ID A0A452QTP0_URSAM Unreviewed; 989 AA.
AC A0A452QTP0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=EPHA7 {ECO:0000313|Ensembl:ENSUAMP00000008982.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000008982.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000008982.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A452QTP0; -.
DR Ensembl; ENSUAMT00000010111.1; ENSUAMP00000008982.1; ENSUAMG00000007337.1.
DR GeneTree; ENSGT00940000160189; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05066; PTKc_EphR_A; 1.
DR CDD; cd09548; SAM_EPH-A7; 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; 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:SF9; EPHRIN TYPE-A RECEPTOR 7; 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}; 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:UP000291022};
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 546..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..189
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 310..420
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 438..533
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 624..885
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 914..978
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 749
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 630..638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 656
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 53..171
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 88..98
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 989 AA; 110808 MW; 95DD4D32BAADFE37 CRC64;
SLNLFAITTL PRSLVPTLAQ QTELEWISSP PNGWEEISGL DENYTPIRTY QVCQVMEPNQ
NNWLRTNWIS KGNAQRIFVE LKFTLRDCNS LPGVLGTCKE TFNLYYYETD YDTGRNIREN
LYVKIDTIAA DESFTQGDLG ERKMKLNTEV REIGPLSKKG FYLAFQDVGA CIALVSVKVY
YKKCWSIIEN LAIFPDTVTG SEFSSLVEVR GTCVSSAEEE AENSPRMHCS AEGEWLVPIG
KCICKAGYQQ KGDTCEPCGR GFYKSSSQDL QCSRCPTHSF SDKEGSSRCD CEDGYYRAPS
DPPYVACTRP PSAPQNLIFN INQTTVSLEW SPPADNGGRN DVTYRILCKR CSWEQGECVP
CGSNIGYMPQ QTGLEDNYVT VMDLLAHANY TFEVEAVNGV SDLSRSQRLF AAVSITTGQA
GMFFEFSHCL LTCLVQTAPS QVSGVMKERV LQRSVELSWQ EPEHPNGVIT EYEIKYYEKD
QRERTYSTVK TKSTSASINN LKPGTVYVFQ IRAFTAAGYG NYSPRLDVAT LEEATATAVS
SEQNPVIIIA VVAVAGTIIL VFMVFGFIIG RRHCGYSKAD QEGDEELYFH FKFPGTKTYI
DPETYEDPNR AVHQFAKELD ASCIKIERVI GAGEFGEVCS GRLKLPGKRD VAVAIKTLKV
GYTEKQRRDF LCEASIMGQF DHPNVVHLEG VVTRGKPVMI VIEFMENGAL DAFLRKHDGQ
FTVIQLVGML RGIAAGMRYL ADMGYVHRDL AARNILVNSN LVCKVSDFGL SRVIEDDPEA
VYTTTGGKIP VRWTAPEAIQ YRKFTSASDV WSYGIVMWEV MSYGERPYWD MSNQDVIKAI
EEGYRLPAPM DCPAGLHQLM LDCWQKERAE RPKFEQIVGI LDKMIRNPNS LKTPLGTCSR
PISPLLDQNT PDFTTFCSVG EWLQAIKMER YKDNFTAAGY NSLESVARMT IEDVMSLGIT
LVGHQKKIMS SIQTMRAQML HLHGTGIQV
//
