ID A0A2U9AXV5_SCOMX Unreviewed; 994 AA.
AC A0A2U9AXV5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=SMAX5B_012156 {ECO:0000313|EMBL:AWO96448.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWO96448.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWO96448.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; CP026243; AWO96448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9AXV5; -.
DR STRING; 52904.ENSSMAP00000019893; -.
DR Proteomes; UP000246464; Chromosome 1.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 2.
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; 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; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; 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:SF15; EPHRIN TYPE-B 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; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 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 Kinase {ECO:0000313|EMBL:AWO96448.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:AWO96448.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transferase {ECO:0000256|ARBA:ARBA00023137, ECO:0000313|EMBL:AWO96448.1};
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,
KW ECO:0000313|EMBL:AWO96448.1}.
FT TRANSMEM 546..570
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..198
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 324..437
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 438..533
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 621..890
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 912..976
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 746
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT DISULFID 41..180
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 78..88
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 994 AA; 110502 MW; BDB825CEB6E1F269 CRC64;
MLLDTTESTS ELGWTTYPDT GWDEVSVLDD RGKLIRTFEV CNVNQNPRLQ DNWLATPFLY
RHSAPRVFVT LRFSVRDCGS LRSPSPTCRE TLTLYYKQAD SQRELEKTWV AEPSSKEKDS
REGWVKVDTI AADKSFSKVE PSSPHQYQPN RYSRINVKTR SFAPLTRNGF VLAIVDSGAC
VSLMGVSIFY RRCPATSLFL ASYPATPSGA EPTALVPVSG TCVPHSKAQA GAAPRMHCNA
EGEWMVPVGG CVCDGGYEPN LNGSACLACP VGYFKSVPGS APCSVCPANS RTSQRGSSVC
ECRSGFYRAA NDANSSACTT PPSAPVSLSW EYESDDGGVS IRWRPPVDMG GRSEVWYGLV
CRICPSPTFT NPASCSWCGE GVTFSPTQTN LKQTKVTLNN LLTRVTYLIQ VQAMNEVSAL
SPFSARYSSI NFTTSQSVPS TVPMMHQLSR APDSITLSWP QPDRPNGDIL EYQLRYFDKG
SDVDSAVSVY SETNTVTINS LIPGSIYGFQ IRARNERGYG PYSNTIYFTT LPLEEHSQQI
QNRLPLLVGS VMGGAAFLLV VAAIVVVVVF RSKRRESPYS DRLQRYISNR GGVKYYVDPS
TYEDPSEAVK EFAREIDPAH LKIEEVIGPA QFGEVSRGRY RPLGRREVLV AVKTLRWGAS
DRERGMFLSE AGVLGQFDHP NVLKLEGVVT HSPPERIITE FMENGPLDAF LRENEGQFSI
LQLVGMLRGV GAGMRYLSER NFVHRDLAAR NVLVNSNLVC KVSDFGLSRL MRGLDHNIPT
YTASLGSKIP VRWTAPEAFQ HRKFSSASDA WSFGILMWEV MSYGERPYWD MSNQEVMKAV
ADQYRLPAPH SCPPALHSLM LQCWQADRGD RPAFDSLLSS LDRLIRHPAT LKTEPTRSCS
QTLLSPTPTD LSAVATVSDW LKALRMERYQ DEFDRAHLDD LDRVSKLTMD DVQHLGVNLL
GHQRKIVTAA QQLRAHLTQG QVEHAYVHRA HFEP
//
