LipidDB-10116-00777

Lipid Modification Database

Tag

Content

LipidDB ID

LipidDB-10116-00777

Entry Name

UniProt Accession

Theoretical PI

6.13

Molecular Weight

111007.39

Genbank Protein ID

Genbank Nucleotide ID

Protein Name

Ephrin type-A receptor 5

Protein Synonyms/Alias

2.7.10.1; EPH homology kinase 1; EHK-1;

Gene Name

Epha5

Gene Synonyms/Alias

Ehk-1; Ekh1; Rek7;

Created Date

01-OCT-1996

Lipid Modification Sites
Position	Sequence Form	Peptide	References	Modification Type
45	Canonical	LKGPLWTCLLLCAAL	[1]	S-Palmitoylation
600	Canonical	GFLLSGSCCECGCGR	[1]	S-Palmitoylation
601	Canonical	FLLSGSCCECGCGRA	[1]	S-Palmitoylation
603	Canonical	LSGSCCECGCGRASS	[1]	S-Palmitoylation

Organism

Rattus norvegicus (Rat)

NCBI Taxa ID

10116

Reference

[1] Predicted from GPS-Lipid

Functional Description

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 most probably constitutes the cognate/functional ligand for EPHA5. Functions as an axon guidance molecule during development and may be involved in the development of the retinotectal, entorhino- hippocampal and hippocamposeptal pathways. Together with EFNA5 plays also a role in synaptic plasticity in adult brain through regulation of synaptogenesis. In addition to its function in the nervous system, the interaction of EPHA5 with EFNA5 mediates communication between pancreatic islet cells to regulate glucose- stimulated insulin secretion (By similarity).

Sequence Annotation

Topological domain: 27 575 Extracellular.
Transmembrane: 576 596 Helical.
Topological domain: 597 1005 Cytoplasmic.
Domain: 62 240 Eph LBD.
Domain: 359 469 Fibronectin type-III 1.
Domain: 470 564 Fibronectin type-III 2.
Domain: 677 938 Protein kinase.
Domain: 967 1005 SAM.
Nucleotide-binding: 683 691 ATP.
Active site: 802 802 Proton acceptor.
Binding site: 709 709 ATP.
Modified residue: 652 652 Phosphotyrosine; by autocatalysis.
Modified residue: 658 658 Phosphotyrosine; by autocatalysis.
Modified residue: 835 835 Phosphotyrosine; by autocatalysis.
Modified residue: 984 984 Phosphotyrosine; by autocatalysis.

Protein Length

1005 AA.

Protein Sequence
(Canonical)

MRGSGPRGAG RRRTQGRGGG GDTPRVPASL AGCYSAPLKG PLWTCLLLCA ALRTLLASPS  60
NEVNLLDSRT VLGDLGWIAF PKNGWEEIGE VDENYAPIHT YQVCKVMEQN QNNWLLTSWI  120
SNEGASRIFI ELKFTLRDCN SLPGGLGTCK ETFNMYYFES DDENGRNIKD NQYIKIDTIA  180
ADESFTELDL GDRVMKLNTE VRDVGPLSKK GFYLAFQDVG ACIALVSVRV YYKKCPSVVR  240
HLAVFPDTIT GADSSQLLEV SGSCVNHSVT DDPPKMHCSA EGEWLVPIGK CMCKAGYEEK  300
NGTCQVCRPG FFKASPHSQT CSKCPPHSYT HEEASTSCVC EKDYFRRESD PPTMACTRPP  360
SAPRNAISNV NETSVFLEWI PPADTGGGKD VSYYILCKKC NSHAGVCEEC GGHVRYLPQQ  420
IGLKNTSVMM ADPLAHTNYT FEIEAVNGVS DLSPGTRQYV SVNVTTNQAA PSPVTNVKKG  480
KIAKNSISLS WQEPDRPNGI ILEYEIKYFE KDQETSYTII KSKETTITAE GLKPASVYVF  540
QIRARTAAGY GVFSRRFEFE TTPVFGASND QSQIPIIGVS VTVGVILLAV MIGFLLSGSC  600
CECGCGRASS LCAVAHPSLI WRCGYSKAKQ DPEEEKMHFH NGHIKLPGVR TYIDPHTYED  660
PTQAVHEFGK EIEASCITIE RVIGAGEFGE VCSGRLKLPG KRELPVATKT LKVGYTEKQR  720
RDFLSEASIM GQFDHPNIIH LEGVVTKSKP VMIVTEYMEN GSLDTFLKKN DGQFTVIQLV  780
GMLRGIAAGM KYLSDMGYVH RDLAARNILI NSNLVCKVSD FGLSRVLEDD PEAAYTTRGG  840
KIPIRWTAPE AIAFRKFTSA SDVWSYGIVM WEVVSYGERP YWEMTNQDVI KAVEEGYRLP  900
SPMDCPAALY QLMLDCWQKD RNSRPKFDDI VNMLDKLIRN PSSLKTLVNA SSRVSTLLAE  960
HGSLGSGAYR SVGEWLEATK MGRYTEIFME NGYSSMDAVA QVTLE                  1005

FASTA
(Canonical)

>LipidDB-10116-00777|P54757
MRGSGPRGAGRRRTQGRGGGGDTPRVPASLAGCYSAPLKGPLWTCLLLCAALRTLLASPS
NEVNLLDSRTVLGDLGWIAFPKNGWEEIGEVDENYAPIHTYQVCKVMEQNQNNWLLTSWI
SNEGASRIFIELKFTLRDCNSLPGGLGTCKETFNMYYFESDDENGRNIKDNQYIKIDTIA
ADESFTELDLGDRVMKLNTEVRDVGPLSKKGFYLAFQDVGACIALVSVRVYYKKCPSVVR
HLAVFPDTITGADSSQLLEVSGSCVNHSVTDDPPKMHCSAEGEWLVPIGKCMCKAGYEEK
NGTCQVCRPGFFKASPHSQTCSKCPPHSYTHEEASTSCVCEKDYFRRESDPPTMACTRPP
SAPRNAISNVNETSVFLEWIPPADTGGGKDVSYYILCKKCNSHAGVCEECGGHVRYLPQQ
IGLKNTSVMMADPLAHTNYTFEIEAVNGVSDLSPGTRQYVSVNVTTNQAAPSPVTNVKKG
KIAKNSISLSWQEPDRPNGIILEYEIKYFEKDQETSYTIIKSKETTITAEGLKPASVYVF
QIRARTAAGYGVFSRRFEFETTPVFGASNDQSQIPIIGVSVTVGVILLAVMIGFLLSGSC
CECGCGRASSLCAVAHPSLIWRCGYSKAKQDPEEEKMHFHNGHIKLPGVRTYIDPHTYED
PTQAVHEFGKEIEASCITIERVIGAGEFGEVCSGRLKLPGKRELPVATKTLKVGYTEKQR
RDFLSEASIMGQFDHPNIIHLEGVVTKSKPVMIVTEYMENGSLDTFLKKNDGQFTVIQLV
GMLRGIAAGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGG
KIPIRWTAPEAIAFRKFTSASDVWSYGIVMWEVVSYGERPYWEMTNQDVIKAVEEGYRLP
SPMDCPAALYQLMLDCWQKDRNSRPKFDDIVNMLDKLIRNPSSLKTLVNASSRVSTLLAE
HGSLGSGAYRSVGEWLEATKMGRYTEIFMENGYSSMDAVAQVTLE

Gene Ontology

GO:0030425; C:dendrite; ISS:UniProtKB
GO:0005887; C:integral component of plasma membrane; IEA:InterPro
GO:0005886; C:plasma membrane; ISS:UniProtKB
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0005003; F:ephrin receptor activity; IDA:UniProtKB
GO:0005004; F:GPI-linked ephrin receptor activity; ISS:UniProtKB
GO:0070851; F:growth factor receptor binding; IPI:BHF-UCL
GO:0007411; P:axon guidance; ISS:UniProtKB
GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB
GO:0060997; P:dendritic spine morphogenesis; IDA:UniProtKB
GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB
GO:0021766; P:hippocampus development; ISS:UniProtKB
GO:0032793; P:positive regulation of CREB transcription factor activity; IMP:UniProtKB
GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL
GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB
GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB
GO:0032314; P:regulation of Rac GTPase activity; ISS:UniProtKB

Interpro

InterPro; IPR027936; Eph_TM
InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom
InterPro; IPR003961; Fibronectin_type3
InterPro; IPR008979; Galactose-bd-like
InterPro; IPR009030; Growth_fac_rcpt_N_dom
InterPro; IPR013783; Ig-like_fold
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR001660; SAM
InterPro; IPR013761; SAM/pointed
InterPro; IPR021129; SAM_type1
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom
InterPro; IPR008266; Tyr_kinase_AS
InterPro; IPR020635; Tyr_kinase_cat_dom
InterPro; IPR016257; Tyr_kinase_ephrin_rcpt
InterPro; IPR001426; Tyr_kinase_rcpt_V_CS

Pfam

Pfam; PF14575; EphA2_TM;
Pfam; PF01404; Ephrin_lbd;
Pfam; PF00041; fn3;
Pfam; PF07714; Pkinase_Tyr;
Pfam; PF00536; SAM_1;

SMART

SMART; SM00615; EPH_lbd;
SMART; SM00060; FN3;
SMART; SM00219; TyrKc;

PROSITE

PROSITE; PS01186; EGF_2;
PROSITE; PS51550; EPH_LBD;
PROSITE; PS50853; FN3;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00109; PROTEIN_KINASE_TYR;
PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1;
PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2;
PROSITE; PS50105; SAM_DOMAIN;

PRINTS

PRINTS; PR00109; TYRKINASE;