GenomeNet

Database: UniProt
Entry: M3YWX7_MUSPF
LinkDB: M3YWX7_MUSPF
Original site: M3YWX7_MUSPF 
ID   M3YWX7_MUSPF            Unreviewed;       963 AA.
AC   M3YWX7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=EPHB2 {ECO:0000313|Ensembl:ENSMPUP00000015837.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000015837.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000015837.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   EMBL; AEYP01008276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01008277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004741281.1; XM_004741224.2.
DR   AlphaFoldDB; M3YWX7; -.
DR   STRING; 9669.ENSMPUP00000015837; -.
DR   Ensembl; ENSMPUT00000016078.1; ENSMPUP00000015837.1; ENSMPUG00000015942.1.
DR   eggNOG; KOG0196; Eukaryota.
DR   GeneTree; ENSGT00940000155503; -.
DR   HOGENOM; CLU_000288_141_4_1; -.
DR   InParanoid; M3YWX7; -.
DR   OMA; GAINCIC; -.
DR   OrthoDB; 1614410at2759; -.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR   GO; GO:0001540; F:amyloid-beta binding; 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:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR   GO; GO:0005005; F:transmembrane-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:0042113; P:B cell activation; IEA:Ensembl.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IEA:Ensembl.
DR   GO; GO:0071679; P:commissural neuron axon guidance; 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:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR   GO; GO:0007612; P:learning; IEA:Ensembl.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; IEA:Ensembl.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:Ensembl.
DR   GO; GO:0106028; P:neuron projection retraction; IEA:Ensembl.
DR   GO; GO:0021631; P:optic nerve morphogenesis; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:Ensembl.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
DR   GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR   GO; GO:0031915; P:positive regulation of synaptic plasticity; IEA:Ensembl.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:2000785; P:regulation of autophagosome assembly; IEA:Ensembl.
DR   GO; GO:0030193; P:regulation of blood coagulation; 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:0099557; P:trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; IEA:Ensembl.
DR   GO; GO:0001655; P:urogenital system development; IEA:Ensembl.
DR   CDD; cd10477; EphR_LBD_B2; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05065; PTKc_EphR_B; 1.
DR   CDD; cd09552; SAM_EPH-B2; 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; IPR034238; EphB2_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; 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; 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:SF11; EPHRIN TYPE-B RECEPTOR 2; 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; SSF57184; Growth factor receptor domain; 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}; Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   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   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        520..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..179
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          301..411
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          412..507
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          598..861
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          890..954
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   ACT_SITE        723
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT   BINDING         604..612
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   BINDING         630
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        39..161
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        74..84
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   963 AA;  107386 MW;  96883C2EEAC84ACE CRC64;
     MDSTTATAEL GWIVHPPSGW EEVSGYDENM NTIRTYQVCN VFESSQNNWL RTKFIRRRGA
     HRIHVEMKFS VRDCSSIPSV PGSCKETFNL YYYEADYDSA TKTFPNWMEN PWVKVDTIAA
     DESFSQVDLG GRVMKINTEV RSFGPVSRSG FYLAFQDYGG CMSLIAVRVF YRKCPRVIQN
     GAVFQETLSG AESTSLVAAR GSCIANAEEV DVPIKLYCNG DGEWLVPIGR CMCKAGFEAA
     ENGTVCRGCP SGTFKANQGD EACTHCPINS RTTSEGATNC VCRNGYYRAD LDPLDMPCTT
     IPSAPQAVIS SVNETSLMLE WTPPRDSGGR EDLVYNIICK SCGSGRGACT RCGDNVQYAP
     RQLGLTEPRI YISDLLAHTQ YTFEIQAVNG VTDQSPFSPQ FASVNITTNQ AAPSAVSIMH
     QVSRTVDSIT LSWSQPDQPN GVILDYELQY YEKELSEYNA TAIKSPTNTV TVQGLKAGAI
     YVFQVRARTV AGYGRYSGKM YFQTMTEAEY QTSIQEKLPL IIGSSAAGLV FLIAVVVIAI
     VCNRRGFERA DSEYTDKLQH YTSGHMTPGM KIYIDPFTYE DPNEAVREFA KEIDISCVKI
     EQVIGAGEFG EVCSGHLKLP GKREIFVAIK TLKSGYTEKQ RRDFLSEASI MGQFDHPNVI
     HLEGVVTKST PVMIITEFME NGSLDSFLRQ NDGQFTVIQL VGMLRGIAAG MKYLADMNYV
     HRDLAARNIL VNSNLVCKVS DFGLSRFLED DTSDPTYTSA LGGKIPIRWT APEAIQYRKF
     TSASDVWSYG IVMWEVMSYG ERPYWDMTNQ DVINAIEQDY RLPPPMDCPS ALHQLMLDCW
     QKDRNHRPKF GQIVNTLDKM IRNPNSLKAM APLSSGINLP LLDRTIPDYT SFNTVDEWLE
     AIKMGQYKES FANAGFTSFD VVSQMMMEDI LRVGVTLAGH QKKILNSIQV MRAQMNQIQS
     VEV
//
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