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Database: UniProt
Entry: A0A2Y9SKB7_PHYMC
LinkDB: A0A2Y9SKB7_PHYMC
Original site: A0A2Y9SKB7_PHYMC 
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}.
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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
//
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