ID M3VYX2_FELCA Unreviewed; 992 AA.
AC M3VYX2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Tyrosine kinase non receptor 2 {ECO:0000313|Ensembl:ENSFCAP00000002450.6};
GN Name=TNK2 {ECO:0000313|Ensembl:ENSFCAP00000002450.6,
GN ECO:0000313|VGNC:VGNC:66420};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000002450.6, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000002450.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002450.6,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000002450.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002450.6,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000002450.6}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000002450.6};
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 EMBL; AANG04001815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3VYX2; -.
DR Ensembl; ENSFCAT00000002663.6; ENSFCAP00000002450.6; ENSFCAG00000002658.6.
DR VGNC; VGNC:66420; TNK2.
DR eggNOG; KOG0199; Eukaryota.
DR GeneTree; ENSGT00940000160853; -.
DR HOGENOM; CLU_000288_7_39_1; -.
DR Proteomes; UP000011712; Chromosome C2.
DR Bgee; ENSFCAG00000002658; Expressed in tip of external ear and 10 other cell types or tissues.
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-UniRule.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR CDD; cd05040; PTKc_Ack_like; 1.
DR CDD; cd09539; SAM_TNK-like; 1.
DR CDD; cd14328; UBA_TNK1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR015116; Cdc42-bd-like.
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; 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 PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 158..417
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 942..984
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 122..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..738
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..789
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 992 AA; 109639 MW; 872BB7BC8C150C2E CRC64;
MPAARRFPGL ELSFPLLARL RRRLYTRLGS SSMQPEEGTG WLLELLSEVQ LQQYFLRLRD
DLNVTRLSHF EYVKNEDLEK IGMGRPGQRR LWEAVKRRKA MCKRKSWMSK VFSGKRLEAE
FPPHHSQSTF RKTSPTPGGP AGEGPLQSLT CLIGEKDLHL FEKLGDGSFG VVRRGEWDAP
SGKTVSVAVK CLKPDVLSQP EAMDDFIREV NAMHSLDHRN LIRLYGVVLT PPMKMVTELA
PLGSLLDRLR KHQGHFLLGT LSRYAVQVAE GMGYLESKRF IHRDLAARNL LLATRDLVKI
GDFGLMRALP QNDDHYVMQE HRKVPFAWCA PESLKTRTFS HASDTWMFGV TLWEMFTYGQ
EPWIGLNGSQ ILHKIDKEGE RLPRPEDCPQ DIYNVMVQCW AHKPEDRPTF VALRDFLLEA
QPTDMRALQD FEEPDKLHIQ MNDVITVIEG RLYLGNPMDP PDLLSVELST SRPTQHLGRV
KREPPPRPPQ PAIFAQKPTY DPVSEDQDPL SSDFKRLGLR KPGLTRGLWL AKPSARVPGT
KAGRGGGSEV TLIDFGEEPV VPAPRPCAPS LAQLAMDACS LLDKTPPQSP TRALPRPLHP
TPVVDWDARP LPPPPAYDDV AQDEDDFEVC SINSTLVAAG VCAGPSQGET NYAFVPEQAQ
LLPPLEDNLF LPPQGGSKPP SSAQTAQIFQ ALQQECMRQL RVPAGSLVPS PGPAPAGEDK
PQVPPRVPIP PRPTRPRGEL SPAPSGEEEI GRWPGPASPP RVPPREPLSP QGSRTPSPLV
PPGSSPLPPR LSSSPGKTMP TTQSFASDPK YATPQVIQAP GPRAGPCILP IVRDGKKVSN
THYYLLPERP PYLERYQRFL REAQSPEEPA PLPVPLLLPP PSTPAPAAPT ATVRPMPQAA
PDPKANFSTN NSNPGVRPPA LRATARLPQR GCPGDGPEAG RPTDKIQMVE QLFGLGLRPR
SECHKVLEMC DWNLEQAGCH LLGSCGPAHH KR
//
