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Database: UniProt
Entry: A0A3B3VPU9_9TELE
LinkDB: A0A3B3VPU9_9TELE
Original site: A0A3B3VPU9_9TELE 
ID   A0A3B3VPU9_9TELE        Unreviewed;      1186 AA.
AC   A0A3B3VPU9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Tyrosine kinase non receptor 2 {ECO:0000313|Ensembl:ENSPLAP00000026912.1};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000026912.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000026912.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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DR   AlphaFoldDB; A0A3B3VPU9; -.
DR   Ensembl; ENSPLAT00000019402.1; ENSPLAP00000026912.1; ENSPLAG00000015092.1.
DR   GeneTree; ENSGT00940000165248; -.
DR   Proteomes; UP000261500; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd05040; PTKc_Ack_like; 1.
DR   CDD; cd09539; SAM_TNK-like; 1.
DR   CDD; cd00174; SH3; 1.
DR   CDD; cd14274; UBA_ACK1; 1.
DR   CDD; cd14328; UBA_TNK1; 1.
DR   Gene3D; 4.10.680.10; Cdc42-like binding domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR030220; Ack1_UBA_dom.
DR   InterPro; IPR015116; Cdc42-bd-like.
DR   InterPro; IPR037085; Cdc42-bd-like_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR021619; Mig-6.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR049587; TNK-like_SAM.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR015940; UBA.
DR   PANTHER; PTHR14254; GENE 33 POLYPEPTIDE; 1.
DR   PANTHER; PTHR14254:SF6; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR   Pfam; PF09027; GTPase_binding; 1.
DR   Pfam; PF11555; Inhibitor_Mig-6; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR630220-
KW   2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR630220-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..58
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          142..439
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          442..502
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          1133..1178
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          562..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          820..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..582
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..884
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        306
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630220-1"
FT   BINDING         148..156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630220-2"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630220-2"
SQ   SEQUENCE   1186 AA;  132101 MW;  159F2C69FD881841 CRC64;
     MQCEEGTEWL LELLMEVQLQ QYFKRIRDDL NVTRLSHFDY VKNEDLEKIG MGRPGQRRLW
     EAVKRRKAKR KTWMSKVFSG KRIEGEFPQQ GQLASSFRKL SLTPPLCLGD GVLDTQLHGG
     SGSSPLDGQQ LALTCLIPEK DLTLFEKLGD GSFGVVKRGE WLTPGGNVVR RRFGSFSPFL
     GNEVKFSRQG GGGKKSAINL LILQVNVAVK CLKTDVLSQP DALEDFICEV NAMHSLDHQN
     LIRLYGVVLT HPMKMVTELA PLGSLLDRLR CVHPQGPVLI HTLCQYAVQV ASGMAYLEQR
     RFIHRDLAAR NILLSSANRV KIGDFGLMRA LPNNDEHYVM QEHRKVPFAW CAPESLKTRT
     FSHATDTWMF GVTLWEMFTH GQEPWLGLNG SQILHKIDKE GERLPKPEDC PQDIYNVMLQ
     CWAQKPGDRP TFVALREFLL ETMPTDMCAL QDFDELDKLH IKVNDVITII EGRAENYWWR
     GQNKRTLKVG QFPRNVVTSV AGLSAHDISR PLKNSFIHTG HGDTNPHRCW GFPDRIDDLY
     LGNPMDPPDV LEVDLSAARP TQLPGRTKKE PPPRPPQPAV LIKKPCYDPV TEDEDSTSAV
     LRRLSLRKTG SLKGLKLKPA AWVSANKQSS RTSSSAHTPS SDVSLIDFGE DFSPSPVVEN
     QNPVLAKLAL QVGNILDKTP PQSPSKWLPR PLHPTPVVDW DARPLPPPPA YDDVAQDEDD
     MEVSSITSSE QQLEHDQAAV HGVDGALSSG QMTESDGVVS KDPERPVLED NLFLPGKHNH
     AASPSFSQSA EIFQELQQEC MRKLNVPTGG VGQWTQISAS CPTQNTQEDQ QRLSTNEDKP
     QIPPRVPIPP RPIKRGDYTS ARWSRDLSVS PMLSDPTYGI SGTTLERPPQ IPPRDPLSQP
     NSRTPSPNCA VVGSLHQRIC SVSPSTHQAS HAYSSYLSTS PGKPMPTTHS FASDPKYAAP
     KVIQAQDRDN ANRGPCILPI VRDGQKVSNT HYYLLPERPP YLDRFERFFR EAENLPGGGS
     AEDRHTRHAN TATVRPMVVT AQTVQGLIQP GELKANFSCN NNFGMSAQRS GMKTSVSLPR
     VCSDGLTGPT VNSSCSRTED GGNSLDRVQM VQEAVHGVTI AECQAALQNN SWDVQKAVHY
     LKVEQLFCLG LRNRSECIKL LEMCDWNLEQ ASTQILEDYG SITRQR
//
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