EPHB6_RAT
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-AUG-2022, entry version 128.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., 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., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., 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., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- FUNCTION: Kinase-defective receptor for members of the ephrin-B family.
CC Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration
CC by exerting both positive and negative effects upon stimulation with
CC ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2
CC secretion and CD25 expression upon stimulation with ephrin-B2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CBL and EPHB1. Interacts with FYN; this
CC interaction takes place in a ligand-independent manner (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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 ephrin-B2,
CC but its cytoplasmic domain is essential for cell repulsion and
CC inhibition of migration induced by high concentrations of ephrin-B2 (By
CC similarity). {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- PTM: Ligand-binding increases phosphorylation on tyrosine residues.
CC Phosphorylation on tyrosine residues is mediated by
CC transphosphorylation by the catalytically active EPHB1 in a ligand-
CC independent manner. Tyrosine phosphorylation of the receptor may act as
CC a switch on the functional transition from cell adhesion/attraction to
CC de-adhesion/repulsion (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AABR03031938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001101327.1; NM_001107857.1.
DR AlphaFoldDB; P0C0K7; -.
DR SMR; P0C0K7; -.
DR STRING; 10116.ENSRNOP00000019720; -.
DR GlyGen; P0C0K7; 1 site.
DR iPTMnet; P0C0K7; -.
DR PhosphoSitePlus; 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; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000160399; -.
DR HOGENOM; CLU_000288_141_4_1; -.
DR InParanoid; P0C0K7; -.
DR OMA; PQGPSCM; -.
DR OrthoDB; 933071at2759; -.
DR PhylomeDB; P0C0K7; -.
DR TreeFam; TF314013; -.
DR Reactome; R-RNO-2682334; EPH-Ephrin signaling.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-3928664; Ephrin signaling.
DR Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
DR PRO; PR:P0C0K7; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000014367; Expressed in thymus and 19 other tissues.
DR Genevisible; P0C0K7; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
DR GO; GO:0050798; P:activated T cell proliferation; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:2000525; P:positive regulation of T cell costimulation; ISO:RGD.
DR GO; GO:0002456; P:T cell mediated immunity; ISO:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0001806; P:type IV hypersensitivity; ISO:RGD.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
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; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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; Glycoprotein; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000250"
FT CHAIN 32..1013
FT /note="Ephrin type-B receptor 6"
FT /id="PRO_0000042113"
FT TOPO_DOM 32..590
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..1013
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..231
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 363..478
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 479..574
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 662..911
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 940..1004
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT MOTIF 1011..1013
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT BINDING 668..676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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
