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Database: UniProt
Entry: A0A673T791_SURSU
LinkDB: A0A673T791_SURSU
Original site: A0A673T791_SURSU 
ID   A0A673T791_SURSU        Unreviewed;       955 AA.
AC   A0A673T791;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS   Suricata suricatta (Meerkat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Herpestidae; Suricata.
OX   NCBI_TaxID=37032 {ECO:0000313|Ensembl:ENSSSUP00005004831.1, ECO:0000313|Proteomes:UP000472268};
RN   [1] {ECO:0000313|Ensembl:ENSSSUP00005004831.1, ECO:0000313|Proteomes:UP000472268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dudchenko O., Lieberman Aiden E., Tung J., Barreiro L.B.,
RA   Clutton-Brock T.H.;
RT   "A Chromosome-scale Meerkat (S. suricatta) Genome Assembly.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSUP00005004831.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001171};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; A0A673T791; -.
DR   Ensembl; ENSSSUT00005005594.1; ENSSSUP00005004831.1; ENSSSUG00005003149.1.
DR   Proteomes; UP000472268; Chromosome 1.
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   CDD; cd09546; SAM_EPH-A5; 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:SF13; EPHRIN TYPE-A RECEPTOR 5; 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};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472268};
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        512..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..177
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51550"
FT   DOMAIN          296..406
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          407..501
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          593..854
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          883..947
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   ACT_SITE        718
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT   BINDING         599..607
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT   BINDING         625
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        41..159
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
FT   DISULFID        76..86
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000666-3"
SQ   SEQUENCE   955 AA;  106408 MW;  25ADF0EB6724B1F4 CRC64;
     NLLDSRTVMG DLGWIAFPKN GWEEIGEVDE NYAPIHTYQV CKVMEQNQNN WLLTSWISNE
     GASRIFIELK FTLRDCNSLP GGLGTCKETF NMYYFESDDE NGRNIKENQY IKIDTIAADE
     SFTELDLGDR VMKLNTEVRD VGPLSKKGFY LAFQDVGACI ALVSVRVYYK KCPSVVRHLA
     VFPDTITGAD SSQLLEVSGS CVNHSVTDEP PKMHCSAEGE WLVPIGKCMC KAGYEEKNGT
     CQVCRPGFFK ASPHSQSCSK CPPHSYTHEE ASTSCVCEKD YFRRESDPPT MACTRPPSAP
     RNAISNVNET SVFLEWIPPA DTGGRKDVSY YIACKKCNSH AGVCDQCGGH VRYLPRQIGL
     KNTSVMMVDL LAHTNYTFEI EAVNGVSDLS PGARQYVSVN VTTNQAAPSP VTNVKKGKIA
     KNSISLSWQE PDRPNGIILE YEIKYFEKDQ ETSYTIIKSK ETTVTAEGLK PASVYVFQIR
     ARTAAGYGVF SRRFEFETIP VSVAASSDQS QIPIIAVSVT VGVILLAVVI GFLLSGRRCG
     YSKAKQDPEE EKMHFHNGHI KLPGVRTYID PHTYEDPNQA VHEFAKEIEA SCITIERVIG
     AGEFGEVCSG RLKLPGKREL PVAIKTLKVG YTEKQRRDFL GEASIMGQFD HPNIIHLEGV
     VTKSKPVMIV TEYMENGSLD TFLKKNDGQF TVIQLVGMLR GISAGMKYLS DMGYVHRDLA
     ARNILINSNL VCKVSDFGLS RVLEDDAEAA YTTRGGKIPI RWTAPEAIAF RKFTSASDVW
     SYGIVMWEVV SYGERPYWEM TNQDVIKAVE EGYRLPSPMD CPAALYQLML DCWQKDRNSR
     PKFDEIVNML DKLIRNPSSL KTLVNASSRV SNLLAEHGPL GSGAYRSVGE WLEAIKMGRY
     TEIFMENGYS SMDAVAQVTL EDLRRLGVTL VGHQKKIMNS LQEMKVQLVN GMVPL
//
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