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Database: UniProt
Entry: A0A8C9D5F0_PANLE
LinkDB: A0A8C9D5F0_PANLE
Original site: A0A8C9D5F0_PANLE 
ID   A0A8C9D5F0_PANLE        Unreviewed;      1012 AA.
AC   A0A8C9D5F0;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   RecName: Full=Ephrin type-B receptor 6 {ECO:0000256|ARBA:ARBA00070274};
DE   AltName: Full=Tyrosine-protein kinase-defective receptor EPH-6 {ECO:0000256|ARBA:ARBA00077388};
GN   Name=EPHB6 {ECO:0000313|Ensembl:ENSPLOP00000015775.1};
OS   Panthera leo (Lion).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Pantherinae;
OC   Panthera.
OX   NCBI_TaxID=9689 {ECO:0000313|Ensembl:ENSPLOP00000015775.1, ECO:0000313|Proteomes:UP000694399};
RN   [1] {ECO:0000313|Ensembl:ENSPLOP00000015775.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Armstrong E.E., Taylor R.W., Miller D.E., Kaelin C., Barsh G., Hadly E.A.,
RA   Petrov D.;
RT   "Long live the king: chromosome-level assembly of the lion (Panthera leo)
RT   using linked-read, Hi-C, and long read data.";
RL   bioRxiv 0:0-0(2019).
RN   [2] {ECO:0000313|Ensembl:ENSPLOP00000015775.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSPLOP00000015775.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
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.
CC       {ECO:0000256|ARBA:ARBA00059300}.
CC   -!- SUBUNIT: Interacts with CBL and EPHB1. Interacts with FYN; this
CC       interaction takes place in a ligand-independent manner.
CC       {ECO:0000256|ARBA:ARBA00062552}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A8C9D5F0; -.
DR   Ensembl; ENSPLOT00000017467.1; ENSPLOP00000015775.1; ENSPLOG00000011477.1.
DR   GeneTree; ENSGT00940000160399; -.
DR   OMA; PQGPSCM; -.
DR   Proteomes; UP000694399; Chromosome A3.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; IEA:TreeGrafter.
DR   GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl.
DR   GO; GO:0007411; P:axon guidance; IEA:TreeGrafter.
DR   GO; GO:2000525; P:positive regulation of T cell costimulation; IEA:Ensembl.
DR   GO; GO:0001806; P:type IV hypersensitivity; IEA:Ensembl.
DR   CDD; cd10475; EphR_LBD_B6; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd00185; TNFRSF; 1.
DR   FunFam; 2.10.50.10:FF:000001; Ephrin type-A receptor 5; 1.
DR   FunFam; 2.60.40.10:FF:000059; Ephrin type-A receptor 6; 1.
DR   FunFam; 1.10.150.50:FF:000068; Ephrin type-B receptor 6; 1.
DR   FunFam; 1.10.510.10:FF:000470; Ephrin type-B receptor 6; 1.
DR   FunFam; 2.60.120.260:FF:000064; Ephrin type-B receptor 6; 1.
DR   FunFam; 2.60.40.10:FF:000508; ephrin type-B receptor 6; 1.
DR   FunFam; 2.60.40.1770:FF:000004; ephrin type-B receptor 6; 1.
DR   FunFam; 3.30.200.20:FF:000143; Ephrin type-B receptor 6; 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; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
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; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR   InterPro; IPR050449; Ephrin_rcpt_TKs.
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   PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR   PANTHER; PTHR46877:SF15; EPHRIN TYPE-B RECEPTOR 6; 1.
DR   Pfam; PF14575; EphA2_TM; 1.
DR   Pfam; PF25599; Ephrin_CRD; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF07699; Ephrin_rec_like; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF07647; SAM_2; 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   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; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000666-
KW   2}; Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000666-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694399};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..1012
FT                   /note="Ephrin type-B receptor 6"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5034235920"
FT   TRANSMEM        586..610
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..228
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          360..477
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          478..573
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          661..910
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          939..1003
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   BINDING         667..675
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   DISULFID        75..210
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        114..124
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   1012 AA;  109481 MW;  9F63F230E338C9A2 CRC64;
     MAAEGAARSG SGVAGMVCSL WVLGLASSVL ALEEVLLDTT GETSEIGWLT YPPGGWDEVS
     VLDDQRRLTR TFEACHVAGA PPGTGQDNWL QTHFVERRGA QRAHIRLHFS VRACASLGVA
     GGTCRETFTL YYRQAEEPDG PDSISSWHLK RWTKVDTIAA DESFPASSAW AVGPRGAGQR
     AGLQLNVKER SFGPLTQRGF YVAFQDTGAC LALVAVKLFS YTCPSVLRAF ASFPETQASG
     AGGASLVAAV GTCVAHAEPE EDGGGGQVGG SPPRLHCNGE GKWMVAVGGC RCQPGHQPAR
     GDKACQACPE GSYKAMAGNA PCLPCPARSH APDPASPVCP CLEGFYRAGS DPPEAPCTGP
     PSAPRELWFE VQGSVLMLHW RLPQELGGRG DLLFNVVCKE CGGHQEPGTG TPGTCRRCRD
     EVHFDPRQRG LTESRVLVGG LRAHVPYILE VQAVNGVSEL SPDPPQAAAI NVSTSHAVPS
     AVPALHQVSR ASNSITVSWP QPDQTNGNIL DYQLRYYDQA EDESHSFTLT SETNTATVTQ
     LSPGHIYGFQ VRARTAAGHG PYGGKVYFQT LPQGELSTQL PERLSLVIGS ILGALAFLLL
     AAITVLAVVF RRKRRGTGYT EQLQQYSSPG LGVKYYIDPS TYEDPCQAIR EFTREVDPAY
     IKIEEVIGAG SFGEVRRGRL QPRGRREQAV AIQALWAGGT ESLQMTFLGQ AAVLGQFQHP
     NILRLEGVVT KSRPLMVLTE LMELGPLDSF LRQREGQFSS LQLVAMQRGV AAAMQYLSSF
     AFVHRALSAH SVLVNSHLVC KVARLGHSPQ GPSCMLRWAA PEVIAHGKHT TSSDIWSFGI
     VMWEVMSYGE RPYWDMSDQE VLNAIEQEFR LPPPPGCPPG LHLLMLDTWQ KDRTQRPHFD
     QLVAAFDKMI RKPDTLQADG GPGDRPSQAL LNPVALDFPS LDSPQAWLLA IGLECYQENF
     SKFGLCTFSD VVQLGLEDLP ALGITLAGHQ KKLLHNIQLL QQHLTQPGSV EV
//
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