ID G3U2F0_LOXAF Unreviewed; 589 AA.
AC G3U2F0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000604};
DE EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000604};
GN Name=ZAP70 {ECO:0000313|Ensembl:ENSLAFP00000022008.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000022008.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000022008.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022008.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000022008.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022008.1};
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|PIRNR:PIRNR000604};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SYK/ZAP-70 subfamily. {ECO:0000256|PIRNR:PIRNR000604}.
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DR AlphaFoldDB; G3U2F0; -.
DR Ensembl; ENSLAFT00000031022.1; ENSLAFP00000022008.1; ENSLAFG00000030913.1.
DR GeneTree; ENSGT00940000159185; -.
DR HOGENOM; CLU_000288_7_2_1; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR023420; Kinase_SYK/ZAP-70_inter-SH2_sf.
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; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR012234; Tyr_kinase_non-rcpt_SYK/ZAP70.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF369; TYROSINE-PROTEIN KINASE ZAP-70; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 2.
DR PIRSF; PIRSF000604; TyrPK_SYK; 2.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR000604, ECO:0000256|PIRSR:PIRSR000604-
KW 2}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000604};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000604,
KW ECO:0000256|PIRSR:PIRSR000604-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000604};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW ECO:0000256|PIRNR:PIRNR000604}.
FT DOMAIN 10..88
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 154..245
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 332..584
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 88..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 448
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-1"
FT BINDING 338..346
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000604-2"
SQ SEQUENCE 589 AA; 66252 MW; 9FF3F58B1BD47139 CRC64;
MPDPAAHLPF FYGSISRAEA EDHLKLAGMS DGLFLLRQCL RSLGGLRALA GARRGPFHHF
PVERQAPTGT YSNSGRRPTG LPWKTLAKAG QPGRRGLGSP KPGVARPIKD GLRPRRDRGD
RWSFGGEALE QAIISQAPQV EKLIATTAHE RMPWYHTNLT REEAERKLYS GAQTDGKFLL
RPRKEQGTYA LSLIYGKTVY HYLISQDKAG KYCIPEGTKF DTLWQLVEYL KLKADGLIYC
LKEACPNSSA SAASGAAAPT LPAHPSTLTQ PQRRMDTLNS DGYTPEPARP VSSEKTEKKR
PLPMDTSVYE SPYSDPEELK DKKLFLKREN LLVADLELGC GNFGSVRQGV YRMRKYGGPA
RVGALPGWGP WGAGAGVASP WVKPHLLRSA GLHYPNTWGQ IHQPRDAADI SLSLTKKEEI
PVSNVAELLH QVTMGMRYLE EKNFVHRDLA ARNVLLVNRH YAKISDFGLS KALGADDSYY
TARSAGKWPL KWYAPECINF RKFSSRSDVW SFGVTMWEAF SYGQKPYKKM KGPEVITFIE
QGKRMECPAE CPPEMYTLMR DCWTYKWEDR PDFLTVEQRM RTYYYSLAS
//
