UniProt: A0A3Q1B2V7

Database: UniProt
Entry: A0A3Q1B2V7_AMPOC

LinkDB:  A0A3Q1B2V7_AMPOC 
Original site:  A0A3Q1B2V7_AMPOC

All links

Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (27)   
   InterPro (12)   
   Pfam (4)   
   PROSITE (7)   
   SMART (4)   
All databases (37)   

Download RDF

ID   A0A3Q1B2V7_AMPOC        Unreviewed;       678 AA.
AC   A0A3Q1B2V7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Protein kinase C {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000551};
DE            EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429, ECO:0000256|PIRNR:PIRNR000551};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000004411.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000004411.1}
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=2.7.11.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00000946};
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=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569,
CC         ECO:0000256|PIRNR:PIRNR000551};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490,
CC       ECO:0000256|PIRNR:PIRNR000551}.
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; A0A3Q1B2V7; -.
DR   STRING; 80972.ENSAOCP00000004411; -.
DR   Ensembl; ENSAOCT00000008112.1; ENSAOCP00000004411.1; ENSAOCG00000007835.1.
DR   GeneTree; ENSGT00940000158220; -.
DR   OMA; MTKNPNM; -.
DR   OrthoDB; 841660at2759; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd20835; C1_nPKC_epsilon-like_rpt1; 1.
DR   CDD; cd20838; C1_nPKC_epsilon-like_rpt2; 1.
DR   CDD; cd04014; C2_PKC_epsilon; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR014376; Prot_kin_PKC_delta.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF198; PROTEIN KINASE C ETA TYPE; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000551; PKC_delta; 2.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000551};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000551};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000551};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000551};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000551};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1..118
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          168..219
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          240..290
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          348..608
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          609..678
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          625..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        472
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000551-50"
FT   BINDING         354..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000551-51"
FT   BINDING         377
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000551-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   678 AA;  77070 MW;  8835760A6067E8EA CRC64;
     MKFNGYLKLR IGEAVDLKPT TFSLRHSVIF NKAPPALDPY IVVKVDDYKI GQTHTKQKTN
     MPTYNEEFCL NVNDGKQIEL AVFHDTPIGY DDFVANCIIQ LEDLIQTSNT GETFEGWMDL
     EPEGKVYVLI TLTGSFTDDD ALVKEKTYKQ FTRKRQRAVK RKIHQVNGHK FMSTFLRQPT
     FCFHCKEFIW GVFGKQGYQC QVCTCVVHKR CHEHVVTVCP LMKKPAKEQP INQGFSINVP
     HKFNMHNYKS PTFCDHCGSL LWGIVRQGLH CKSCKMNVHI RCKGNVAPNC GVNSVELANR
     LAEMGLQAGG LAKRNSVVKS VEPMKAPSER RESTEVQRQT PRLGISNFTF LQVLGKGSFG
     KVMLARLNNK ERVFAVKVLK KDIILQDDDV ECTMTEKRVL SLARCHPYLT QLYCCFQTPD
     RLFFVMEFVN GGDLMFHIQK SRKFEEARAR FYSAEITSAL MFLHSKGIIY RDLKLDNVLL
     DKDGHCKLAD FGMCKEGIFE GVATGTFCGT PDYIAPEILQ EMLYGPSVDW WALGVLLFEM
     LSGHAPFEAE NEDDLFESIL NEEIVYASWL STEAVNILKA LLTKNPARRL GCVASEGGES
     AVTSHAFFAN IDWEKLNRRE IEPPFKPRIK TPEDVNNFDP DFTQEEPTLT PIDDPVIPSV
     SQEEFKNFSF TSPELLES
//

DBGET integrated database retrieval system