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 03-APR-2013, entry version 74.
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 IPI; IPI00203223; -.
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 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; ENSGT00700000104274; -.
DR HOGENOM; HOG000233856; -.
DR HOVERGEN; HBG062180; -.
DR InParanoid; P0C0K7; -.
DR KO; K05114; -.
DR OMA; KVYFQTL; -.
DR OrthoDB; EOG4PK272; -.
DR NextBio; 664743; -.
DR ArrayExpress; P0C0K7; -.
DR Genevestigator; P0C0K7; -.
DR GermOnline; ENSRNOG00000014367; Rattus norvegicus.
DR GO; GO:0005887; C:integral to 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:Compara.
DR GO; GO:0035898; P:parathyroid hormone secretion; IEA:Compara.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
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_cat_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; 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; SSF49265; FN_III-like; 2.
DR SUPFAM; SSF49785; Gal_bind_like; 1.
DR SUPFAM; SSF56112; Kinase_like; 1.
DR SUPFAM; SSF47769; SAM_homology; 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 2: Evidence at transcript level;
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 363 470 Fibronectin type-III 1.
FT DOMAIN 480 571 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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