Ephrin type-A receptor 4-A precursor - Xenopus laevis (African clawed frog)

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Q91845 (EPA4A_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ephrin type-A receptor 4-A
EC=2.7.10.1

Alternative name(s):
Tyrosine-protein kinase receptor SEK-1
Short name=xSEK-1

Gene names

Name:	epha4-a
Synonyms:	sek1

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	986 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Receptor tyrosine kinase which binds 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, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections By similarity.
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subcellular location	Cell membrane; Single-pass type I membrane protein By similarity. Early endosome By similarity. Note: Clustered upon activation and targeted to early endosome By similarity.
Developmental stage	Expression occurs in R3, R5 and transiently at lower levels in R2.
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily. Contains 1 Eph LBD (Eph ligand-binding) domain. Contains 2 fibronectin type-III domains. Contains 1 protein kinase domain. Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
Biological process	Cell adhesion Neurogenesis
Cellular component	Cell membrane Endosome Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW nervous system development Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of Rac GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of Rap GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	early endosome membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GPI-linked ephrin receptor activity Inferred from sequence or structural similarity. Source: UniProtKB transmembrane-ephrin receptor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Potential

Chain

21 – 986

966

Ephrin type-A receptor 4-A

PRO_0000016810

Regions

Topological domain

21 – 547

527

Extracellular Potential

Transmembrane

548 – 569

Helical; Potential

Topological domain

570 – 986

417

Cytoplasmic Potential

Domain

30 – 209

180

Eph LBD

Domain

328 – 430

103

Fibronectin type-III 1

Domain

440 – 533

Fibronectin type-III 2

Domain

620 – 881

262

Protein kinase

Domain

911 – 975

SAM

Nucleotide binding

626 – 634

ATP By similarity

Motif

984 – 986

PDZ-binding Potential

Compositional bias

191 – 325

135

Cys-rich

Sites

Active site

745

Proton acceptor By similarity

Binding site

652

ATP By similarity

Amino acid modifications

Modified residue

595

Phosphotyrosine; by autocatalysis By similarity

Modified residue

601

Phosphotyrosine; by autocatalysis By similarity

Modified residue

778

Phosphotyrosine; by autocatalysis Potential

Modified residue

928

Phosphotyrosine; by autocatalysis Potential

Glycosylation

340

N-linked (GlcNAc...) Potential

Glycosylation

407

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q91845 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C34F4078DB3F025F
Show »

FASTA

986

109,841

        10         20         30         40         50         60 
MAGIVHGILF CGLFGLCWAV TGSRIYPASE VTLLDSRSVQ GELGWIASPL EGGWEEVSIM 

        70         80         90        100        110        120 
DEKNTPIRTY QVCNVMESSQ NNWLRTDWIP RSGAQRVYVE IKFTLRDCNS LPGVMGTCKE 

       130        140        150        160        170        180 
TFNLYYYESN NDKERFIRET QYVKIDTIAA DESFTQVDIG DRIMKLNTEV RDVGPLSKKG 

       190        200        210        220        230        240 
FYLAFQDVGA CIALVSVRVF YKKCPLTVRN LAQFPDTITG SDTSSLVEVR GSCVDNSEEK 

       250        260        270        280        290        300 
DVPKMYCGAD GEWLVPIGNC LCNAGFEEHN GGCQACKVGY YKALSTDAAC SKCPPHSYAL 

       310        320        330        340        350        360 
REGSTSCTCD RGYFRADTDP ASMPCTRPPS APQNLISNVN ETSVNLEWSP PQNSGGRPDV 

       370        380        390        400        410        420 
SYNLVCKRCG SDLTRCRPCG SGVHYSPQQN GLKTTKVSIT DLQAHTNYTF EVWSINGVSK 

       430        440        450        460        470        480 
QNPGQDQAVS VTVTTNQAAP STVTQIQPKD ITRHSVSLTW PEPERPNGVI LEYEVKYYEK 

       490        500        510        520        530        540 
DQNERTYRIV KTTSRSADIK GLNPLTAYVF HVRARTAAGY GEFSGPFEFT TNTVPSPMIG 

       550        560        570        580        590        600 
EGASPTVLLV SVAGSIVLVV ILIAAFVISR RRSKYSKAKQ EADEEKHLNQ GVKTYVDPFT 

       610        620        630        640        650        660 
YEDPNQAVRE FAKEIDASCI KIEKVIGVGE FGEVCSGRLK VPGKREIYVA IKTLKAGYTD 

       670        680        690        700        710        720 
KQRRDFLSEA SIMGQFDHPN IIHLEGVVTK CKPVMIITEY MENGSLDAFL RKNDGRFTVI 

       730        740        750        760        770        780 
QLVGILRGIG SGMKYLSDMS YVHRDLAARN ILVNSNLVCK VSDFGMSRVL EDDPEAAYTT 

       790        800        810        820        830        840 
RGGKIPIRWT APEAIAYRKF TSASDVWSYG IVMWEVMSYG ERPYWDMSNQ DVIKAIEEGY 

       850        860        870        880        890        900 
RLPPPMDCPI ALHQLMLDCW QKERSDRPKF GQIVSMLDKL IRNPNSLKRT GLDNSSRTNT 

       910        920        930        940        950        960 
TLLDPSSPEW SQVASVLDWL QAIKMERYKD NFTAAGYTSL EAVVHVNQDD LTRIGISSPS 

       970        980 
HQNKILSSVQ GMRTQMQQIQ GRMVPV

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References

[1]	"Expression of truncated Sek-1 receptor tyrosine kinase disrupts the segmental restriction of gene expression in the Xenopus and zebrafish hindbrain." Xu Q., Alldus G., Holder N., Wilkinson D.G. Development 121:4005-4016(1995) [PubMed: 8575301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X91191 mRNA. Translation: CAA62601.1.
RefSeq	NP_001090183.1. NM_001096714.1.
UniGene	Xl.57159.
3D structure databases
ProteinModelPortal	Q91845.
SMR	Q91845. Positions 29-205, 607-884, 910-981.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	779062.
KEGG	xla:779062.
Organism-specific databases
CTD	779062.
Xenbase	XB-GENE-6253098. epha4.
Phylogenomic databases
HOVERGEN	HBG062180.
Enzyme and pathway databases
BRENDA	2.7.10.1. 6726.
Family and domain databases
InterPro	IPR001090. Ephrin_rcpt_lig-bd. IPR003961. Fibronectin_type3. IPR008979. Galactose-bd-like. IPR013783. Ig-like_fold. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR001660. SAM. IPR013761. SAM/pointed. IPR011510. SAM_2. IPR001245. Ser-Thr/Tyr_kinase. IPR008266. Tyr_kinase_AS. IPR020635. Tyr_kinase_cat_dom. IPR016257. Tyr_kinase_ephrin_rcpt. IPR001426. Tyr_kinase_rcpt_V_CS. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 2 hits. G3DSA:1.10.150.50. SAM_type. 1 hit.
KO	K05105.
Pfam	PF01404. Ephrin_lbd. 1 hit. PF00041. fn3. 2 hits. PF07714. Pkinase_Tyr. 1 hit. PF07647. SAM_2. 1 hit. [Graphical view]
PIRSF	PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTS	PR00109. TYRKINASE.
SMART	SM00615. EPH_lbd. 1 hit. SM00060. FN3. 2 hits. SM00454. SAM. 1 hit. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF49265. FN_III-like. 2 hits. SSF49785. Gal_bind_like. 1 hit. SSF56112. Kinase_like. 1 hit. SSF47769. SAM_homology. 1 hit.
PROSITE	PS01186. EGF_2. 1 hit. Uncertain. 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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EPA4A_XENLA

Accession

Primary (citable) accession number: Q91845

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents