ID A0A1U8DFQ1_ALLSI Unreviewed; 1126 AA.
AC A0A1U8DFQ1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=TEK {ECO:0000313|RefSeq:XP_014376539.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014376539.1};
RN [1] {ECO:0000313|RefSeq:XP_014376539.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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}.
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 RefSeq; XP_014376539.1; XM_014521053.2.
DR AlphaFoldDB; A0A1U8DFQ1; -.
DR STRING; 38654.A0A1U8DFQ1; -.
DR GeneID; 102376701; -.
DR KEGG; asn:102376701; -.
DR CTD; 7010; -.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; A0A1U8DFQ1; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.
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; IPR013098; Ig_I-set.
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; PF07679; I-set; 1.
DR Pfam; PF10430; Ig_Tie2_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 5.
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 Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_014376539.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW 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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1126
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010530594"
FT TRANSMEM 747..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..252
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 350..442
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 447..541
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 545..637
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 642..735
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 826..1098
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 966
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 857
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 971
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 984
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT DISULFID 242..251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1126 AA; 125668 MW; F7D262D36FBDF3E8 CRC64;
MDPLAHLLLY GFSLMISGKV EAALDLMLIN SFPLVGNTET SLICIAAKWR PCESVTIGRD
YEALMSQHQN PLEVTEDEKR GTAKKVVWKR EQAGETIGAY YCEGKVKDEV TRIRTMKMSQ
RASFLPVALT VTANKGESVN ISFIRKVSKE EDAVIYKNGS FIHAVPRHEV PGELEVAYSP
VQLQDAGVYY ARYIGGNTFT SAYTRLIVRR CEAQKWGPTC SSICPACMNN GICHEDTGEC
ICPPGFMGKT CEKACEANTF GRTCKESCEE KSGCKYYMFC LPDPYGCSCA TGWRGLECDK
ECQPGFYGPD CKLRCNCRHQ GSCDRFKGCV CNSGWHGLQC EKEGPADVSP QIKSSPGNVE
LNSGMEFKPT CRATGEPRPV NEDFKLLKKD GTVLKPNSFL TVTQNCSEAT FHIYRVHPPD
SGMWVCTVQT VAGEEPFQVT VKVPPVPQYP PKMQDSGHNF LIIDINADPH TGDGPIVLTK
LLYKPAKGLQ PWKSVKVHGR TKKLDNLEPK TEYKFCVQLS RQGDSGEGHP GPEASFTTVA
LGLPPPEGLS LLPKSRTSLN LSWNPITQKP EDDISIEVEG RNVNDDSDHI VTKVQGNISS
VIIDKLKPRQ QYMCRVRVNT RSPGEWSDYL YAWTYSDTFP PAPNNIKTCN ITDTSVLISW
STAEGESISS IIISYKICGK AEYNHIDVTI RNTTITQYHL KGLEPNTVYE VELSAQNNVG
SSSPNNSVQL KTLPEAKAQH ESKGGKMLLI AILGSAGMTC LTILLAFLIM LQLKRANFQH
RMAQAFQNVV REEPAVQFNS GTLTLSRKAK NSPDPTIYPV LEWNDIKFQD VIGEGNFGQV
LKARIKKDGL RMDAAIKRMK EYASKDDHRD FAGELEVLCK LGHHPNIINL LGACEHRGYL
YLAIEYAPHG NLLDFLRKSR VLETDPAFAI ANSTASTLSS QQLLHFAADV ARGMDYLSQK
QFIHRDLAAR NILVGENYVA KIADFGLSRG QEVYVKKTMG RLPVRWMAIE SLNYSVYTTN
SDVWSYGVLL WEIVSLGGTP YCGMTCAELY EKLPQGYRLE KPLNCDDEVY DLMRQCWREK
PYERPSFAQI LVSLNRMLEE RKTYVNTTLY EKFTYAGIDC SAEEAA
//
