ID F7CSX5_CALJA Unreviewed; 512 AA.
AC F7CSX5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN Name=LCK {ECO:0000313|Ensembl:ENSCJAP00000001647.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000001647.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000001647.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000001647.3}
RP IDENTIFICATION.
RG Ensembl;
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=2.7.10.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001149,
CC ECO:0000256|RuleBase:RU362096};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004342}. Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Membrane
CC {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004423}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|RuleBase:RU362096}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; F7CSX5; -.
DR Ensembl; ENSCJAT00000001750.4; ENSCJAP00000001647.3; ENSCJAG00000000957.4.
DR GeneTree; ENSGT00940000161163; -.
DR Proteomes; UP000008225; Chromosome 7.
DR Bgee; ENSCJAG00000000957; Expressed in kidney and 3 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd10362; SH2_Src_Lck; 1.
DR CDD; cd12005; SH3_Lck; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR035850; Lck_SH2.
DR InterPro; IPR035749; Lck_SH3.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
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; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF39; TYROSINE-PROTEIN KINASE LCK; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362096};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023139};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362096}; Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|RuleBase:RU362096}.
FT DOMAIN 115..175
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 181..265
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 234..501
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 512 AA; 58015 MW; 578A9FECF467E215 CRC64;
MGCGCSSHPE DDWMENIDVC ENCHYPIVPL DGKATLLFRN GSEVRDPLVT YEGSNPPASP
LQGDPRQQGL KNSLAVGFHL LPTYSLPCPA FLVACPITPG FLPISGRFSL MPLVFTDNLV
IALHSYKPSH DGDLGFEKGE QLRILEQNGE WWKAQSLTTG QEGFVPFNFV AKANSLEPEP
WFFKNLSRKD AERQLLAPGN THGSFLIRES ESTAGSFSLS VRDFDQNQGE VVKHYKIRNL
DNGGFYISPR ITFPGLHELV RHYTRYYNEH TKVAVKSLKQ GSMSPDAFLA EANLMKQLQH
QRLVRLYAVV TQEPIYIITE YMENGSLVDF LKTPSGIKLT INKLLDMAAQ IAEGMAFIEE
RNYIHRDLRA ANILVSDTLS CKIADFGLAR LIEDNEYTAR EGAKFPIKWT APEAINYGTF
TIKSDVWSFG ILLTEIVTHG RIPYPGMTNP EVIQNLERGY RMVRPDNCPE ELYHLMMLCW
KERPEDRPTF DYLRSVLEDF FTATEGQYQP QP
//
