ID   EPHB6_PANTR             Reviewed;        1020 AA.
AC   P0C0K6;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 4.
DT   03-AUG-2022, entry version 93.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The chimpanze genome sequencing consortium;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AADA01063189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AADA01251555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0C0K6; -.
DR   SMR; P0C0K6; -.
DR   STRING; 9598.ENSPTRP00000033908; -.
DR   PaxDb; P0C0K6; -.
DR   eggNOG; KOG0196; Eukaryota.
DR   InParanoid; P0C0K6; -.
DR   Proteomes; UP000002277; Unplaced.
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   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; IPR009030; Growth_fac_rcpt_cys_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   SUPFAM; SSF57184; SSF57184; 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..1020
FT                   /note="Ephrin type-B receptor 6"
FT                   /id="PRO_0000042112"
FT   TOPO_DOM        32..597
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        598..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        619..1020
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          33..236
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT   DOMAIN          368..485
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          486..581
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          669..918
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          947..1011
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   MOTIF           1018..1020
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000255"
FT   BINDING         675..683
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        479
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1020 AA;  110692 MW;  A3E63E2DF11BEEC5 CRC64;
     MATEGAAQLG NRVAGMVCSL WVLLLVSSVL ALEEVLLDTT GETSEIGWLT YPPGGWDEVS
     VLDDQRRLTR TFEACHVAGA PPGTGQDNWL QTHFVERRGA QRAHIRLHFS VRACSSLGVS
     GGTCRETFTL YYRQAEEPDS PDSVSSWHLK RWTKVDTIAA DESFPSSSSS SSSSSAAWAV
     GPHGAGQRAG LQLNVKERSF GPLTQRGFYV AFQDTGACLA LVAVRLFSYT CPAVLRSFAS
     FPETQASGAG GASLVAAVGT CVAHAEPEED GVGGQAGGSP PRLHCNGEGK WMVAVGGCRC
     QPGYQPARGD KACQACPRGL YKASAGNAPC SPCPARSHAA NPAAPVCPCL EGFYRASSDP
     PEAPCTGPPS APQELWFEVQ GSALMLHWRL PRELGGRGDL LFNVVCKECE GRQEPASGGG
     GTCRRCRDEV HFDPRQRGLT ESRVLVGGLR AHVPYILEVQ AVNGVSELSP DPPQAAAINV
     STSHEVPSAV PVVHQVSRAS NSITVSWPQP DQTNGNILDY QLRYYDQVED ESHSFTLTSE
     TNTATVTQLS PGHIYGFQVR ARTAAGHGPY GGKVYFQTLP QGELSSQLPE RLSLVIGSIL
     GALAFLLLAA ITVLAVVFQR KRRGTGYTEQ LQQYSSPGLG VKYYIDPSTY EDPCQAIREL
     AREVDPAYIK IEEVIGTGSF GEVRRGRLQP RGRREQTVAI QALWAGGAES LQMTFLGRAA
     VLGQFQHPNI LRLEGVVTKS RPLMVLTEFM ELGPLDSFLR QREGQFSSLQ LVAMQRGVAA
     AMQYLSSFAF VHRSLSAHSV LVNSHLVCKV ARLGHSPQGP SCLLRWAAPE VIAHGKHTTS
     SDVWSFGILM WEVMSYGERP YWDMSEQEVL NAIEQEFRLP PPPGCPPGLH LLMLDTWQKD
     RARRPHFDQL VAAFDKMIRK PDTLQACGDP GERPSQALLT PVALDFPCLD SPQAWLSAIG
     LECYQDNFSK FGLCTFSDVA QLSLEDLPAL GITLAGHQKK LLHHIQLLQQ HLRQQGSVEV