ID   A0A2U3XFL3_LEPWE        Unreviewed;       454 AA.
AC   A0A2U3XFL3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Protein kinase C gamma type {ECO:0000256|ARBA:ARBA00039208};
GN   Name=PRKCH {ECO:0000313|RefSeq:XP_006730123.1};
OS   Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC   Leptonychotes.
OX   NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006730123.1};
RN   [1] {ECO:0000313|RefSeq:XP_006730123.1}
RP   IDENTIFICATION.
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_006730123.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
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DR   RefSeq; XP_006730123.1; XM_006730060.2.
DR   AlphaFoldDB; A0A2U3XFL3; -.
DR   STRING; 9713.A0A2U3XFL3; -.
DR   GeneID; 102749030; -.
DR   KEGG; lww:102749030; -.
DR   CTD; 5583; -.
DR   OrthoDB; 841660at2759; -.
DR   Proteomes; UP000245341; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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   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; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR22968:SF14; -; 1.
DR   PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 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; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Kinase {ECO:0000313|RefSeq:XP_006730123.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245341};
KW   Synapse {ECO:0000256|ARBA:ARBA00022599};
KW   Synaptosome {ECO:0000256|ARBA:ARBA00022599};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1..118
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          171..222
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          245..295
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          355..454
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          320..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   454 AA;  51416 MW;  12AE017E36EF6327 CRC64;
     MTSGTMKFNG YLRVRIGEAV GLQPTRWSLR HSLFKKGYQL LDPYLTVSVD QVRVGQTSTK
     QKTNKPTYNE EFCTNVTDGG HLELAVFHET PLGYDHFVAN CTLQFQELLR TAGASDTFEG
     WVDLEPEGKV FVVITLTGSF TEATLQRDRI FKHFTRKRQR AMRRRVHQIN GHKFMATYLR
     QPTYCSHCRE FIWGVFGKQG YQCQVCTCVV HKRCHHLIVT ACTCQNNINK MDSKIAEQRF
     GINIPHKFSI HNYKVPTFCD HCGSLLWGIM RQGLQCKICK MNVHIRCQAN VAPNCGVNAV
     ELAKTLAGMG LQPGNISPTS KLVSRSTLRR QGRENTKEGN GIGVDSSSRL GINNFEFIRV
     LGKGSFGKVM LARIKETGDL YAVKVLKKDV ILQDDDVECT MTEKRILSLA RNHPFLTQLF
     CCFQTPGRME VPVTSDDLWE KVEISELTAT VMLS
//