ID A0A2U9CA58_SCOMX Unreviewed; 986 AA.
AC A0A2U9CA58;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=SMAX5B_018220 {ECO:0000313|EMBL:AWP12920.1};
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:AWP12920.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP12920.1, 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; CP026256; AWP12920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CA58; -.
DR STRING; 52904.ENSSMAP00000012416; -.
DR Proteomes; UP000246464; Chromosome 14.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 CDD; cd05066; PTKc_EphR_A; 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; 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; 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; IPR016257; Tyr_kinase_ephrin_rcpt.
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; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
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|PIRSR:PIRSR000666-
KW 2}; Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW Kinase {ECO:0000313|EMBL:AWP12920.1};
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:AWP12920.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transferase {ECO:0000256|ARBA:ARBA00023137, ECO:0000313|EMBL:AWP12920.1};
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:AWP12920.1}.
FT TRANSMEM 486..509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..150
FT /note="Eph LBD"
FT /evidence="ECO:0000259|PROSITE:PS51550"
FT DOMAIN 269..379
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 383..475
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 569..830
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 861..921
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT ACT_SITE 694
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 575..583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 14..132
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT DISULFID 49..59
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ SEQUENCE 986 AA; 111151 MW; E56CF8DFF5501292 CRC64;
MDEHNRPIHT FQVCNVMEPN QNNWLRSNWI SRQAAQKIYV ELRFTLRDCN SIPWVSGTCK
ETFNLFYHET DEAHGVKFKP VQYTKIDTIA ADESFTQMDL GDRILKLNTE VREVGPMTRK
GFYLAFQDIG ACIALVSVRV YYKKCPFTLR NLASFPDTVP RVDSSSLVEV RGACIDHAEE
RDTPKLFCGA DGDWLVPLGK CVCSVGYEEI DGSCVACHPG FYKAYAGNIK CSKCPPHSFS
YGEGAAFCRC EKGFFRAEKD PPTMACTRPP SPPRSILFNL NDTCLMLEWS PPSDTGGRRD
LTYNVQCKRC GPEPDRCQLC EEELRFLPRS LGLTNATVTV MDFSAHANYT FEIESLNGVS
DMSSFARQVA VITVITDQGG PTVFGALKKD WASPNSIALS WQQPEPTTLP ILDYEIKYYE
KEHEQLSYSS TRTKAPSVII SGLKPATWYV FSVRTRTAAG YSSYSPKYEY ETTGDSSDMA
SDQGQVLVIV TAAVGGFTLL VILTLFLLIT GRCQWYFKAK ITSEEKRRTS YQNGHVPVPG
VKTYVDPDTY EDPSQAVHEF TKEIDPSRIR IERVIGAGEF GEVCSGRLRT PGKKEIAVAI
KTLKGGYVER QRRDFLREAS IMGQFDHPNI IRLEGVVTKS RPVMIVVEYV ENGSLDSFLR
QHDGHFTVIQ LVGMLRGIAS GMKYLSDTGY VHRDLAARNI LVNSNLVCKV SDFGLSRVLE
DDPEAAYTTT GGKIPIRWTA PEAISYRKFS SASDAWSYGI VMWEVMSYGE RPYWEMSNQD
VILSIEEGYR LPAPMGCPVA LHQLMLHCWQ KERSHRPKFI DVVSFLDKLI RNPSSLLPLV
EDIQSLPESP GEEMDYPMFI SVSDWLDSIK MSQYNSNFMA AGYDTLDSVA RMSIEEVRRT
GVELIGHQRR IISSLQTLRL QLLHEQEKGF HEVIGPTSTA DCPVVSLTSS SNRLFFYYTP
LSQYTWSQHT RLLQPDRLYG LAQALT
//
