ID A0A452FIZ5_CAPHI Unreviewed; 950 AA.
AC A0A452FIZ5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 32.
DE RecName: Full=Ephrin type-A receptor 1 {ECO:0000256|ARBA:ARBA00072212};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=EPHA1 {ECO:0000313|Ensembl:ENSCHIP00000024062.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000024062.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000024062.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000024062.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCHIP00000024062.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-
CC bound ephrin-A family ligands residing on adjacent cells, leading to
CC contact-dependent bidirectional signaling into neighboring cells. The
CC signaling pathway downstream of the receptor is referred to as forward
CC signaling while the signaling pathway downstream of the ephrin ligand
CC is referred to as reverse signaling. Binds with a low affinity EFNA3
CC and EFNA4 and with a high affinity to EFNA1 which most probably
CC constitutes its cognate/functional ligand. Upon activation by EFNA1
CC induces cell attachment to the extracellular matrix inhibiting cell
CC spreading and motility through regulation of ILK and downstream RHOA
CC and RAC. Also plays a role in angiogenesis and regulates cell
CC proliferation. May play a role in apoptosis.
CC {ECO:0000256|ARBA:ARBA00059287}.
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: Homodimer. Forms a signaling complex with LCK; PTK2B/PYK2 and
CC PI3-kinase upon activation by EFNA1; regulates T-lymphocytes migration.
CC Interacts (via SAM domain) with ILK (via ANK repeats); stimulated by
CC EFNA1 but independent of the kinase activity of EPHA1. Interacts
CC (kinase activity-dependent) with PTK2/FAK1.
CC {ECO:0000256|ARBA:ARBA00062471}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
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DR EMBL; LWLT01000003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452FIZ5; -.
DR Ensembl; ENSCHIT00000031922.1; ENSCHIP00000024062.1; ENSCHIG00000021379.1.
DR GeneTree; ENSGT00940000160920; -.
DR OMA; SCWSHDR; -.
DR Proteomes; UP000291000; Chromosome 4.
DR Bgee; ENSCHIG00000021379; Expressed in rumen and 15 other cell types or tissues.
DR GO; GO:0030425; C:dendrite; IEA:TreeGrafter.
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:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd10479; EphR_LBD_A1; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd12841; TM_EphA1; 1.
DR FunFam; 1.10.150.50:FF:000029; Ephrin type-A receptor 1; 1.
DR FunFam; 2.60.40.10:FF:000626; Ephrin type-A receptor 1; 1.
DR FunFam; 3.30.200.20:FF:000317; Ephrin type-A receptor 1; 1.
DR FunFam; 2.60.120.260:FF:000023; Ephrin type-A receptor 2; 1.
DR FunFam; 2.10.50.10:FF:000001; Ephrin type-A receptor 5; 1.
DR FunFam; 2.60.40.10:FF:000059; Ephrin type-A receptor 6; 1.
DR FunFam; 1.10.510.10:FF:000268; Receptor protein-tyrosine kinase; 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; IPR034251; EphA1_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; 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:SF20; RECEPTOR PROTEIN-TYROSINE KINASE; 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; 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 Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000666-
KW 2}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {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 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:UP000291000};
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};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 519..539
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 303..416
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 418..509
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 598..859
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 887..950
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 76..88
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 950 AA; 105530 MW; C8A72D36ECD93C2E CRC64;
MDTSKAQEEL GWLLDPPEDG WSEVQQILNG TPLYMYQDCP VEEGRDTDHW LRTNWIYRGE
EASRVHVELQ FTVRDCKSFP GEAGPLGCKE TFNLLYMESD QDVGIQLRRP LFQKVTTVAA
DQSFTVRDLA SRAVKMNVER CSLGRLTRRG LYLAFHNPGA CVALVSVRVF YQRCPETVHG
LARFPDTLPG PGGLAEVAGT CLPHAHISPG PSGAPLMHCS PDGEWLVPVG RCHCEPGYEE
GSSDAEECLA CPSGSYRSDV DAPQCLKCPQ HSTAEAEGAT ECACESGHYR APGEGPHAAC
TRPPSTPRNL SFSISGTQLS LRWEPPADLG EREDIRYNVE CSQCQGAALD WGPCQPCGAG
VRFSAGPSGL TASSVRVDGL DPHANYTFSV EAQNGVSGLG ASKPASASLS INMGSAESLS
GLSLRLVKKA PRQLELTWAG SRPRSPEGNL SYELHVLNQD EERYQMVLEP RVLLTELQPD
TTYIVRVRMV TPLGPGPFSA DHEFRTSPPV SSVLTGGEIV AIIFGLLLGV ALLLGMLVFR
SRRAQRRRHQ RQQRQRDRVA DGDREDKLWL KPYVDLQAYE DPAQGALDFT QELDPAWLVV
DTVIGEGEFG EVYRGSLRLP SQDCKIVAIK TLKDTSPDGQ WWNFLREATI MGQFNHPHIL
HLEGVVTKRK PIMIITEFME NGALDAFLRE REDQLVPGQL VAMLQGIASG MNYLSDHNYV
HRDLAARNIL VSQNLCCKVS DFGLTRLLDN FDGTYETQGG KIPIRWTAPE AIAHRIFTTA
SDVWSFGIVM WEVLSFGDKP YGEMSNQEVM KSIEDGYRLP PPMDCPAPLY ELMKNCWAYD
RARRPPFHRL KAQLEHLQAN PHSLRTIANF DPRVTLRLPS LSGSDGIPYR SVAEWLESIR
MKRYALHFHS AGLDTMECVL DLTAEDLVQM GITLPGHQKR ILYSIQGFKD
//
