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Database: UniProt
Entry: A0A672GXN4_SALFA
LinkDB: A0A672GXN4_SALFA
Original site: A0A672GXN4_SALFA 
ID   A0A672GXN4_SALFA        Unreviewed;       987 AA.
AC   A0A672GXN4;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=epha3 {ECO:0000313|Ensembl:ENSSFAP00005016264.1};
OS   Salarias fasciatus (Jewelled blenny) (Blennius fasciatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Blenniimorphae; Blenniiformes; Blennioidei; Blenniidae;
OC   Salariinae; Salarias.
OX   NCBI_TaxID=181472 {ECO:0000313|Ensembl:ENSSFAP00005016264.1, ECO:0000313|Proteomes:UP000472267};
RN   [1] {ECO:0000313|Ensembl:ENSSFAP00005016264.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A672GXN4; -.
DR   Ensembl; ENSSFAT00005016909.1; ENSSFAP00005016264.1; ENSSFAG00005006423.1.
DR   Proteomes; UP000472267; Unplaced.
DR   GO; GO:0005886; C:plasma 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; 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:SF12; EPHRIN TYPE-A RECEPTOR 3; 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; 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|PIRSR:PIRSR000666-
KW   2}; Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000666-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472267};
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        546..568
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..203
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          321..439
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          440..535
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          625..886
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          915..979
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   ACT_SITE        750
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT   BINDING         631..639
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   BINDING         657
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        67..185
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        102..112
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   987 AA;  109932 MW;  8FFB504F22925B9F CRC64;
     VGKNKHIFTL VFVTLAALGY LRQLPVNLLD SKASQGELGW ISYPSHGWEE ISGVDEHYTP
     IRTFQVCNVM EYSQNNWLRT NWIPRQSAQK IYVELKFTLR DCNSIPLVLG TCKETFNLLY
     LETDDDQGSH FREHQFSKID TIAADESFTQ TDLGDRILKL NTEVREVGPL TKKGFYLAFQ
     DVGACVALVS VRVYFKKCPY TVRNLATFPD TVPMDSHSLV EVKGLCVNHS KEEEPPRMYC
     STEGEWLVPI GKCLCNPGYE ERSNTCQMCR AGFYKSALGN LECSKCPPHS FSHHEGSLHC
     GCEKNFFRAE GDPASMACTR PPSAPRNVIS SINETSVILD WSWPEDTGGR RDVTFTVLCK
     RCRGVTANGS NSGTQRCEPC RSNVRFLPRA AGLHNTTVTV GDLLAHTNYT FEIEALNGVS
     ALAPKMRQYA AVTITTNQAA PSPVTVIRKE KTSRNSVSLS WQEPERPNGI ILDYEIKYYE
     KEEQETSYTI LRARGCNVTL NGLKSNTAYL LQIRARTAAG YGASSPTFQF ETSPDSFSIS
     SESSQVVLIA ISAAVAIILL TVLLYVLIGR FCCRSKSKHP DEKRLHFGNG HLRLPGIRTY
     VDPHTYEDPS QAVHEFAKEL DASCIAIDKV VGAGEFGEVC SGRLKLPSKK EICVAIKTLK
     GGYTDKQRRD FLAEASIMGQ FDHPNIIRLE GVVTRSKPVM IVTEYMENGS LDSFLRKHDA
     QFTGIQLVGM LRGIASGMKY LSDMGYVHRD LAARNILVNS NLVCKVSDFG LSRVLEDDPE
     AAYTTRGGKI PIRWTAPEAI AYRKFTSASD AWSYGIVLWE VMSYGERPYW EMSNQDVIKA
     VDEGYRLPPP MDCPATLYQL MLDCWQKERN NRPKFEQIVS ILDKLIRNPG SLKITANTTS
     RPANLLLDRS SSEVPSMGTM GDWMDGMRTL PCKEAFSGVS YSSCDTLAKT STEDLKKVGV
     TIVGPQKKIV SSLKALDSHT KNGPVPV
//
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