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Database: UniProt
Entry: P0C0K7
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Original site: P0C0K7 
ID   EPHB6_RAT               Reviewed;        1013 AA.
AC   P0C0K7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 3.
DT   14-MAY-2014, entry version 84.
DE   RecName: Full=Ephrin type-B receptor 6;
DE   AltName: Full=Tyrosine-protein kinase-defective receptor EPH-6;
DE   Flags: Precursor;
GN   Name=Ephb6;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
CC   -!- FUNCTION: Kinase-defective receptor for members of the ephrin-B
CC       family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion
CC       and migration by exerting both positive and negative effects upon
CC       stimulation with ephrin-B2. Inhibits JNK activation, T-cell
CC       receptor-induced IL-2 secretion and CD25 expression upon
CC       stimulation with ephrin-B2 (By similarity).
CC   -!- SUBUNIT: Interacts with CBL and EPHB1. Interacts with FYN; this
CC       interaction takes place in a ligand-independent manner (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive. Its extracellular domain is capable of promoting cell
CC       adhesion and migration in response to low concentrations of
CC       ephrin-B2, but its cytoplasmic domain is essential for cell
CC       repulsion and inhibition of migration induced by high
CC       concentrations of ephrin-B2 (By similarity).
CC   -!- PTM: Ligand-binding increases phosphorylation on tyrosine
CC       residues. Phosphorylation on tyrosine residues is mediated by
CC       transphosphorylation by the catalytically active EPHB1 in a
CC       ligand-independent manner. Tyrosine phosphorylation of the
CC       receptor may act as a switch on the functional transition from
CC       cell adhesion/attraction to de-adhesion/repulsion (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Ephrin receptor subfamily.
CC   -!- SIMILARITY: Contains 1 Eph LBD (Eph ligand-binding) domain.
CC   -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
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DR   EMBL; AABR03031938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001101327.1; NM_001107857.1.
DR   UniGene; Rn.125930; -.
DR   ProteinModelPortal; P0C0K7; -.
DR   STRING; 10116.ENSRNOP00000019720; -.
DR   PhosphoSite; P0C0K7; -.
DR   PaxDb; P0C0K7; -.
DR   PRIDE; P0C0K7; -.
DR   Ensembl; ENSRNOT00000019720; ENSRNOP00000019720; ENSRNOG00000014367.
DR   GeneID; 312275; -.
DR   KEGG; rno:312275; -.
DR   UCSC; RGD:1306163; rat.
DR   CTD; 2051; -.
DR   RGD; 1306163; Ephb6.
DR   eggNOG; COG0515; -.
DR   GeneTree; ENSGT00740000115081; -.
DR   HOGENOM; HOG000233856; -.
DR   HOVERGEN; HBG062180; -.
DR   InParanoid; P0C0K7; -.
DR   KO; K05114; -.
DR   OMA; EQAVAIQ; -.
DR   OrthoDB; EOG7VTDM6; -.
DR   PhylomeDB; P0C0K7; -.
DR   TreeFam; TF314013; -.
DR   NextBio; 664743; -.
DR   PRO; PR:P0C0K7; -.
DR   Genevestigator; P0C0K7; -.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR   GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0035898; P:parathyroid hormone secretion; IEA:Ensembl.
DR   Gene3D; 1.10.150.50; -; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR027936; Eph_TM.
DR   InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR   InterPro; IPR003961; Fibronectin_type3.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR   InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR   Pfam; PF14575; EphA2_TM; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51550; EPH_LBD; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR   PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Glycoprotein; Membrane;
KW   Nucleotide-binding; Receptor; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     31       By similarity.
FT   CHAIN        32   1013       Ephrin type-B receptor 6.
FT                                /FTId=PRO_0000042113.
FT   TOPO_DOM     32    590       Extracellular (Potential).
FT   TRANSMEM    591    611       Helical; (Potential).
FT   TOPO_DOM    612   1013       Cytoplasmic (Potential).
FT   DOMAIN       33    231       Eph LBD.
FT   DOMAIN      363    478       Fibronectin type-III 1.
FT   DOMAIN      479    574       Fibronectin type-III 2.
FT   DOMAIN      662    911       Protein kinase.
FT   DOMAIN      940   1004       SAM.
FT   NP_BIND     668    676       ATP (By similarity).
FT   MOTIF      1011   1013       PDZ-binding (Potential).
FT   COMPBIAS    167    172       Poly-Ser.
FT   COMPBIAS    213    360       Cys-rich.
FT   COMPBIAS    873    876       Poly-Pro.
FT   CARBOHYD    472    472       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1013 AA;  110313 MW;  7D62A6C0DBCE2BCB CRC64;
     MASENTAGSG SRVAGMVYSL WLLVLGPSVL ALEEVLLDTT GETSEIGWLT YPPGGWDEVS
     VLDDQRRLTR TFEACHVAGL PPGSGQDNWL QTHFVERRGA QRAHIRLHFS VRACSSLGVS
     GGTCRETFTL YYRQADEPDS PDSISAWHLK RWTKVDTIAA DESFPASSSS SSWAVGPHRT
     DQRVGLQLNV KERSFGPLTQ RGFYVAFQDT GACLALVAVK LFSYTCPSVL RAFASFPETQ
     ASGAGGASLV AAVGTCVAHA EPEEDGVGGQ AGGSPPRLHC NGEGRWMVAV GGCRCQPGHQ
     PARGDKLCQA CPEGSYKALP GNVPCSPCPA RSHSPDPAAP VCPCLQGFYR ASSDPPEAPC
     TGPPSAPREL WFEVQGSALM LHWRLPQELG GRGDLLFNVV CKECGGHKEP SSGGMCRRCR
     DEVHFDPRQR GLTESRVLVG GLRAHVPYIL EVQAVNGVSE LSPDPPQAAA INVSTSHEVP
     SAVPVMHQVS RAANSITVSW PQPEQTNGNI LDYQLRYYDQ AEDESHSFTM TSETNTATVT
     RLSPGHIYGF QVRARTAAGH GPYGGKVYFQ TLPQGELSSQ LPEKLSLVIG SILGALAFLL
     LAAITVLAVI FQRKRRGTGY TEQLQQYSSP GLGVKYYIDP STYDDPCQAI RELAREVDPT
     YIKIEEVIGA GSFGEVRRGR LQPRGRREQA VAIQALWAGG AESLKMTFLG RAALLGQFQH
     PNILRLEGVV TRSRPVMVLT ELMELGPLDS FLRQREGQFS SLQLVAMQRG VAAAMQYLSS
     FAFVHRALSA RSVLVNSHLV CKVARLGHSP QGSSSLLRWA APEVITHGKY TTSSDVWSFG
     ILMWEVMSYG ERPYWDMSDQ EVLNAIEQEF RLPPPPGCPT GLHLLMLDTW QKDRARRPHF
     DQLVAAFDKM IRKPDTLQAE GSSGDRPSQA LLNPVALDFP CLDSPQAWLS AIGLECYQDN
     FSKFGLSTFS DVAQLSLEDL PGLGITLAGH QKKLLHNIQL LQQHLRQPGS VEV
//
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