ID Q7SZH8_XENLA Unreviewed; 683 AA.
AC Q7SZH8;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Protein kinase C delta type {ECO:0000256|PIRNR:PIRNR000551};
DE EC=2.7.11.13 {ECO:0000256|PIRNR:PIRNR000551};
DE AltName: Full=nPKC-delta {ECO:0000256|PIRNR:PIRNR000551};
GN Name=PKC-delta1 {ECO:0000313|EMBL:BAC79119.1};
GN Synonyms=may1 {ECO:0000313|RefSeq:XP_041447208.1}, npkc-delta
GN {ECO:0000313|RefSeq:XP_041447208.1}, PKC-delta
GN {ECO:0000313|RefSeq:XP_041447208.1}, pkc-delta1
GN {ECO:0000313|RefSeq:XP_041447208.1}, pkcd
GN {ECO:0000313|RefSeq:XP_041447208.1}, PKCd1
GN {ECO:0000313|RefSeq:XP_041447208.1}, PKCd2
GN {ECO:0000313|RefSeq:XP_041447208.1}, PKCdelta
GN {ECO:0000313|RefSeq:XP_041447208.1}, PKCdelta1
GN {ECO:0000313|RefSeq:XP_041447208.1}, PKCdelta2
GN {ECO:0000313|RefSeq:XP_041447208.1}, prkcd
GN {ECO:0000313|RefSeq:XP_041447208.1}, prkcd-a
GN {ECO:0000313|RefSeq:XP_041447208.1}, prkcd-b
GN {ECO:0000313|RefSeq:XP_041447208.1}, prkcd.L
GN {ECO:0000313|RefSeq:XP_041447208.1}, prkcd.S
GN {ECO:0000313|RefSeq:XP_041447208.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:BAC79119.1};
RN [1] {ECO:0000313|EMBL:BAC79119.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12842914; DOI=10.1101/gad.1101303;
RA Kinoshita N., Iioka H., Miyakoshi A., Ueno N.;
RT "PKC delta is essential for Dishevelled function in a noncanonical Wnt
RT pathway that regulates Xenopus convergent extension movements.";
RL Genes Dev. 17:1663-1676(2003).
RN [2] {ECO:0000313|RefSeq:XP_041447208.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_041447208.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_041447208.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-
CC dependent serine/threonine-protein kinase that plays contrasting roles
CC in cell death and cell survival by functioning as a pro-apoptotic
CC protein during DNA damage-induced apoptosis, but acting as an anti-
CC apoptotic protein during cytokine receptor-initiated cell death, is
CC involved in tumor suppression. {ECO:0000256|PIRNR:PIRNR000551}.
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 -!- ACTIVITY REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
CC calcium-insensitive, but activated by diacylglycerol (DAG) and
CC phosphatidylserine. {ECO:0000256|PIRNR:PIRNR000551}.
CC -!- SUBUNIT: Interacts with PDPK1 (via N-terminal region), RAD9A, CDCP1,
CC MUC1 and VASP. {ECO:0000256|PIRNR:PIRNR000551}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm
CC {ECO:0000256|PIRNR:PIRNR000551}. Cytoplasm, perinuclear region
CC {ECO:0000256|PIRNR:PIRNR000551}. Nucleus
CC {ECO:0000256|PIRNR:PIRNR000551}.
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}.
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DR EMBL; AB109739; BAC79119.1; -; mRNA.
DR RefSeq; XP_041447208.1; XM_041591274.1.
DR Proteomes; UP000186698; Chromosome 4S.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of 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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0019222; P:regulation of metabolic process; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd20834; C1_nPKC_theta-like_rpt1; 1.
DR CDD; cd20837; C1_nPKC_theta-like_rpt2; 1.
DR CDD; cd05620; STKc_nPKC_delta; 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; IPR034667; nPKC_delta.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR027436; PKC_delta.
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; PTHR24356:SF427; PROTEIN KINASE C DELTA TYPE; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF21494; PKC_C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000551; PKC_delta; 1.
DR PIRSF; PIRSF501104; Protein_kin_C_delta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
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 2: Evidence at transcript level;
KW Apoptosis {ECO:0000256|PIRNR:PIRNR000551};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000551};
KW Cell cycle {ECO:0000256|PIRNR:PIRNR000551};
KW Cytoplasm {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}; Nucleus {ECO:0000256|PIRNR:PIRNR000551};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..106
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 157..207
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 229..279
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 356..610
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 611..682
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT ACT_SITE 480
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-50"
FT BINDING 362..370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51"
FT BINDING 385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000551-51,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 683 AA; 78199 MW; A89BE315FEE5D163 CRC64;
MSPFLRISFN SFDLGGMLSP SDHNQPFCAV KVKESLTTER GKTLVQKKPT MYPDWKSVFD
AHIYEGRVIQ IVLMKAAEDP LSEATVGVSV LAERCKKGNG KSEFWLDLQP QAKVLMSVQY
FLEDADLKQS IREDEGLVTI NKRRGAIKQA KIHYIKNHEF TATFFGQPTF CSVCREFVWG
LNKQGYKCRQ CNAAIHKKCI DKIIGRCTGT AANSRDTVFQ KERFNIDMPH RFKVYNYKSP
TFCDHCGSLL WGLVKQGLKC DECTMNVHHK CQSKVANLCG INQKLLAEAL NQVSMKSSTR
KSDSGLDNIA IYQGVGPKVP GLPVPNAPDN QYDKLWEGIT PHPHISLSSR LKIDNFIFHK
VLGKGSFGKV LLAELKGKGE YFAVKALKKD VVLIDDDVEC TMVEKRVLAL AWENPFLTHV
HCTFQTKEHL FFVMEFLNGG DLMFHIQDKG RFDLYRATFY ASEIICGLQF LHSKGIIYRD
LKLDNVMLDR DGHIKIADFG MCKENVYGDN KASTFCGTPD YIAPEILQGL KYTFSVDWWS
FGVLLYEMLI GQSPFHGDDE DELFESIRQD TPHYPRWITK ESKDILEKFF ERDPFKRLGV
VGNIKLHPFF KTINWTALER RELDPPFKPK VKSPSDYSNF DREFLSEKPR LSFSDKNLID
SMDQSAFHGF SFINPKMERL LEK
//
