ID G1K381_MOUSE Unreviewed; 1130 AA.
AC G1K381;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=Epha6 {ECO:0000313|Ensembl:ENSMUSP00000066734.7,
GN ECO:0000313|MGI:MGI:108034};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000066734.7, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000066734.7, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000066734.7,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000066734.7}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000066734.7};
RG Ensembl;
RL Submitted (NOV-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 RefSeq; NP_031964.2; NM_007938.2.
DR AlphaFoldDB; G1K381; -.
DR SMR; G1K381; -.
DR MaxQB; G1K381; -.
DR PeptideAtlas; G1K381; -.
DR ProteomicsDB; 353020; -.
DR Antibodypedia; 32095; 437 antibodies from 35 providers.
DR DNASU; 13840; -.
DR Ensembl; ENSMUST00000068860.13; ENSMUSP00000066734.7; ENSMUSG00000055540.16.
DR GeneID; 13840; -.
DR KEGG; mmu:13840; -.
DR UCSC; uc007zpo.1; mouse.
DR AGR; MGI:108034; -.
DR CTD; 285220; -.
DR MGI; MGI:108034; Epha6.
DR VEuPathDB; HostDB:ENSMUSG00000055540; -.
DR GeneTree; ENSGT00940000154490; -.
DR HOGENOM; CLU_000288_141_2_1; -.
DR OMA; YKNNFVA; -.
DR OrthoDB; 1614410at2759; -.
DR PhylomeDB; G1K381; -.
DR TreeFam; TF315363; -.
DR BioGRID-ORCS; 13840; 4 hits in 80 CRISPR screens.
DR ChiTaRS; Epha6; mouse.
DR Proteomes; UP000000589; Chromosome 16.
DR Bgee; ENSMUSG00000055540; Expressed in dentate gyrus of hippocampal formation granule cell and 67 other cell types or tissues.
DR Genevisible; G1K381; MM.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR CDD; cd10484; EphR_LBD_A6; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05066; PTKc_EphR_A; 1.
DR CDD; cd09547; SAM_EPH-A6; 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; IPR042746; EPH-A6_SAM.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034280; EphA6_rcpt_lig-bd.
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; IPR001426; Tyr_kinase_rcpt_V_CS.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF10; EPHRIN TYPE-A RECEPTOR 6; 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; 2.
DR Pfam; PF00536; SAM_1; 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 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|MaxQB:G1K381,
KW ECO:0007829|ProteomicsDB:G1K381}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 642..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 128..306
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 425..535
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 536..631
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 725..1038
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1059..1119
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 757
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1130 AA; 126511 MW; DBA5B55C59EE9262 CRC64;
MQFPSPPAAR SSPAAQAASS PQAAAPAPGQ PGPSCPAHRA SRGGRPGTSP ADRVEEEEEE
EEEEESLVQD PHATRNTWLR CCHFFLRRRR EPTRAMGGCE VREFLLQFGF FLPLLTAWTG
DCSHVSNQVV LLDTTTVMGE LGWKTYPLNG WDAITEMDEH NRPIHTYQVC NVMEPNQNNW
LRTNWISRDA AQKIYVEMKF TLRDCNSIPW VLGTCKETFN LYYIESDESH GTKFKPSQYI
KIDTIAADES FTQMDLGDRI LKLNTEIREV GPIERKGFYL AFQDIGACIA LVSVRVFYKK
CPFTVRNLAM FPDTIPRVDS SSLVEVRGSC VKSAEERDTP KLYCGADGDW LVPLGRCICS
TGYEEIEGSC HACRPGFYKA FAGNTKCSKC PPHSSTYVEA TSVCHCEKGY FRAEKDPPSM
ACTRPPSAPR NVAFNINETA LILEWSPPSD TGGRKDLTYS VICKKCGLDT TQCEDCGGGL
RFIPRHTGLI NNSVVVLDFV SHVNYTFEIE AMNGVSELSI SPKPFTAITV TTDHDAPSLI
GMMRKDWASQ NSLALSWQAP AFSNGAILDY EIKYYEKEHE QLTYSSTRSK APSVIVTGLK
PATTYIFHIR VRTATGYSGY SQKFEFETGD ETSDMAAEQG QILVIATAAV GGFTLLVILT
LFFLITGRCQ WYIKAKMKSE EKRRTHLQNG HLRFPGIKTY IDPDTYEDPS LAVHEFAKEI
DPSRIRIERV IGAGEFGEVC SGRLKTPGKR EIPVAIKTLK GGHMDRQRRD FLREASIMGQ
FDHPNIIRLE GVVTKRSFPA IGVEAFCPSF LRAGFLNGIQ APHPVTAGGS LPPRIPAGRP
VMIVVEYMEN GSLDSFLRKH DGHFTVIQLV GMLRGIASGM KYLSDMGYVH RDLAARNILV
NSNLVCKVSD FGLSRVLEDD PEAAYTTTGG KIPIRWTAPE AIAYRKFSSA SDAWSYGIVM
WEVMSYGERP YWEMSNQDVI LSIEEGYRLP APMGCPPSLH QLMLHCWQKE RNHRPKFTDI
VSFLDKLIRN PSALHTLVED ILVMPESPGD VPEYPLFVTV GDWLDSIKMG QYKSNFMAAG
FTTFDLISRM SIDDIRRIGV ILIGHQRRIV SSIQTLRLHM MHIQEKGFHV
//
