ID A0A2Y9SKB7_PHYMC Unreviewed; 1169 AA.
AC A0A2Y9SKB7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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|RefSeq:XP_023976189.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023976189.1};
RN [1] {ECO:0000313|RefSeq:XP_023976189.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023976189.1};
RG RefSeq;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_023976189.1; XM_024120421.1.
DR AlphaFoldDB; A0A2Y9SKB7; -.
DR KEGG; pcad:102981681; -.
DR InParanoid; A0A2Y9SKB7; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000248484; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 4: Predicted;
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 Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_023976189.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
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 657..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 126..304
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 423..533
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 534..646
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 740..1053
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1098..1158
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 BINDING 772
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1169 AA; 130628 MW; D2A1809A4008063F CRC64;
MQFRSPTAAR SSLAPQAASS SEAAAPAPGQ PGPSCPAPGA SHGGRPGTPP VGRVEEEEEE
EEDVDRDPSP TLNTWLRCCH FSLRGRREPG RAMGGSEVRE FLLQFGFFLP LLTAWPGDCS
HVSSNQVVLL DTTTVLGELG WKTYPLNGWD AITEMDEHNR PIHTYQVCNV MEPNQNNWLR
TNWISRDAAQ KIYVEMKFTL RDCNSIPWVL GTCKETFNLY YVESDESHGI KFKPSQYTKI
DTIAADESFT QMDLGDRILK LNTEIREVGP VERKGFYLAF QDIGACIALV SVRVFYKKCP
FTVRNLAMFP DTIPRVDSSS LVEVRGSCVK SAEERDTPKL YCGADGDWLV PLGRCICSTG
YEEIEGSCHA CRPGFYKAFA GNTKCSKCPP HSLTYMEATS VCQCEKGYFR AEQDPPSMAC
TRPPSAPRNV VFNINETALI LEWSPPSDTG GRKDLTYSVI CKKCGLDTSQ CEDCGGGLRF
IPRHTGLINN SVIVLDFVPH VNYTFEIEAM NGVSELSFSP KPFTAITVTT NQDAPSLIGM
VRKDWASQNS IAISWQAPAF SNGPILDYEI KYYEKVYPRI APAFWHYLRV EQHEQQLSYS
STRSKAPSAI ITGLKPATKY IFHIRVRTAT GYSGYSQKFE FETGDETSDM AAEQGQILVI
ATAAVGGFTL LVILTLFFLI TGRCQWYVKA KMKSEEKRRK DLQNGHLHFP GIKTYIDPDT
YEDPSLAVHE FAKEIDPSRI RIERVIGAGE FGEVCSGRLK TPGKREILVA IKTLKGGHMD
RQRRDFLREA SIMGQFDHPN IIRLEGVVTK RSFPAIGVET FCPSFLRAGF LNSLQAPHPV
PGGGSLPPRI PAGRPVMIVV EYMENGSLDS FLRKHDGHFT VIQLVGMLRG IASGMKYLSD
MGYVHRDLAA RNILVNSNLV CKVSDFGLSR VLEDDPEAAY TTTGGKIPIR WTAPEAIAYR
KFSSASDAWS YGIVMWEVMS YGERPYWEMS NQDVILSIEE GYRLPAPMGC PASLHQLMLH
CWQKERNHRP KFTDIVSFLD KLIRNPSTLH TLVEDILVVN GLHSQCPSTE LSDCSMAVDA
GRMPDSPGEV PEYPLFVTVG DWLDSIKMGQ YKNNFMAAGF TTFDLISRMN IDDIRRIGVI
LIGHQRRIVS SIQTLRLHMM HIQEKGFHV
//