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Entry version 166 (07 Apr 2021)
Sequence version 1 (01 Jul 1997)
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Protein

Ephrin type-A receptor 3

Gene

Epha3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei654ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei747Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi629 – 634ATPPROSITE-ProRule annotation6
Nucleotide bindingi701 – 707ATPPROSITE-ProRule annotation7
Nucleotide bindingi751 – 752ATPPROSITE-ProRule annotation2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1, 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-2682334, EPH-Ephrin signaling
R-RNO-3928663, EPHA-mediated growth cone collapse
R-RNO-3928665, EPH-ephrin mediated repulsion of cells

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ephrin type-A receptor 3 (EC:2.7.10.1)
Alternative name(s):
EPH-like kinase 4
Short name:
EK4
Short name:
rEK4
Tyrosine-protein kinase TYRO4
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Epha3
Synonyms:Rek4, Tyro4
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
68389, Epha3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini21 – 541ExtracellularSequence analysisAdd BLAST521
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei542 – 565HelicalSequence analysisAdd BLAST24
Topological domaini566 – 984CytoplasmicSequence analysisAdd BLAST419

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20By similarityAdd BLAST20
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001680421 – 984Ephrin type-A receptor 3Add BLAST964

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi232N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi337N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi391N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi404N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi493N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei597Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei603Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei702Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei780Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei938PhosphotyrosineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-603 mediates interaction with NCK1. Dephosphorylated by PTPN1 (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O08680

PRoteomics IDEntifications database

More...
PRIDEi
O08680

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
O08680, 5 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O08680

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O08680

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O08680

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Most abundant in the heart, brain and lung.

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Down-regulated by IL1-beta in neonatal cardiac myocytes.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

Forms a ternary EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain shedding by ADAM10 which regulates the EFNA5-EPHA3 complex internalization and function.

Interacts (phosphorylated) with PTPN1; dephosphorylates EPHA3 and may regulate its trafficking and function.

Interacts (phosphorylated) with CRK; mediates EFNA5-EPHA3 signaling through RHOA GTPase activation.

Interacts with NCK1 (via SH2 domain); mediates EFNA5-EPHA3 signaling (By similarity).

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000043263

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O08680

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini29 – 207Eph LBDPROSITE-ProRule annotationAdd BLAST179
Domaini325 – 435Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST111
Domaini436 – 532Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST97
Domaini622 – 883Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini912 – 976SAMPROSITE-ProRule annotationAdd BLAST65

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi982 – 984PDZ-bindingSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi189 – 322Cys-richAdd BLAST134

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0196, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O08680

Database of Orthologous Groups

More...
OrthoDBi
933071at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O08680

Family and domain databases

Conserved Domains Database

More...
CDDi
cd10481, EphR_LBD_A3, 1 hit
cd00063, FN3, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.150.50, 1 hit
2.60.120.260, 1 hit
2.60.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027936, Eph_TM
IPR034266, EphA3_rcpt_lig-bd
IPR001090, Ephrin_rcpt_lig-bd_dom
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR008979, Galactose-bd-like_sf
IPR009030, Growth_fac_rcpt_cys_sf
IPR013783, Ig-like_fold
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR001660, SAM
IPR013761, SAM/pointed_sf
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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF14575, EphA2_TM, 1 hit
PF01404, Ephrin_lbd, 1 hit
PF07699, Ephrin_rec_like, 1 hit
PF00041, fn3, 2 hits
PF07714, PK_Tyr_Ser-Thr, 1 hit
PF07647, SAM_2, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000666, TyrPK_ephrin_receptor, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109, TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00615, EPH_lbd, 1 hit
SM00060, FN3, 2 hits
SM00454, SAM, 1 hit
SM00219, TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47769, SSF47769, 1 hit
SSF49265, SSF49265, 1 hit
SSF49785, SSF49785, 1 hit
SSF56112, SSF56112, 1 hit
SSF57184, SSF57184, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01186, 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

O08680-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDCHLSILIL FGCCVLSCSR ELSPQPSNEV NLLDSKTIQG ELGWISYPSH
60 70 80 90 100
GWEEISGVDE HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK
110 120 130 140 150
FTLRDCNSIP LVLGTCKETF NLYYMESDDD HGVKFLEHQF TKIDTIAADE
160 170 180 190 200
SFTQMDLGDR ILKLNTEIRE VGPVNKKGFY LAFQDVGACV ALVSVRVYFK
210 220 230 240 250
KCPFTVKNLA MFPDTVPMDS QSLVEVRGSC VNNSKEEDPP RMYCSTEGEW
260 270 280 290 300
LVPIGKCTCN AGYEERGFIC QACRPGFYKA LDGVAKCTKC PPHSSTQEDG
310 320 330 340 350
SMNCRCENNY FRAEKDPPSM ACTRPPSAPR NVISNINETS VILDWSWPLD
360 370 380 390 400
TGGRKDITFN IICKKCGWNV RQCEPCSPNV RFLPRQLGLT NTTVTVTDLL
410 420 430 440 450
AHTNYTFEID AINGVSELSS PPRQFAAVSI TTNQAAPSPV MTIKKDRTSR
460 470 480 490 500
NSISLSWQEP EHPNGIILDY EVKYYEKQEQ ETSYTILRAR GTNVTISSLK
510 520 530 540 550
PDTTYVFQIR ARTAAGYGTN SRKFEFENSP DSFSISGENS HVVMIAISAA
560 570 580 590 600
VAIIVLTVVT YVLVGRFCGY HKSKHSSDEK RLHFGNGHLR LPGLRTYVDP
610 620 630 640 650
HTYEDPTQAV HEFAKELDAT NIAIDKVVGA GEFGEVCSGR LKLPSKKEIS
660 670 680 690 700
VAIKTLKVGY TEKQRRDFLG EASIMGQFDH PNIIRLEGVV TKSKPVMIVT
710 720 730 740 750
EYMENGSLDS FLRKHDAQFT VIQLVGMLRG IASGMKYLSD MGYVHRDLAA
760 770 780 790 800
RNILINSNLV CKVSDFGLSR VLEDDPEAAY TTRGGKIPVR WTSPEATAYR
810 820 830 840 850
KFTSASDVWS YGIVLWEVMS YGERPYWEMS NQDVIKAVDE GYRLPLPMDC
860 870 880 890 900
PAALYQLMLD CWQKDRNNRP KFEQIVSILD KLIRNPGSLK IITSAAARPS
910 920 930 940 950
NLLLDQSNVD IATFHTTGDW LNGMRTAHCK EIFTGVEYSS CDTIAKISTD
960 970 980
DMKKVGVTVV GPQKKIISSI KALETQSKNG PVPV
Length:984
Mass (Da):110,228
Last modified:July 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF170C49312F7A0AB
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V9D5G3V9D5_RAT
Receptor protein-tyrosine kinase
Epha3 rCG_47005
984Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0G2JT71A0A0G2JT71_RAT
Receptor protein-tyrosine kinase
Epha3
981Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U69278 mRNA Translation: AAC06273.1

Protein sequence database of the Protein Information Resource

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PIRi
PT0186

NCBI Reference Sequences

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RefSeqi
NP_113752.1, NM_031564.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
29210

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:29210

UCSC genome browser

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UCSCi
RGD:68389, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U69278 mRNA Translation: AAC06273.1
PIRiPT0186
RefSeqiNP_113752.1, NM_031564.1

3D structure databases

SMRiO08680
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000043263

PTM databases

GlyGeniO08680, 5 sites
iPTMnetiO08680
PhosphoSitePlusiO08680
SwissPalmiO08680

Proteomic databases

PaxDbiO08680
PRIDEiO08680

Genome annotation databases

GeneIDi29210
KEGGirno:29210
UCSCiRGD:68389, rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2042
RGDi68389, Epha3

Phylogenomic databases

eggNOGiKOG0196, Eukaryota
InParanoidiO08680
OrthoDBi933071at2759
PhylomeDBiO08680

Enzyme and pathway databases

BRENDAi2.7.10.1, 5301
ReactomeiR-RNO-2682334, EPH-Ephrin signaling
R-RNO-3928663, EPHA-mediated growth cone collapse
R-RNO-3928665, EPH-ephrin mediated repulsion of cells

Miscellaneous databases

Protein Ontology

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PROi
PR:O08680

Family and domain databases

CDDicd10481, EphR_LBD_A3, 1 hit
cd00063, FN3, 2 hits
Gene3Di1.10.150.50, 1 hit
2.60.120.260, 1 hit
2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR027936, Eph_TM
IPR034266, EphA3_rcpt_lig-bd
IPR001090, Ephrin_rcpt_lig-bd_dom
IPR003961, FN3_dom
IPR036116, FN3_sf
IPR008979, Galactose-bd-like_sf
IPR009030, Growth_fac_rcpt_cys_sf
IPR013783, Ig-like_fold
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR001660, SAM
IPR013761, SAM/pointed_sf
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
PfamiView protein in Pfam
PF14575, EphA2_TM, 1 hit
PF01404, Ephrin_lbd, 1 hit
PF07699, Ephrin_rec_like, 1 hit
PF00041, fn3, 2 hits
PF07714, PK_Tyr_Ser-Thr, 1 hit
PF07647, SAM_2, 1 hit
PIRSFiPIRSF000666, TyrPK_ephrin_receptor, 1 hit
PRINTSiPR00109, TYRKINASE
SMARTiView protein in SMART
SM00615, EPH_lbd, 1 hit
SM00060, FN3, 2 hits
SM00454, SAM, 1 hit
SM00219, TyrKc, 1 hit
SUPFAMiSSF47769, SSF47769, 1 hit
SSF49265, SSF49265, 1 hit
SSF49785, SSF49785, 1 hit
SSF56112, SSF56112, 1 hit
SSF57184, SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS01186, 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEPHA3_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O08680
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: April 7, 2021
This is version 166 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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