ID F1N6H6_BOVIN Unreviewed; 1008 AA.
AC F1N6H6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=EPH receptor A10 {ECO:0000313|Ensembl:ENSBTAP00000033182.5};
GN Name=EPHA10 {ECO:0000313|Ensembl:ENSBTAP00000033182.5,
GN ECO:0000313|VGNC:VGNC:28533};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000033182.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000033182.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000033182.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000033182.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000033182.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; F1N6H6; -.
DR SMR; F1N6H6; -.
DR STRING; 9913.ENSBTAP00000033182; -.
DR PaxDb; 9913-ENSBTAP00000033182; -.
DR Ensembl; ENSBTAT00000033263.5; ENSBTAP00000033182.5; ENSBTAG00000020510.6.
DR VEuPathDB; HostDB:ENSBTAG00000020510; -.
DR VGNC; VGNC:28533; EPHA10.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000160752; -.
DR HOGENOM; CLU_000288_141_4_1; -.
DR InParanoid; F1N6H6; -.
DR OMA; FGCLQLP; -.
DR TreeFam; TF315608; -.
DR Reactome; R-BTA-2682334; EPH-Ephrin signaling.
DR Reactome; R-BTA-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-BTA-3928665; EPH-ephrin mediated repulsion of cells.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000020510; Expressed in oocyte and 39 other cell types or tissues.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/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:SF16; EPHRIN TYPE-A RECEPTOR 10; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 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 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; PS50011; PROTEIN_KINASE_DOM; 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 Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 35..216
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 340..452
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 456..554
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 645..900
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 933..997
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 322..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 651..659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT DISULFID 77..198
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 112..122
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 1008 AA; 109347 MW; B61314DF8B28A643 CRC64;
METGAGPHPL RLFICLMPLC LALLLGPGRP GTAEEVILLD SKASQAELGW TALPSNGWEE
ISGVDEHDRP IRTYQVCNVL EPNQDNWLQT GWIGRGRGQR IFVELQFTLR DCSSIPGAAG
TCKETFNVYY LETEADLGRG RTRPGGSRPR KIDTIAADES FTQGDLGERK MKLNTEVREI
GPLSRQGFHL AFQDVGACVA LVSVRVYYKQ CRATVRGLAA FPATAAESAF STLVEVTGTC
VAHSEGEPGS PPRMHCGADG EWLVPVGRCS CSAGFQERGD ICEACPPGFY KVSPRRPLCS
PCPEHSRALE NASTFCVCQD SYARSPTDPP SASCTRPPSA PRDLQYSLSR SPLALRLRWL
PPADSGGRSD VTYSLLCLRC GREGPAGACE PCGPRVAFVP RQVGLRERAA TLLHLRPGAR
YTVRVAALNG VSGPAAAAGA TYAQVTVSTG PGAPWEEDEI RRDRVEPQSV SLSWREPIPA
GAPGANGTEY EIRYFEKGQS EQTYSTVKTG APAVTVTNLK PATRYVFQIR AASPGPSWET
QSFNPSIEVL TPGEATSRSK DQSPAVVVTV VTISALLVLG SVMSVLAIWR RPCSYGKGGR
DAHDEEELYF HFKVPTRRTF VDPQSCGDPL QAVHLFAKEL DAKSVTLEKS LGTGRFGELC
CGCLQLPGRQ ELPVAVHTLR EGCSDSQRLS FLAEALTLGQ FDHSHVVRLE GVVTRGSTLM
IVIEYMSHGA LDGFLRRHEG QLVAAQLMGL LPGLASAMKY LSEMGYVHRG LAARRVLVSS
ELVCKISGFG RGPRDRAEAV YTTMSGRSPA LWAAPETLQF GHFSSASDVW SFGVVMWEVM
AFGERPYWDM SGQDVIKAVE DGFRLPPPRN CPSPLHRLML DCWQKDPGER PRFSQIHGLL
SKMMQDPEPP RCADTTCARP PTPLEDRAFS TFPSFGSVGA WLEALDLGRY KDSFAAAGYG
SLEAVAAMTA QDLVSLGISS AEHREDLLSG ISALRARVLQ LQGRGVQV
//
