ID   D3ZH39_RAT              Unreviewed;      1048 AA.
AC   D3ZH39;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Ephrin type-B receptor 3 {ECO:0000256|ARBA:ARBA00040789};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=Ephb3 {ECO:0000313|Ensembl:ENSRNOP00000039489.3,
GN   ECO:0000313|RGD:1305602};
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 {ECO:0000313|Ensembl:ENSRNOP00000039489.3, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000039489.3, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000039489.3,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
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).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000039489.3}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000039489.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001171};
CC   -!- SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer
CC       is composed of an ephrin dimer and a receptor dimer. Oligomerization is
CC       probably required to induce biological responses.
CC       {ECO:0000256|ARBA:ARBA00038546}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   RefSeq; NP_001099338.1; NM_001105868.1.
DR   AlphaFoldDB; D3ZH39; -.
DR   SMR; D3ZH39; -.
DR   STRING; 10116.ENSRNOP00000039489; -.
DR   PaxDb; 10116-ENSRNOP00000039489; -.
DR   Ensembl; ENSRNOT00000044896.4; ENSRNOP00000039489.3; ENSRNOG00000031801.5.
DR   KEGG; rno:287989; -.
DR   AGR; RGD:1305602; -.
DR   CTD; 2049; -.
DR   RGD; 1305602; Ephb3.
DR   eggNOG; KOG0196; Eukaryota.
DR   GeneTree; ENSGT00940000158024; -.
DR   HOGENOM; CLU_000288_141_0_1; -.
DR   OMA; TSACSRC; -.
DR   OrthoDB; 1614410at2759; -.
DR   TreeFam; TF315608; -.
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   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000031801; Expressed in stomach and 18 other cell types or tissues.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008046; F:axon guidance receptor activity; ISO:RGD.
DR   GO; GO:0005003; F:ephrin receptor activity; ISO:RGD.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR   GO; GO:0007411; P:axon guidance; ISO:RGD.
DR   GO; GO:0007413; P:axonal fasciculation; ISO:RGD.
DR   GO; GO:0016477; P:cell migration; ISO:RGD.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; ISO:RGD.
DR   GO; GO:0022038; P:corpus callosum development; ISO:RGD.
DR   GO; GO:0060996; P:dendritic spine development; ISO:RGD.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; ISO:RGD.
DR   GO; GO:0048546; P:digestive tract morphogenesis; ISO:RGD.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; ISO:RGD.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR   GO; GO:0050770; P:regulation of axonogenesis; ISO:RGD.
DR   GO; GO:0022407; P:regulation of cell-cell adhesion; ISO:RGD.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; ISO:RGD.
DR   GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
DR   GO; GO:0048538; P:thymus development; ISO:RGD.
DR   GO; GO:0001655; P:urogenital system development; ISO:RGD.
DR   CDD; cd10478; EphR_LBD_B3; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05065; PTKc_EphR_B; 1.
DR   CDD; cd00185; TNFRSF; 1.
DR   Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR   InterPro; IPR027936; Eph_TM.
DR   InterPro; IPR034245; EphB3_rcpt_lig-bd.
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; IPR017441; Protein_kinase_ATP_BS.
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; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR   InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR   PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR   PANTHER; PTHR46877:SF6; EPHRIN TYPE-B RECEPTOR 3; 1.
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; PF00536; SAM_1; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM01411; Ephrin_rec_like; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS51550; EPH_LBD; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
SQ   SEQUENCE   1048 AA;  115537 MW;  340974E05953244D CRC64;
     MAGARPPPGL LPLLAPLLLP LLLPAGCRAL EETLMDTKWV TSELAWTSHP ESGWEEVSGY
     DEAMNPIRTY QVCNVRESSQ NNWLRTGFIW RREVQRVYVE LKFTVRDCNS IPNIPGSCKE
     TFNLFYYEAD SDVASASSPF WMENPYVKVD TIAPDESFSR LDAGRVNTKV RSFGPLSKAG
     FYLAFQDQGA CMSLISVRAF YKKCASTTAG FALFPETLTG AEPTSLVIAP GTCIANAVEV
     SVPLKLYCNG DGEWMVPVGA CTCATGHEPA AKETQCRACP PGSYKAKQGE GPCLPCPPNS
     RTTSPAASIC TCHNNFYRAD SDTADSACTT VPSPPRGVIS NVNETSLILE WSEPRDLGGR
     DDLLYNVICK KCRGSSGAGG PATCSRCDDN VEFEPRQLGL TERRVHISHL LAHTRYTFEV
     QAVNGVSGKS PLPPRYAAVN ITTNQAAPSE VPTLHLHSSS GSSLTLSWAP PERPNGVILD
     YEMKYFEKSK GIASTVTSQK NSVQLDGLQP DARYVVQVRA RTVAGYGQYS RPAEFETTSE
     RGSGAQQLQE QLPLIVGSTV AGFVFMVVVV VIALVCLRKQ RQGPDAEYTE KLQQYVAPRM
     KVYIDPFTYE DPNEAVREFA KEIDVSCVKI EEVIGAGEFG EVCRGRLKLP GRREVFVAIK
     TLKVGYTERQ RRDFLSEASI MGQFDHPNII RLEGVVTKSR PVMILTEFME NCALDSFLRL
     NDGQFTVIQL VGMLRGIAAG MKYLSEMNYV HRDLAARNIL VNSNLVCKVS DFGLSRFLED
     DPSDPTYTSS LGGKIPIRWT APEAIAYRKF TSASDVWSYG IVMWEVMSYG ERPYWDMSNQ
     DVINAVEQDY RLPPPMDCPT ALHQLMLDCW VRDRNLRPKF SQIVNTLDKL IRNAASLKVI
     ASAPSGMSQP LLDRTVPDYT TFTTVGDWLD AIKMGRYKES FVGAGFASFD LVAQMTAEDL
     LRIGVTLAGH QKKILSSIQD MRLQMNQTLP VQEVCPKPLH IEDGLEEGVI SPPQMPQGPG
     LPALQSGIFT TQIWLCFSSG GPGRVGWG
//