE GVVTNSMPVM ILTEFMENGA LDSFLRLNDG QFTVIQLVGM LRGIASGMRY LAEMSYVHRD LAARNILVNS NLVCKVSDFG LSRFLEENSS DPTYTSSLGG KIPIRWTAPE AIAFRKFTSA SDAWSYGIVM WEVMSFGERP YWDMSNQDVI NAIEQDYRLP PPPDCPTSLH QLMLDCWQKD RNARPRFPQV VSALDKMIRN PASLKIVARE NGGASHPLLD QRQPHYSAFG SVGEWLRAIK MGRYEESFAA AGFGSFELVS QISAEDLLRI GVTLAGHQKK ILASVQHMKS QAKPGTPGGT GGPAPQY