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Database: UniProt
Entry: G3WDZ1_SARHA
LinkDB: G3WDZ1_SARHA
Original site: G3WDZ1_SARHA 
ID   G3WDZ1_SARHA            Unreviewed;       514 AA.
AC   G3WDZ1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   Name=LYN {ECO:0000313|Ensembl:ENSSHAP00000013646.1};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000013646.1, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000013646.1, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000013646.1}
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR   RefSeq; XP_012396769.1; XM_012541315.1.
DR   AlphaFoldDB; G3WDZ1; -.
DR   STRING; 9305.ENSSHAP00000013646; -.
DR   Ensembl; ENSSHAT00000013758.2; ENSSHAP00000013646.1; ENSSHAG00000011662.2.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000158011; -.
DR   HOGENOM; CLU_000288_7_2_1; -.
DR   InParanoid; G3WDZ1; -.
DR   OMA; TGNMGCI; -.
DR   OrthoDB; 1614410at2759; -.
DR   TreeFam; TF351634; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0141038; F:phosphatidylinositol 3-kinase activator activity; IEA:Ensembl.
DR   GO; GO:0140031; F:phosphorylation-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR   GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR   GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0038159; P:C-X-C chemokine receptor CXCR4 signaling pathway; IEA:Ensembl.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0097028; P:dendritic cell differentiation; IEA:Ensembl.
DR   GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR   GO; GO:0030222; P:eosinophil differentiation; IEA:Ensembl.
DR   GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0002774; P:Fc receptor mediated inhibitory signaling pathway; IEA:Ensembl.
DR   GO; GO:0002431; P:Fc receptor mediated stimulatory signaling pathway; IEA:Ensembl.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0038043; P:interleukin-5-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0070667; P:negative regulation of mast cell proliferation; IEA:Ensembl.
DR   GO; GO:0002762; P:negative regulation of myeloid leukocyte differentiation; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; IEA:Ensembl.
DR   GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0002576; P:platelet degranulation; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0070668; P:positive regulation of mast cell proliferation; IEA:Ensembl.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0070304; P:positive regulation of stress-activated protein kinase signaling cascade; IEA:Ensembl.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR   GO; GO:0002902; P:regulation of B cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0050855; P:regulation of B cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR   GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl.
DR   GO; GO:0045646; P:regulation of erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0033003; P:regulation of mast cell activation; IEA:Ensembl.
DR   GO; GO:0043304; P:regulation of mast cell degranulation; IEA:Ensembl.
DR   GO; GO:0090025; P:regulation of monocyte chemotaxis; IEA:Ensembl.
DR   GO; GO:0090330; P:regulation of platelet aggregation; IEA:Ensembl.
DR   GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR   GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR   GO; GO:0002513; P:tolerance induction to self antigen; IEA:Ensembl.
DR   GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:Ensembl.
DR   CDD; cd05072; PTKc_Lyn; 1.
DR   CDD; cd10364; SH2_Src_Lyn; 1.
DR   CDD; cd12004; SH3_Lyn; 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; IPR035852; Lyn_SH2.
DR   InterPro; IPR035748; Lyn_SH3.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
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:SF42; TYROSINE-PROTEIN KINASE LYN; 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; PS00107; PROTEIN_KINASE_ATP; 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|PROSITE-ProRule:PRU10141,
KW   ECO:0000256|RuleBase:RU362096};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW   SH2 domain {ECO:0000256|PROSITE-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          65..125
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          131..228
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          249..503
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         277
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   514 AA;  59063 MW;  17873851F48F100A CRC64;
     MGCIKSKRKD NPPHDGIDLK TQPVRNTDRT IYVRDPTSNK QQRPVLNQGT QLLPGQRFQN
     KDPEEQGNVV IALYAYEGLH PDDLSFKKGE KLKILEEHGE WWKARSLISK KEGFIPSNYV
     AKINTLETEE WFFKDITRKD AERQLLAPGN SAGAFLIRES ETLKGSYSLS VRDYDPLHGD
     VIKHYKIRSL DNGGYYISPR ITFPCISDMI KHYQKQPDGL CRRLEKACIS PKPQKPWDKD
     AWEIPRESIK LVKKLGAGQF GEVWMGYYNN STKVAVKTLK PGTMSVQAFL EEANLMKTLQ
     HDKLVRLYAV VTKEEPIYII TEYMAKGSLL DFLKSDEGGK LLLPKLIDFS AQIAEGMAYI
     ERKNYIHRDL RAANVLVSDS LMCKIADFGL ARIIEDNEYT AREGAKFPIK WTAPEAINFG
     YFTIKSDVWS FGILLYEIVT YGKIPYPGRT NADVMMALGQ GYRMPRMENC PEELYDIMKM
     CWKEKAEERP TFDYLQSVLD DFYTATEGQY QQQP
//
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