ID A0A2K5Z7S8_MANLE Unreviewed; 897 AA.
AC A0A2K5Z7S8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=EPH receptor A10 {ECO:0000313|Ensembl:ENSMLEP00000023869.1};
GN Name=EPHA10 {ECO:0000313|Ensembl:ENSMLEP00000023869.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000023869.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000023869.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; A0A2K5Z7S8; -.
DR STRING; 9568.ENSMLEP00000023869; -.
DR Ensembl; ENSMLET00000047389.1; ENSMLEP00000023869.1; ENSMLEG00000036102.1.
DR GeneTree; ENSGT00940000160752; -.
DR OMA; FGCLQLP; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR CDD; cd10487; EphR_LBD_A10; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd09549; SAM_EPH-A10; 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; 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; 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; 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; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00454; SAM; 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; 1.
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:UP000233140};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..897
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014331096"
FT DOMAIN 35..216
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 339..437
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 528..783
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 816..880
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT BINDING 534..542
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 897 AA; 97918 MW; 6ADADB35AA7C1814 CRC64;
METGAGPHPL RLFLCRMPLC LVLLLGPWRP GTAEEVILLD SKASQAELGW TALPSNGWEE
ISGVDEHDRP IRTYQVCNVL EPNQDNWLQT GWISRGRGQR IFVELQFTLR DCSSIPGAAG
TCKETFNVYY LETEADLGRG RPRLGGSRPR KIDTIAADES FTQGDLGERK MKLNTEVREI
GPLSRRGFHL AFQDVGACVA LVSVRVYYKQ CRATVRGLAA FPATAAESAF STLVEVAGTC
VAHSEGEPGS PPRMHCGADG EWLVPVGRCS CSAGFQERGD ICEACPPGFY KVSPRRPLCS
PCPEHSRALE NASTFCVCQD SYARSPTDPP SASCTPPWEE DEIRRDRVEP QSVSLSWREP
IPAGAPGANG TEYEIRYYEK GQSEQTYSMV KTGAPTVTVT NLKPATRYVF QIRAASPGPS
WEAQSFNPSI EVQTPGEAAS GSRDQSPAVV VTVVTISALL VLGSVMSVLA IWRRPCSYGK
GGGDAHDEEE LYFHFKVPTR RTFLDPQSCG DPLQAVHLFA KELDAKSVTL ERRLGAGRFG
ELCCGCLQLP GRQELPVAVH TLRDSASDSQ RLGFLAEALT LGQFDHSHIV RLEGVVTRGS
TLMIVTEYMS HGALDGFLRR HEGQLVAGQL MGLLPGLASA MKYLSEMGYV HRGLAARRVL
ISSDLVCKIS GFGRGPRDRA EAVYTTMSGR SPALWAAPET LQFGHFSSAS DVWSFGIVMW
EVMAFGERPY WDMSGQDVIK AVEDGFRLPP PRNCPTPLHR LMLDCWQKDP GERPRFSQIH
SILSKMVQDP EPPNCAPTTC PRPPTPLADR AFSTFPSFGS VGAWLEALDL CRYKDSFAAA
GYGSLEAVAE MTAQDLVSLG ISSAEHREAL LSGISALQAR VLQLQGQGVQ VIIKTCL
//
