Tag |
Content |
dbPAF ID |
dbPAF-0000323 |
Uniprot Accession |
O08680; EPHA3_RAT; |
Genbank Protein ID |
NP_113752.1; |
Genbank Nucleotide ID |
NM_031564.1; |
Protein Name |
Ephrin type-A receptor 3 |
Protein Synonyms/Alias |
EPH-like kinase 4;EK4;rEK4;Tyrosine-protein kinase TYRO4; |
Gene Name |
Epha3 |
Gene Synonyms/Alias |
Rek4;Tyro4; |
Organism |
Rattus norvegicus(Rat) |
NCBI Taxa ID |
10116 |
Functional Description (View all) |
Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin 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. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development (By similarity).Functional Description
Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin 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. Highly promiscuous for ephrin-A ligands it binds preferentially EFNA5. Upon activation by EFNA5 regulates cell-cell adhesion, cytoskeletal organization and cell migration. Plays a role in cardiac cells migration and differentiation and regulates the formation of the atrioventricular canal and septum during development probably through activation by EFNA1. Involved in the retinotectal mapping of neurons. May also control the segregation but not the guidance of motor and sensory axons during neuromuscular circuit development (By similarity).
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Phosphorylation Sites
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dbPAF PTMs: 1 |
Sequence (Fasta) | MDCHLSILIL FGCCVLSCSR ELSPQPSNEV NLLDSKTIQG ELGWISYPSH GWEEISGVDE 60 HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK FTLRDCNSIP LVLGTCKETF 120 NLYYMESDDD HGVKFLEHQF TKIDTIAADE SFTQMDLGDR ILKLNTEIRE VGPVNKKGFY 180 LAFQDVGACV ALVSVRVYFK KCPFTVKNLA MFPDTVPMDS QSLVEVRGSC VNNSKEEDPP 240 RMYCSTEGEW LVPIGKCTCN AGYEERGFIC QACRPGFYKA LDGVAKCTKC PPHSSTQEDG 300 SMNCRCENNY FRAEKDPPSM ACTRPPSAPR NVISNINETS VILDWSWPLD TGGRKDITFN 360 IICKKCGWNV RQCEPCSPNV RFLPRQLGLT NTTVTVTDLL AHTNYTFEID AINGVSELSS 420 PPRQFAAVSI TTNQAAPSPV MTIKKDRTSR NSISLSWQEP EHPNGIILDY EVKYYEKQEQ 480 ETSYTILRAR GTNVTISSLK PDTTYVFQIR ARTAAGYGTN SRKFEFENSP DSFSISGENS 540 HVVMIAISAA VAIIVLTVVT YVLVGRFCGY HKSKHSSDEK RLHFGNGHLR LPGLRTYVDP 600 HTYEDPTQAV HEFAKELDAT NIAIDKVVGA GEFGEVCSGR LKLPSKKEIS VAIKTLKVGY 660 TEKQRRDFLG EASIMGQFDH PNIIRLEGVV TKSKPVMIVT EYMENGSLDS FLRKHDAQFT 720 VIQLVGMLRG IASGMKYLSD MGYVHRDLAA RNILINSNLV CKVSDFGLSR VLEDDPEAAY 780 TTRGGKIPVR WTSPEATAYR KFTSASDVWS YGIVLWEVMS YGERPYWEMS NQDVIKAVDE 840 GYRLPLPMDC PAALYQLMLD CWQKDRNNRP KFEQIVSILD KLIRNPGSLK IITSAAARPS 900 NLLLDQSNVD IATFHTTGDW LNGMRTAHCK EIFTGVEYSS CDTIAKISTD DMKKVGVTVV 960 GPQKKIISSI KALETQSKNG PVPV
985Fasta Sequence
>O08680|Epha3|Rattus norvegicus(Rat) MDCHLSILILFGCCVLSCSRELSPQPSNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFLEHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEDPPRMYCSTEGEWLVPIGKCTCNAGYEERGFICQACRPGFYKALDGVAKCTKCPPHSSTQEDGSMNCRCENNYFRAEKDPPSMACTRPPSAPRNVISNINETSVILDWSWPLDTGGRKDITFNIICKKCGWNVRQCEPCSPNVRFLPRQLGLTNTTVTVTDLLAHTNYTFEIDAINGVSELSSPPRQFAAVSITTNQAAPSPVMTIKKDRTSRNSISLSWQEPEHPNGIILDYEVKYYEKQEQETSYTILRARGTNVTISSLKPDTTYVFQIRARTAAGYGTNSRKFEFENSPDSFSISGENSHVVMIAISAAVAIIVLTVVTYVLVGRFCGYHKSKHSSDEKRLHFGNGHLRLPGLRTYVDPHTYEDPTQAVHEFAKELDATNIAIDKVVGAGEFGEVCSGRLKLPSKKEISVAIKTLKVGYTEKQRRDFLGEASIMGQFDHPNIIRLEGVVTKSKPVMIVTEYMENGSLDSFLRKHDAQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILINSNLVCKVSDFGLSRVLEDDPEAAYTTRGGKIPVRWTSPEATAYRKFTSASDVWSYGIVLWEVMSYGERPYWEMSNQDVIKAVDEGYRLPLPMDCPAALYQLMLDCWQKDRNNRPKFEQIVSILDKLIRNPGSLKIITSAAARPSNLLLDQSNVDIATFHTTGDWLNGMRTAHCKEIFTGVEYSSCDTIAKISTDDMKKVGVTVVGPQKKIISSIKALETQSKNGPVPV
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Keyword |
KW-0067--ATP-binding KW-1003--Cell membrane KW-0181--Complete proteome KW-0325--Glycoprotein KW-0418--Kinase KW-0472--Membrane KW-0547--Nucleotide-binding KW-0597--Phosphoprotein KW-0675--Receptor KW-1185--Reference proteome KW-0677--Repeat KW-0732--Signal KW-0808--Transferase KW-0812--Transmembrane KW-1133--Transmembrane helix KW-0829--Tyrosine-protein kinase
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Interpro |
IPR027936--Eph_TM IPR001090--Ephrin_rcpt_lig-bd_dom IPR003961--FN3_dom IPR008979--Galactose-bd-like IPR009030--Growth_fac_rcpt_N_dom 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
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PROSITE |
PS01186--EGF_2 PS51550--EPH_LBD PS50853--FN3 PS00107--PROTEIN_KINASE_ATP PS50011--PROTEIN_KINASE_DOM PS00109--PROTEIN_KINASE_TYR PS00790--RECEPTOR_TYR_KIN_V_1 PS00791--RECEPTOR_TYR_KIN_V_2 PS50105--SAM_DOMAIN
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Pfam |
PF14575--EphA2_TM PF01404--Ephrin_lbd PF00041--fn3 PF07699--GCC2_GCC3 PF07714--Pkinase_Tyr PF07647--SAM_2
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Gene Ontology |
GO:0005769--C:early endosome GO:0005887--C:integral component of plasma membrane GO:0005524--F:ATP binding GO:0005004--F:GPI-linked ephrin receptor activity GO:0016477--P:cell migration GO:0048013--P:ephrin receptor signaling pathway GO:0097156--P:fasciculation of motor neuron axon GO:0097155--P:fasciculation of sensory neuron axon GO:0001660--P:fever generation GO:0032956--P:regulation of actin cytoskeleton organization GO:0010717--P:regulation of epithelial to mesenchymal transition GO:0051893--P:regulation of focal adhesion assembly GO:0043087--P:regulation of GTPase activity GO:0070507--P:regulation of microtubule cytoskeleton organization GO:0034097--P:response to cytokine GO:0032496--P:response to lipopolysaccharide
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