ID H2N406_PONAB Unreviewed; 884 AA.
AC H2N406; A0A2J8V736; A0A2J8V769;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Dual serine/threonine and tyrosine protein kinase {ECO:0000256|ARBA:ARBA00040421};
DE EC=2.7.12.1 {ECO:0000256|ARBA:ARBA00013203};
DE AltName: Full=Dusty protein kinase {ECO:0000256|ARBA:ARBA00042638};
DE AltName: Full=Receptor-interacting serine/threonine-protein kinase 5 {ECO:0000256|ARBA:ARBA00041268};
GN Name=DSTYK {ECO:0000313|Ensembl:ENSPPYP00000000336.3};
GN ORFNames=CR201_G0022182 {ECO:0000313|EMBL:PNJ53339.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000000336.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000000336.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ53339.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ53339.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000000336.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000972};
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=2.7.12.1; Evidence={ECO:0000256|ARBA:ARBA00001076};
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=2.7.12.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001687};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Basolateral cell membrane
CC {ECO:0000256|ARBA:ARBA00004187}. Cell junction
CC {ECO:0000256|ARBA:ARBA00004282}. Lateral cell membrane
CC {ECO:0000256|ARBA:ARBA00004124}.
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DR EMBL; NDHI03003431; PNJ53339.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000000336; -.
DR Ensembl; ENSPPYT00000000353.3; ENSPPYP00000000336.3; ENSPPYG00000000309.3.
DR eggNOG; KOG0192; Eukaryota.
DR GeneTree; ENSGT00840000129948; -.
DR HOGENOM; CLU_014116_0_0_1; -.
DR OrthoDB; 5400763at2759; -.
DR TreeFam; TF331821; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46392; DUAL SERINE/THREONINE AND TYROSINE PROTEIN KINASE; 1.
DR PANTHER; PTHR46392:SF1; DUAL SERINE_THREONINE AND TYROSINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 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; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 652..884
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 884 AA; 100024 MW; 3D1EBE0D4C782BC4 CRC64;
MESDGVPWGS EPVSGPGPGG GGMIRELCRG FGRYRRYLGR LRQNLRETQK FFRDIKCSHN
HTCLSSLTGG GGAERGPAGD VAETGLQAGK LSCISFPPKE EKYLQQIVDC LPCILILGQD
CNVKCQLLNL LLGVQVLPTT KLGSEESCKL RRLRFTYGTQ TRVSLALPGQ YELVHTLAAH
QGNWETIPEE DLEVQENNED AAHVLAELEV TMHHALLQEV DVVVAPCQGL RPTVDVLGDL
VNDFLPVITY ALHKDELSER DEQELQEIRK YFSFPVFFFK VPKLGSEIID SSTRRMESER
SPLYRQLIDL GYLSSSHWNC GAPGQDTKAQ SMLVEQSEKL RHLSTFSHQV LQTRLVDAAK
ALNLVHCHCL DIFINQAFDM QRDLQITPKR LEYTRKKENE LYESLMNIAN RKQEEMKDMI
VETLNTMKEE LLDDATNMEF KDVIVPENGE PVGTREIKCC IRQIQELIIS RLNQAVANKL
ISSVDYLRES FVGTLERCLQ SLEKSQDVSV HITSNYLKQI LNAAYHVEVT FHSGSSVTRM
LWEQIKQIIQ RITWVSPPAI TLEWKRKVAQ EAIESLSASK LAKSICSQFR TRLNSSHEAF
AASLRQLEAG HSGRLEKTED LWLRVRKDHA PRLARLSLES RSLQDVLLHR KPKLGQELGR
GQYGVVYLCD NWGGHFPCAL KSVVPPDEKH WNDLALEFHY MRSLPKHERL VDLHGSVIDY
NYGGGSSIAV LLIMERLHRD LYTGLKAGLT LETRLQIALD VVEGIRFLHS QGLVHRDIKL
KNVLLDKQNR AKITDLGFCK PEAMMSGSIV GTPIHMAPEL FTGARPERLP VFDEECWQLM
EACWDGDPLK RPLLGIVQPM LQGIMDRLCK SNSEQPNRGL DDST
//
