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P54758 (EPHA6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin type-A receptor 6
EC=2.7.10.1
Alternative name(s):
EPH homology kinase 2
Short name=EHK-2
Gene names
Name:Epha6
Synonyms:Ehk-2, Ehk2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1035 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

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 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Brain.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 10351013Ephrin type-A receptor 6
PRO_0000016817

Regions

Topological domain23 – 549527Extracellular Potential
Transmembrane550 – 57021Helical; Potential
Topological domain571 – 1035465Cytoplasmic Potential
Domain33 – 211179Eph LBD
Domain330 – 434105Fibronectin type-III 1
Domain438 – 53396Fibronectin type-III 2
Domain630 – 943314Protein kinase
Domain960 – 102465SAM
Nucleotide binding636 – 6449ATP By similarity
Motif1033 – 10353PDZ-binding Potential
Compositional bias193 – 327135Cys-rich

Sites

Active site7971Proton acceptor By similarity
Binding site6621ATP By similarity

Amino acid modifications

Modified residue6051Phosphotyrosine; by autocatalysis Potential
Modified residue6111Phosphotyrosine; by autocatalysis Potential
Modified residue8301Phosphotyrosine; by autocatalysis Potential
Modified residue9771Phosphotyrosine; by autocatalysis Potential
Glycosylation3421N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P54758 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 5ADEDB20A8B5AD95

FASTA1,035116,209
        10         20         30         40         50         60 
MGGCEVREFL LQFGFFLPLL TAWTGDCSHV SNQVVLLDTS TVMGELGWKT YPLNGWDAIT 

        70         80         90        100        110        120 
EMDEHNRPIH TYQVCNVMEP NQNNWLRTNW ISRDAAQKIY VEMKFTLRDC NSIPWVLGTC 

       130        140        150        160        170        180 
KETFTLYYIE SDESHGTKFK PSQYIKIDTI AADESFTQMD LGDRILKLNT EVREVGPIER 

       190        200        210        220        230        240 
KGFYLAFQDI GACIALVSVR VFYKKCPFTV RNLAMFPDTI PRVDSSSLVE VRGSCVKSSE 

       250        260        270        280        290        300 
ERDTPKLYCG ADGDWLVPLG RCICTTGYEE IEGSCHACRP GFYKAFAGNT KCSKCPPHSS 

       310        320        330        340        350        360 
TFVEATSVCH CEKGYFRAEK DPPSMACTRP PSAPRNVAFN INETALILEW SPPSDTGGRK 

       370        380        390        400        410        420 
DLTYSVICKK CGVDASQCED CGAGLRFIPR PTGLINNSVV VLDFVSHVNY TFEIEAMNGV 

       430        440        450        460        470        480 
SELSISPKPF TAITVTTDQD APSLIGMMRK DWASQNSLAL SWQAPAFSNG AILDYEIKYY 

       490        500        510        520        530        540 
EKEHEQLTYS STRSKAPSVI ITGLKPATTY IFHIRVRTAT GYSGYSQKFE FETGDETSDM 

       550        560        570        580        590        600 
AAEQGQILVI ATAAVGGFTL LVILTLFFLI TGRCQWYIKA KMKSEEKRRT HLQNSHLRFP 

       610        620        630        640        650        660 
GIKTYIDPDT YEDPSLAVHE FEKEIDPSRI RIERVIGAGE FGEVCSGRLK TPGKREIPVA 

       670        680        690        700        710        720 
IKTLKGGHMD RQRRDFLREA SIMGQFDHPN IIRLEGVVTK RSFPAIGVEA FCPSFLRAGF 

       730        740        750        760        770        780 
LNGIQAPHPV TAGGSLPPRI PAGRPVMIVV EYMENGSLDS FLRKHDGHFT VIQLVGMLRG 

       790        800        810        820        830        840 
IASGMKYLSD MGYVHRDLAA RNILVNSNLV CKVSDFGLSR VLEDDPEAAY TTTGGKIPIR 

       850        860        870        880        890        900 
WTAPEAIAYR KFSSASDVWS YGIVMWEVMS YGERPYWEMS NQDVILSIEE GYRLPAPMGC 

       910        920        930        940        950        960 
PPSLHQLMLH CWQKERNHRP KFTDIVSFLD KLIRNPSALH TLVEDILVMP ESPGDVPEYP 

       970        980        990       1000       1010       1020 
LFVTVGDWLD SIKMGQYKSN FMAAGFTTFD LISRMSIEDI RRIGVILIGH QRRIVSSIQT 

      1030 
LRLHMMHIQE KGFHV

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Ehk-1 and Ehk-2: two novel members of the Eph receptor-like tyrosine kinase family with distinctive structures and neuronal expression."
Maisonpierre P.C., Barrezueta N.X., Yancopoulos G.D.
Oncogene 8:3277-3288(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-948.
Strain: Sprague-Dawley.
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AABR03078339 Genomic DNA. No translation available.
AABR03079251 Genomic DNA. No translation available.
AABR03078729 Genomic DNA. No translation available.
AABR03078861 Genomic DNA. No translation available.
AABR03078320 Genomic DNA. No translation available.
AABR03078411 Genomic DNA. No translation available.
AABR03078368 Genomic DNA. No translation available.
AABR03080204 Genomic DNA. No translation available.
AABR03000001 Genomic DNA. No translation available.
IPIIPI00958321.
PIRS51605.

3D structure databases

ProteinModelPortalP54758.
SMRP54758. Positions 33-207, 617-937, 957-1029.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000049409.

PTM databases

PhosphoSiteP54758.

Proteomic databases

PaxDbP54758.
PRIDEP54758.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:1304614. rat.

Organism-specific databases

RGD1304614. Epha6.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidP54758.
OrthoDBEOG4FR0QX.

Gene expression databases

ArrayExpressP54758.
GenevestigatorP54758.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.40.10. 2 hits.
InterProIPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR021129. SAM_type1.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016257. Tyr_kinase_ephrin_rcpt.
IPR001426. Tyr_kinase_rcpt_V_CS.
[Graphical view]
PfamPF01404. Ephrin_lbd. 1 hit.
PF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 2 hits.
PF00536. SAM_1. 1 hit.
[Graphical view]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. FN_III-like. 2 hits.
SSF49785. Gal_bind_like. 1 hit.
SSF57184. Grow_fac_recept. 1 hit.
SSF56112. Kinase_like. 1 hit.
SSF47769. SAM_homology. 1 hit.
PROSITEPS01186. 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]
ProtoNetSearch...

Entry information

Entry nameEPHA6_RAT
AccessionPrimary (citable) accession number: P54758
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 16, 2006
Last modified: April 3, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents