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Database: UniProt
Entry: A0A4W6C4J5_LATCA
LinkDB: A0A4W6C4J5_LATCA
Original site: A0A4W6C4J5_LATCA 
ID   A0A4W6C4J5_LATCA        Unreviewed;       909 AA.
AC   A0A4W6C4J5;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=epha4l {ECO:0000313|Ensembl:ENSLCAP00010008680.1};
OS   Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX   NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010008680.1, ECO:0000313|Proteomes:UP000314980};
RN   [1] {ECO:0000313|Proteomes:UP000314980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sai Rama Sridatta P.;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLCAP00010008680.1}
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       Early endosome {ECO:0000256|ARBA:ARBA00004412}. Endosome
CC       {ECO:0000256|ARBA:ARBA00004177}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A4W6C4J5; -.
DR   Ensembl; ENSLCAT00010008883.1; ENSLCAP00010008680.1; ENSLCAG00010003599.1.
DR   GeneTree; ENSGT00940000156948; -.
DR   Proteomes; UP000314980; Unassembled WGS sequence.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
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   GO; GO:0007155; P:cell adhesion; 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:SF18; EPHRIN TYPE-A RECEPTOR 4; 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; PF07647; SAM_2; 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; 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}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR000666-3};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000666-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000314980};
KW   Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          1..175
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          294..404
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          405..500
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          579..840
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          871..909
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          848..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        704
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT   BINDING         585..593
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   BINDING         611
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        39..157
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        74..84
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   909 AA;  101810 MW;  D16C7B254563D326 CRC64;
     CVCVQEYPCN IFNVVAFSQW EEVSIMDEKN IPIRTYQVCN VMEPNQNNWL RTDWIPRGGA
     QRVYIEIKFT LRDCNSLPGV MGTCKETFNL YYYESNNDKE RYIRENQFGK IDTIAADESF
     TQVDIGDRIM KLNTEVRDVG ALTRKGFYLA FQDVGACIAL VSVRVFYKKC PLAVRNLAQF
     PDTITGADTS SLVEVRGSCV DNSEEKEVPK MYCGADGEWL VPIGNCLCNP GYEERNAECQ
     ACKIGYYRAL ATDGSCSKCP LHSYSVREGS TSCVCDKGYF RSETDPASMP CTRPPSAPVH
     LISNVNETSV NLEWSPPRSS GGRQDLTYNV VCKRCGPDGR RCQPCGNGIH FSPQQLSLKG
     TRVSINELQA HTNYTFEVWA VNGVSPQSPG PEQAVSVTVT TNQAAPSPVT SIQAKDITRH
     TISLAWQPPD RANGVILEYE VKYYEKDQNE RSYRIIKTSS RNTDIKGLTP LTSYVFHVRA
     RTAAGYGDFS GPFEFMTNSG EFSHAALTLL ALMTSVHLKA RERLTASPVT RSKYSKAKQD
     SDEEKHLHQG VRIYVDPFTY EDPNQAVREF AKEIDASCIK IEKVIGIGEF GEVCSGRLKM
     PGKREICVAI KTLKAGYTDK QRRDFLSEAS IMGQFDHPNI IHLEGVVTKC KPVMIITEYM
     ENGSLDAFLR KNDGRFTVIQ LVGILRGIAS GMKYLSDMSY VHRDLAARNI LVNSNLVCKV
     SDFGMSRVLE DDPEAAYTTR GGKIPIRWTA PEAIAYRKFT SASDVWSYGI VMWEVMSYGE
     RPYWDMSNQD VIKAIDEGYR LPPPMDCPVA LHQLMLDCWQ RERADRPKFG QIVNMLDKLI
     RNPNTLKRTG GETAVRPNTT LLEPGSPEAS SAVGTVEDWL QAIGMERYSD NFTAAGYTTP
     EAVVHMTQE
//
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