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Database: UniProt
Entry: A0A2D0SM30_ICTPU
LinkDB: A0A2D0SM30_ICTPU
Original site: A0A2D0SM30_ICTPU 
ID   A0A2D0SM30_ICTPU        Unreviewed;       987 AA.
AC   A0A2D0SM30;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN   Name=LOC108276527 {ECO:0000313|RefSeq:XP_017343762.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017343762.1};
RN   [1] {ECO:0000313|RefSeq:XP_017343762.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017343762.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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_017343762.1; XM_017488273.3.
DR   AlphaFoldDB; A0A2D0SM30; -.
DR   STRING; 7998.ENSIPUP00000037200; -.
DR   Ensembl; ENSIPUT00000038651; ENSIPUP00000037200; ENSIPUG00000024902.
DR   GeneID; 108276527; -.
DR   KEGG; ipu:108276527; -.
DR   OMA; VAWTWTW; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000221080; Chromosome 16.
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   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; 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:SF13; EPHRIN TYPE-A RECEPTOR 5; 1.
DR   Pfam; PF14575; EphA2_TM; 1.
DR   Pfam; PF01404; Ephrin_lbd; 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};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:XP_017343762.1}; Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..987
FT                   /note="receptor protein-tyrosine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012361569"
FT   TRANSMEM        546..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..210
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          329..439
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          440..534
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        74..192
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        109..119
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   987 AA;  110602 MW;  E11AD82E2D5FA161 CRC64;
     MVSLWSCVSI KITCLFFFGF AVFVTQGGPS NEVNLLDSRS IMGDLGWIAY PKNGWEEIGE
     VDENYAPIHT YQVCRVMEHN QNNWLQTSWI LNEGAQRVFV ELKFTLRDCN SLPGGLGTCK
     ETFNVYYFES NDDDDRNIRE SQYTKIDTIA ADESFTELDL GDRVMKLNTE VRDVGPLTKK
     GFYLAFQDLG ACIALVSVRV FYKKCPTVVK NLAVFPDIIT GSDSSQLLEV LGTCVNNSVA
     EELPRMHCSA EGEWLVPIGR CMCQAGHEEV NGSCQVCKPG FYRSALQTRT CSKCPPHSFS
     KTEGSTSCQC EHGYYRKDTD PTNMACTKPP SAPRSAISNV NETSVLLEWS APEETGGRKD
     VTYSVVCRKM SAESRQYEPC GSHVRYLPQR TGLRNTSVMV LDLLAHKNYT FEVEAVNGVS
     ELTKPLRQYV SLNVTTNQAA PSPITVVKRG KTAKNSIAVS WQEPDRPNGI ILEYEIKYFE
     KDQETSYTIV KSKETGFVVD GLKPSSAYIF QIRARTSAGY GGFSRRFEFE TSPYLSASRD
     QGRVPVIAVA VTLGIILLAL ITGFLLSGRR CGYSKAKQDP DEEKMHFHNG HIKFPGVRTY
     IDPHTYEDPN QAVHEFAKEI DVSCITIERV IGAGEFGEVC SGPLRLPGKR ELMVAIKTLK
     AGYTEKQRRD FLAEASIMGQ FDHPNIIHLE GVVTKSKPVM IITEYMENGS LDTFLKKNDG
     QFTVIQLVGM LRGIASGMRY LSDMGYVHRD LAARNILVNS NLVCKVSDFG LSRVLEDDPE
     AAYTTRGGKI PIRWTAPEAI SYRKFTSASD VWSYGIVMWE VMSYGERPYW EMSNQDVIKA
     VEESYRLPGP MDCPTALYHL MMDCWQKDRN SRPKFDEIVS LLDKLIRNPS SLKSLVNPSN
     RVSNLLVEHG SAELCAFSSV GEWLDAIKMG RYTELFMESG YTSLDVVTQM TLEDVRRVGV
     TLAGHQKKIL NSIQEMRVQM TNATIPV
//
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