ID A0A2K5N530_CERAT Unreviewed; 982 AA.
AC A0A2K5N530;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JAN-2026, entry version 40.
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:ENSCATP00000032435.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000032435.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000032435.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCATP00000032435.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00051243};
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: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}.
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DR AlphaFoldDB; A0A2K5N530; -.
DR Ensembl; ENSCATT00000056702.1; ENSCATP00000032435.1; ENSCATG00000039267.1.
DR GeneTree; ENSGT00940000158024; -.
DR Proteomes; UP000233060; Unassembled WGS sequence.
DR Bgee; ENSCATG00000039267; Expressed in lung and 3 other cell types or tissues.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IEA:TreeGrafter.
DR GO; GO:0007411; P:axon guidance; IEA:TreeGrafter.
DR GO; GO:0016477; P:cell migration; IEA:UniProtKB-ARBA.
DR GO; GO:0031589; P:cell-substrate adhesion; IEA:UniProtKB-ARBA.
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 FunFam; 2.60.40.10:FF:000041; ephrin type-A receptor 3; 1.
DR FunFam; 1.10.150.50:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 2.10.50.10:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 2.60.40.1770:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 3.30.200.20:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 1.10.510.10:FF:000015; Ephrin type-B receptor 2; 1.
DR FunFam; 2.60.120.260:FF:000004; Ephrin type-B receptor 2; 1.
DR FunFam; 2.60.40.10:FF:000520; ephrin type-B receptor 3; 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; IPR034245; EphB3_rcpt_lig-bd.
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; 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; PF25599; Ephrin_CRD; 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, ECO:0000256|PIRSR:PIRSR000666-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000666-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 543..566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..201
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 323..435
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 436..529
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 617..880
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 909..973
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 742
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 623..631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 65..183
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 100..110
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 982 AA; 108502 MW; FEA586A1A805B101 CRC64;
RAAHRPPAGV ATPPASLPAG LWAPTLMDTK WVTSELAWTS HPESGWEEVS GYDEAMNPIR
TYQVCNVHES SQNNWLRTGF IWRRDVQRVY VELKFTVRDC NSIPNIPGSC KETFNLFYYE
ADSDVASASS PFWMENPYVK VDTIAPDESF SRLDAGRVNT KVRSFGPLSK AGFYLAFQDQ
GACMSLISVR AFYKKCASTT AGFALFPETL TGAEPTSLVI APGTCIPNAV EVSVPLKLYC
NGDGEWMVPV GACTCATGHE PAAKESQCRP CPPGSYKAKQ GEGPCLPCPP NSRTTSPAAS
ICTCHNNFYR ADSDSADSAC TTVPSPPRGV ISNVNETSLI LEWSEPRDLG GRDDLLYNVI
CKKCHGAGGA SVCSRCDDNV EFVPRQLGLT ERRVHISHLL AHTRYTFEVQ AVNGVSGKSP
LPPRYAAVNI TTNQAAPSEV PTLRLHSSSG SSLTLSWAPP ERPNGVILDY EMKYFEKSEG
IASTVTSQMN SVQLDGLRPD ARYVVQVRAR TVAGYGQYSR PAEFETTSER GSGAQQLQEQ
LPLIVGSATA GLVFVVAVVV IAIVCLRKQR HGSDSEYTEK LQQYIAPGMK VYIDPFTYED
PNEAVREFAK EIDVSCVKIE EVIGAGEFGE VCRGRLKQPG RREVFVAIKT LKVGYTERQR
RDFLSEASIM GQFDHPNIIR LEGVVTKSRP VMILTEFMEN CALDSFLRLN DGQFTVIQLV
GMLRGIAAGM KYLSEMNYVH RDLAARNILV NSNLVCKVSD FGLSRFLEDD PSDPTYTSSL
GGKIPIRWTA PEAIAYRKFT SASDVWSYGI VMWEVMSYGE RPYWDMSNQD VINAVEQDYR
LPPPMDCPTA LHQLMLDCWV RDRNLRPKFS QIVNTLDKLI RNAASLKVIA SAQSGMSQPL
LDRTVPDYTT FTTVGDWLDA IKMGRYKESF VSAGFASFDL VAQMTAEDLL RIGVTLAGHQ
KKILSSIQDM RLQMNQTLPV QV
//
