Ephrin type-A receptor 2 precursor - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot Q03145 (EPHA2_MOUSE)

Last modified November 3, 2009. Version 103. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Ephrin type-A receptor 2
    EC=2.7.10.1
Alternative name(s):
    Tyrosine-protein kinase receptor ECK
    Epithelial cell kinase
    MPK-5
    SEK-2

Gene names

Name:	Epha2
Synonyms:	Eck, Sek2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	977 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Receptor for members of the ephrin-A family. Binds to ephrin-A1, -A3, -A4 and -A5. May function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. May be involved in cell-cell interactions guiding early hindbrain development.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Interacts with INPPL1/SHIP2 By similarity. Interacts with SLA.
Subcellular location	Membrane; Single-pass type I membrane protein.
Developmental stage	First detected in gastrulation stage embryos (6.5-7.5 dpc) in ectodermal cells adjacent to the distal region of the primitive streak. By the neural plate stage (approximately 7.5 dpc), EPHA2 expression becomes restricted to the extreme distal end or node of the primitive streak. After the beginning of somitogenesis (approximately 8.0 dpc), expression persists in the node as this structure regresses toward the caudal end of the embryo. In addition, beginning at the mid head fold stage (approximately 7.75 dpc), we observe that EPHA2 exhibits a dynamic and spatially restricted expression pattern in the prospective hindbrain region. EPHA2 transcripts are initially detected in a 5-cell wide strip of mesodermal cells underlying prospective rhombomere 4 (R4). Subsequently at the beginning of somitogenesis, expression is observed in prospective R4. At the 4-8-somite stage, EPHA2 transcripts are observed in R4, mesenchymal cells underlying R4, and surface ectoderm in the vicinity of the developing second branchial arch. By the 10-somite stage, expression in these cells is down-regulated. Additionally, at the 5-8-somite stage, EPHA2 transcripts are detected initially in the lateral mesenchyme immediately underlying the surface ectoderm adjacent to R5 and R6, and subsequently in surface ectoderm overlying the developing third branchial arch.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily. Contains 2 fibronectin type-III domains. Contains 1 protein kinase domain. Contains 1 SAM (sterile alpha motif) domain.

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Ontologies

Keywords
Cellular component	Membrane
Domain	Repeat Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	axial mesoderm formation Inferred from mutant phenotype. Source: MGI ephrin receptor signaling pathway Inferred from direct assay. Source: MGI neural tube development Inferred from mutant phenotype. Source: MGI neuron differentiation Inferred from direct assay. Source: MGI notochord cell development Inferred from mutant phenotype. Source: MGI notochord formation Inferred from genetic interaction. Source: MGI protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro skeletal system development Inferred from mutant phenotype. Source: MGI tail morphogenesis Inferred from mutant phenotype. Source: MGI vasculogenesis Inferred from mutant phenotype. Source: MGI
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ephrin receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

Potential

Chain

24 – 977

954

Ephrin type-A receptor 2

PRO_0000016801

Regions

Topological domain

24 – 535

512

Extracellular Potential

Transmembrane

536 – 559

Potential

Topological domain

560 – 977

418

Cytoplasmic Potential

Domain

329 – 430

102

Fibronectin type-III 1

Domain

436 – 527

Fibronectin type-III 2

Domain

614 – 876

263

Protein kinase

Domain

905 – 969

SAM

Nucleotide binding

620 – 628

ATP By similarity

Motif

975 – 977

PDZ-binding Potential

Compositional bias

187 – 326

140

Cys-rich

Sites

Active site

740

Proton acceptor By similarity

Binding site

647

ATP By similarity

Amino acid modifications

Modified residue

571

Phosphoserine By similarity

Modified residue

580

Phosphoserine By similarity

Modified residue

589

Phosphotyrosine; by autocatalysis Potential

Modified residue

595

Phosphotyrosine; by autocatalysis By similarity

Modified residue

629

Phosphotyrosine By similarity

Modified residue

648

Phosphothreonine By similarity

Modified residue

773

Phosphotyrosine; by autocatalysis By similarity

Modified residue

893

Phosphoserine By similarity

Modified residue

898

Phosphoserine By similarity

Modified residue

899

Phosphothreonine By similarity

Modified residue

900

Phosphoserine By similarity

Modified residue

902

Phosphoserine By similarity

Modified residue

922

Phosphotyrosine; by autocatalysis Potential

Modified residue

931

Phosphotyrosine By similarity

Modified residue

961

Phosphotyrosine By similarity

Glycosylation

408

N-linked (GlcNAc...) Ref.8

Glycosylation

436

N-linked (GlcNAc...) Ref.8

Experimental info

Sequence conflict

T → A in AAA82113. Ref.2

Sequence conflict

112 – 113

SS → HA in AAA82113. Ref.2

Sequence conflict

189

A → R in AAA82113. Ref.2

Sequence conflict

209

R → C in AAA82113. Ref.2

Sequence conflict

244

P → A in AAA82113. Ref.2

Sequence conflict

258 – 260

IGQ → SE in AAA82113. Ref.2

Sequence conflict

291

C → S in AAA82113. Ref.2

Sequence conflict

339 – 340

IG → C in AAA82113. Ref.2

Sequence conflict

371 – 372

WP → CA in AAA82113. Ref.2

Sequence conflict

383

S → T in AAA82113. Ref.2

Sequence conflict

457

W → R in AAA82113. Ref.2

Sequence conflict

485

V → G in AAA82113. Ref.2

Sequence conflict

511

L → W in AAA82113. Ref.2

Sequence conflict

534

A → R in AAA82113. Ref.2

Sequence conflict

678

P → R Ref.2

Sequence conflict

678

P → R Ref.3

Sequence conflict

681

G → A in AAA82113. Ref.2

Sequence conflict

819 – 820

YW → LL in AAA82113. Ref.2

Sequence conflict

878

A → R in AAA82113. Ref.2

Sequence conflict

919 – 920

MQ → IE in AAA82113. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Q03145-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: D6ADFBD0CCF5A83C
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FASTA

977

108,823

        10         20         30         40         50         60 
MELRTVGFCL ALLWGCALAA AAAQGKEVVL LDFAAMKGEL GWLTHPYGKG WDLMQNIMDD 

        70         80         90        100        110        120 
MPIYMYSVCN VVSGDQDNWL RTNWVYREEA ERIFIELKFT VRDCNSFPGG ASSCKETFNL 

       130        140        150        160        170        180 
YYAESDVDYG TNFQKRQFTK IDTIAPDEIT VSSDFEARNV KLNVEERMVG PLTRKGFYLA 

       190        200        210        220        230        240 
FQDIGACVAL LSVRVYYKKC PEMLQSLARF PETIAVAVSD TQPLATVAGT CVDHAVVPYG 

       250        260        270        280        290        300 
GEGPLMHCTV DGEWLVPIGQ CLCQEGYEKV EDACRACSPG FFKSEASESP CLECPEHTLP 

       310        320        330        340        350        360 
STEGATSCQC EEGYFRAPED PLSMSCTRPP SAPNYLTAIG MGAKVELRWT APKDTGGRQD 

       370        380        390        400        410        420 
IVYSVTCEQC WPESGECGPC EASVRYSEPP HALTRTSVTV SDLEPHMNYT FAVEARNGVS 

       430        440        450        460        470        480 
GLVTSRSFRT ASVSINQTEP PKVRLEDRST TSLSVTWSIP VSQQSRVWKY EVTYRKKGDA 

       490        500        510        520        530        540 
NSYNVRRTEG FSVTLDDLAP DTTYLVQVQA LTQEGQGAGS KVHEFQTLST EGSANMAVIG 

       550        560        570        580        590        600 
GVAVGVVLLL VLAGVGLFIH RRRRNLRARQ SSEDVRFSKS EQLKPLKTYV DPHTYEDPNQ 

       610        620        630        640        650        660 
AVLKFTTEIH PSCVARQKVI GAGEFGEVYK GTLKASSGKK EIPVAIKTLK AGYTEKQRVD 

       670        680        690        700        710        720 
FLSEASIMGQ FSHHNIIPLE GVVSKYKPMM IITEYMENGA LDKFLREKDG EFSVLQLVGM 

       730        740        750        760        770        780 
LRGIASGMKY LANMNYVHRD LAARNILVNS NLVCKVSDFG LSRVLEDDPE ATYTTSGGKI 

       790        800        810        820        830        840 
PIRWTAPEAI SYRKFTSASD VWSYGIVMWE VMTYGERPYW ELSNHEVMKA INDGFRLPTP 

       850        860        870        880        890        900 
MDCPSAIYQL MMQCWQQERS RRPKFADIVS ILDKLIRAPD SLKTLADFDP RVSIRLPSTS 

       910        920        930        940        950        960 
GSEGVPFRTV SEWLESIKMQ QYTEHFMVAG YTAIEKVVQM SNEDIKRIGV RLPGHQKRIA 

       970 
YSLLGLKDQV NTVGIPI

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Eck receptor tyrosine kinase is implicated in pattern formation during gastrulation, hindbrain segmentation and limb development." Ganju P., Shigemoto K., Brennan J., Entwistle A., Reith A.D. Oncogene 9:1613-1624(1994) [PubMed: 8183555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The expression of the receptor-protein tyrosine kinase gene, eck, is highly restricted during early mouse development." Ruiz J.C., Robertson E.J. Mech. Dev. 46:87-100(1994) [PubMed: 7918100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Several receptor tyrosine kinase genes of the Eph family are segmentally expressed in the developing hindbrain." Becker N., Seitanidou T., Murphy P., Mattei M.-G., Topilko P., Nieto A., Wilkinson D.G., Charnay P., Gilardi P. Mech. Dev. 47:3-17(1994) [PubMed: 7947319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-977. Strain: C57BL/6. Tissue: Embryo.
[4]	"An Eph-related receptor protein tyrosine kinase gene segmentally expressed in the developing mouse hindbrain." Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G., Chestier A., Wilkinson D.G., Charnay P. Oncogene 7:2499-2506(1992) [PubMed: 1281307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 742-799. Tissue: Embryonic brain.
[5]	"Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase." Pandey A., Duan H., Dixit V.M. J. Biol. Chem. 270:19201-19204(1995) [PubMed: 7543898] [Abstract] Cited for: INTERACTION WITH SLA. Tissue: Embryonic brain.
[6]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-589 AND TYR-773, MASS SPECTROMETRY.
[7]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-595 AND TYR-773, MASS SPECTROMETRY.
[8]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-408 AND ASN-436, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X78339 mRNA. Translation: CAA55135.1. U07634 mRNA. Translation: AAA82113.1. X76010 mRNA. Translation: CAA53597.1. X57243 mRNA. Translation: CAA40519.1.
IPI	IPI00129220.
PIR	I48759. I48974. S49004.
RefSeq	NP_034269.2.
UniGene	Mm.2581
3D structure databases
HSSP	HSSP built from PDB template 1JPA based on UniProtKB P54763.
SMR	Q03145. Positions 603-884.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:829N.
STRING	Q03145.
PTM databases
PhosphoSite	Q03145.
Proteomic databases
PRIDE	Q03145.
Genome annotation databases
Ensembl	ENSMUST00000006614; ENSMUSP00000006614; ENSMUSG00000006445; Mus musculus. [Genome view]
GeneID	13836.
KEGG	mmu:13836.
Organism-specific databases
CTD	13836.
MGI	MGI:95278. Epha2.
Phylogenomic databases
HOGENOM	Q03145.
HOVERGEN	Q03145.
Enzyme and pathway databases
BRENDA	2.7.10.1. 244.
Gene expression databases
ArrayExpress	Q03145.
Bgee	Q03145.
CleanEx	MM_EPHA2.
Genevestigator	Q03145.
GermOnline	ENSMUSG00000006445. Mus musculus.
Family and domain databases
InterPro	IPR013032. EGF-like_reg_CS. IPR001090. Ephrin_rcpt_lig-bd. IPR008957. Fibronectin_typ-III-like_fold. IPR003961. FN_III. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR001660. SAM. IPR013761. SAM_type. IPR001245. Tyr_pkinase. IPR008266. Tyr_pkinase_AS. IPR016257. TyrPK_ephrin_receptor. IPR001426. YKase_receptorV_CS. [Graphical view]
Gene3D	G3DSA:2.60.40.30. FN_III-like. 1 hit. G3DSA:1.10.150.50. SAM_type. 1 hit.
Pfam	PF01404. Ephrin_lbd. 1 hit. PF00041. fn3. 2 hits. PF07714. Pkinase_Tyr. 1 hit. PF00536. SAM_1. 1 hit. [Graphical view]
PIRSF	PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTS	PR00109. TYRKINASE.
ProDom	PD001495. Ephrin_receptor. 1 hit. PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00615. EPH_lbd. 1 hit. SM00060. FN3. 2 hits. SM00454. SAM. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
PROSITE	PS01186. EGF_2. 1 hit. Uncertain. 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. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	284656.
SOURCE	Search...

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Entry information

Entry name

EPHA2_MOUSE

Accession

Primary (citable) accession number: Q03145
Secondary accession number(s): Q60633, Q62212

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1996
Last modified:	November 3, 2009
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents