ID G3HE12_CRIGR Unreviewed; 931 AA.
AC G3HE12;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Ephrin type-A receptor 10 {ECO:0000313|EMBL:EGW00541.1};
GN ORFNames=I79_008781 {ECO:0000313|EMBL:EGW00541.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW00541.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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DR EMBL; JH000307; EGW00541.1; -; Genomic_DNA.
DR AlphaFoldDB; G3HE12; -.
DR STRING; 10029.G3HE12; -.
DR PaxDb; 10029-XP_007616794-1; -.
DR eggNOG; KOG0196; Eukaryota.
DR InParanoid; G3HE12; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
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; 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; 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; 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};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:EGW00541.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
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..931
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003444054"
FT DOMAIN 35..216
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 379..477
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 567..823
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 856..920
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT BINDING 573..582
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 931 AA; 101471 MW; D7053FE864A0491C CRC64;
METGAGPHPL RRFVCLMPLC LALLLGPGRP GTAEEVILLD SKASQAELGW TALPSNGWEE
ISGVDEHDRP IRTYQVCNVL EPNQDNWLQT GWISRGRGQR IFVELQFTLR DCSSIPGAAG
TCKETFNAYY LETEADLGRG RPRLGGNRPR KIDTIAADES FTQGDLGERK MKLNTEVREI
GPLSRQGFHL AFQDVGACVA LVSVRVYYKQ CRATVRGLAA FPATAAESAF STLVEVTGTC
VSHSEGEPGS PPRMHCGADG EWLVPVGRCS CSAGFQERGD ICEACPPGFF KVSPRRPLCS
PCPEHSLALE NASTFCVCQD TYARSPHSPG QQSPLPPTGH AHIYNEPKCM SRPSCLHPDL
VGSGSWRSVL LFLLSAPWEE DEIRRDRVEP QSVSLSWREP VPAGTPGANG TEYEIRYYEK
GQSEQTYSTV KTGAPAVTVT NLKPATRYVF QIRAASPGPS WESQSFNPSI EVQTPGEVAS
GSRDQSPAVV VTVVTISALL VLGSVMSVLA IWRRPCNGKG SGDAHDEEEL YFHFKVPTRR
TFLDPQSCGD PLQAVHLFAK ELDAKSVTLE KSLGAGSRFG DLCCGCLQLP GRQELPVAVH
TLRDGCSDSQ RLSFLAEALT LGQFDHSHIV RLEGVVTRGK PLMIVTEYMN LGALDDFLRH
HEGELMATQL MALLPGLASA MKYLSEIGYV HRGLAARRVL VSSGLICKIS GFGRGPRDRA
EAVYTTMSGR SPALWAAPET IQFGHFSSAS DVWSFGIVMW EVMAFGERPY WDMSGQDVIK
AVEDGFRLPP PRNCPSPLHR LMLDCWQKDP GERPRFSQIH SILSKMGQEP EPSKCAANTC
LRPPTPLADR AFSTFPSFGS VGAWLEALDL CRYKDNFSAA GYGSLEAVAE MTAQDLGSLG
ISSAEHREAL LSGISALQTR VLQLQGQGVQ V
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