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Database: UniProt
Entry: G9KUI2_MUSPF
LinkDB: G9KUI2_MUSPF
Original site: G9KUI2_MUSPF 
ID   G9KUI2_MUSPF            Unreviewed;      1040 AA.
AC   G9KUI2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE            EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
DE   Flags: Fragment;
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|EMBL:AES08561.1};
RN   [1] {ECO:0000313|EMBL:AES08561.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lungs {ECO:0000313|EMBL:AES08561.1};
RX   PubMed=23236062; DOI=10.1128/JVI.02476-12;
RA   Leon A.J., Banner D., Xu L., Ran L., Peng Z., Yi K., Chen C., Xu F.,
RA   Huang J., Zhao Z., Lin Z., Huang S.H., Fang Y., Kelvin A.A., Ross T.M.,
RA   Farooqui A., Kelvin D.J.;
RT   "Sequencing, annotation, and characterization of the influenza ferret
RT   infectome.";
RL   J. Virol. 87:1957-1966(2013).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; JP019963; AES08561.1; -; mRNA.
DR   AlphaFoldDB; G9KUI2; -.
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-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-KW.
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; cd14274; UBA_ACK1; 1.
DR   CDD; cd14328; UBA_TNK1; 1.
DR   Gene3D; 4.10.680.10; Cdc42-like binding domain; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal 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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
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:0000313|EMBL:AES08561.1};
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   Receptor {ECO:0000313|EMBL:AES08561.1};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00023137};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   DOMAIN          126..385
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          388..448
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REGION          90..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          503..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..842
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          898..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..756
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        774..803
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..829
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630220-1"
FT   BINDING         132..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630220-2"
FT   BINDING         158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR630220-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AES08561.1"
FT   NON_TER         1040
FT                   /evidence="ECO:0000313|EMBL:AES08561.1"
SQ   SEQUENCE   1040 AA;  114707 MW;  5129669520AB41C6 CRC64;
     MQPEEGTGWL LELLSEVQLQ QYFLRLRDDL NVTRLSHFEY VKNEDLEKIG MGRPGQRRLW
     EAVKRRKAMC KRKSWMSKVF SGKRLEAEFP PHHSQSTFRK TSPTPGGPAG EGPLQSLTCL
     IGEKDLHLFE KLGDGSFGVV RRGEWDAPSG KTVSVAVKCL KPDVLSQPEA MDDFIREVNA
     MHSLDHRNLI RLYGVVLTPP MKMVTELAPL GSLLDRLRKH QGHFLLGTLS RYAVQVAEGM
     GYLESKRFIH RDLAARNLLL AARDLVKIGD FGLMRALPQN DDHYVMQEHR KVPFAWCAPE
     SLKTRTFSHA SDTWMFGVTL WEMFTYGQEP WIGLNGSQIL HKIDKEGERL PRPEDCPQDI
     YNVMVQCWAH KPEDRPTFVA LRDFLLEAQP TDMRALQDFE EPDKLHIQMN DVITVIEGRA
     ENYWWRGQNT RTLCVGPFPR NVVTSVAGLS AQDISQPLQN SFIHTGHGDS DPRHCWGFPD
     KIDELYLGNP MDPPDLLSVE LSTSRPTQHL GRVKKPTYDP VSEDQDPLSS DFKRLGLRKP
     ALTRGLWLAK PSARVPGTKA ARGSGGEVTL IDFGEEPVVP APRPCAPSLA QLAMDACSLL
     DKTPPQSPTR ALPRPLHPTP VVDWDARPLP PPPAYDDVAQ DEDDFEVCSI NSTLVGAGVC
     AGPSQGETNY AFVPEQAPLL PPLEDNLFLP PQAGVKPPSS AQTAQIFQAL QQECMRQLQV
     PAASLGPSPG PAPVGEDKPQ VPPRVPIPPR PTRPRGELSP APSGEEELGR WPGPASPPRV
     PPREPLSPQG SRTPSPLVPP GSSPLPARLS SSPGKTMPTT QSFASDPKYA TPQVIQAPGP
     RVGPCILPIV RDGKKVSSTH YYLLPERPPY LERYQRFLRE AQSPEEPAPL PVPLLLPPPS
     TPAPAAPTAT VRPMPQAAPD PKANFSTNNS NPGARPPALR ATARLPQRGC PGDGPEAGRP
     ADKIQMLQAM VHGVTTEECQ AALQSHSWSV QRAAQYLKVE QLFGLGLRPR SECHKVLEMC
     DWSLEQAGCR LLGSCGPAHH
//
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