ID A0A2R9B459_PANPA Unreviewed; 1031 AA.
AC A0A2R9B459;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:ENSPPAP00000022266.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000022266.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000022266.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000022266.1}
RP IDENTIFICATION.
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 EMBL; AJFE02018402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9B459; -.
DR STRING; 9597.ENSPPAP00000022266; -.
DR Ensembl; ENSPPAT00000045074.1; ENSPPAP00000022266.1; ENSPPAG00000034296.1.
DR GeneTree; ENSGT00940000158024; -.
DR Proteomes; UP000240080; Chromosome 3.
DR Bgee; ENSPPAG00000034296; Expressed in placenta and 6 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008046; F:axon guidance receptor activity; IEA:Ensembl.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IEA:Ensembl.
DR GO; GO:0022038; P:corpus callosum development; IEA:Ensembl.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0048546; P:digestive tract morphogenesis; IEA:Ensembl.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR GO; GO:0001655; P:urogenital system development; IEA:Ensembl.
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, ECO:0000256|PIRSR:PIRSR000666-
KW 2}; Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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:UP000240080};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
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 592..615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..250
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 372..484
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 485..578
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 666..929
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 958..1022
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 791
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 672..680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 698
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 114..232
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 149..159
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 1031 AA; 113962 MW; FA92063B8282E459 CRC64;
MAKAERWPRA DPLPPSLAPQ KLNRNEEPPC LPRSLPPSFP PPPLRRPLPP LPPPGASAGL
VLNCGGIWLE GEGTLMDTKW VTSELAWTSH PESGWEEVSG YDEAMNPIRT YQVCNVRESS
QNNWLRTGFI WRRDVQRVYV ELKFTVRDCN SIPNIPGSCK ETFNLFYYEA DSDVASASSP
FWMENPYVKV DTIAPDESFS RLDAGRVNTK VRSFGPLSKA GFYLAFQDQG ACMSLISVRA
FYKKCASTTA GFALFPETLT GAEPTSLVIA PGTCIPNAVE VSVPLKLYCN GDGEWMVPVG
ACTCATGHEP AAKESQCRPC PPGSYKAKQG EGPCLPCPPN SRTTSPAASI CTCHNNFYRA
DSDSADSACT TVPSPPRGVI SNVNETSLIL EWSEPRDLGG RDDLLYNVIC KKCHGAGGAS
ACSRCDDNVE FVPRQLGLTE RRVHISHLLA HTRYTFEVQA VNGVSGKSPL PPRYAAVNIT
TNQAAPSEVP TLRLHSSSGS SLTLSWAPPE RPNGVILDYE MKYFEKSEGI ASTVTSQMNS
VQLDGLRPDA RYVVQVRART VAGYGQYSRP AEFETTSERG SGAQQLQEQL PLIVGSATAG
LVFVVAVVVI AIVCLRKQRH GSDSEYTEKL QQYIAPGMKV YIDPFTYEDP NEAVREFAKE
IDVSCVKIEE VIGAGEFGEV CRGRLKQPGR REVFVAIKTL KVGYTERQRR DFLSEASIMG
QFDHPNIIRL EGVVTKSRPV MILTEFMENC ALDSFLRLND GQFTVIQLVG MLRGIAAGMK
YLSEMNYVHR DLAARNILVN SNLVCKVSDF GLSRFLEDDP SDPTYTSSLG GKIPIRWTAP
EAIAYRKFTS ASDVWSYGIV MWEVMSYGER PYWDMSNQDV INAVEQDYRL PPPMDCPTAL
HQLMLDCWVR DRNLRPKFSQ IVNTLDKLIR NAASLKVIAS AQSGMSQPLL DRTVPDYTTF
TTVGDWLDAI KMGRYKESFI SAGFASFDLV AQMTAEDLLR IGVTLAGHQK KILSSIQDMR
LQMNQTLPVQ V
//
