ID A0A093PE92_PYGAD Unreviewed; 1109 AA.
AC A0A093PE92;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE Flags: Fragment;
GN ORFNames=AS28_01928 {ECO:0000313|EMBL:KFW70557.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW70557.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW70557.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW70557.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KL225291; KFW70557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093PE92; -.
DR STRING; 9238.A0A093PE92; -.
DR Proteomes; UP000054081; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05088; PTKc_Tie2; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR018941; Tyr_kin_Tie2_Ig-like_dom-1_N.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24416:SF125; ANGIOPOIETIN-1 RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF10430; Ig_Tie2_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFW70557.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054081};
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 730..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..235
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 331..421
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 428..522
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 526..620
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 625..718
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 809..1081
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 840
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 225..234
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW70557.1"
FT NON_TER 1109
FT /evidence="ECO:0000313|EMBL:KFW70557.1"
SQ SEQUENCE 1109 AA; 124241 MW; B834127AC27C30E9 CRC64;
GKVEAALDLI LINSFPLVGN SETSLICITS KWRSRESITI DRDQEDVTNQ HREPLEVNED
SKRATAKTVV WKREQASETI GAYYCEGKLK DEVTRIHTMK MPLGASFHPV ALTVTANKGE
HVNISFIRMA AKEEDAVIYK NGSFIHSVPR HEVPGELEVS YPQVQPQDAG VYSARYIGGN
LFTSAYTRLI VRRCEAQKWG PSCSSHCPSC TNNGICHEDT GECICPPGFM GKTCEKACGA
NTFGKTCEES CKENYGCRNY MFCLPDPYGC SCATGWMGLE CDKECKPGFY GSDCKLKCNC
HNRGTCDRFK GCVCSLGWHG LQCEKEADLS PQIENLLDPV ELNSGVEFKP FCIATGMPLP
KSEEFKLLKQ DGTVLRPALI VTSNRSEAMF TINRIQPRDT GTWVCSVQTV AGMAEKPFQV
TVKVPPVPQY APRLTDSGHN FLIIDINAEL HLGDGPVVST KLLYKPAKRY QSWMSVEVKG
TTKRLDNLEP KTEYQFCVQL SRQGEGGEGH PGPQASFTTA ALGLPPPEGL TLFPKSMTSL
NLSWHPLTLR TEDDIRVEVE RKSVNDNGDE SSVITQVPGN MSTLIIKDLE PRQQYMCRVR
VNTRSQGEWS NYLYAWTFSD RIPPAPYNIR FSNTTDTSSV ISWTTAEGHS ISSIIISYKI
YGKAEYNHID IIIKNTSITQ YHLKGLEPNT VYQVQINAQN NIGLSNPNTS FELKTLPETK
APYESKGGKM LLIAILGSAG MTCVTILLAF LIMLQLKRAN FQRRMAQAFQ NVVREEPAVQ
FNSGTLTLSR KAKNSPDPTI YPVLEWNDIK FQDVIGEGNF GQVLKARIKK DGLRMDAAIK
RMKEYASKDD HRDFAGELEV LCKLGHHPNI INLLGACEHR GYLYLAIEYA PHGNLLDFLR
KSRVLETDPA FAIANSTAST LSSQQLLHFA ADVARGMDYL SQKQFIHRDL AARNILVGEN
YVAKIADFGL SRGQEVYVKK TMGRLPVRWM AIESLNYSVY TTNSDVWSYG VLLWEIVSLG
GTPYCGMTCA ELYEKLPQGY RLEKPLNCDD EVYDLMRQCW REKPYERPSF AQILVSLNRM
LEERKTYVNT TLYEKFTYAG IDCSAEEAA
//
