KPCI_DANRE
ID KPCI_DANRE Reviewed; 588 AA.
AC Q90XF2; Q7ZU17;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein kinase C iota type;
DE EC=2.7.11.13;
DE AltName: Full=Atypical protein kinase C-lambda/iota;
DE Short=aPKC-lambda/iota;
DE AltName: Full=Heart and soul protein;
DE AltName: Full=nPKC-iota;
GN Name=prkci; Synonyms=hal;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=11591316; DOI=10.1016/s0960-9822(01)00458-4;
RA Horne-Badovinac S., Lin D., Waldron S., Schwarz M., Mbamalu G., Pawson T.,
RA Jan Y.-N., Stainier D.Y., Abdelilah-Seyfried S.;
RT "Positional cloning of heart and soul reveals multiple roles for PKC lambda
RT in zebrafish organogenesis.";
RL Curr. Biol. 11:1492-1502(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium- and diacylglycerol-independent serine/ threonine-
CC protein kinase that plays a general protective role against apoptotic
CC stimuli, is involved in NF-kappa-B activation, cell survival,
CC differentiation and polarity, and contributes to the regulation of
CC microtubule dynamics in the early secretory pathway (By similarity). Is
CC required for the formation and maintenance of the zonula adherens
CC during early epithelial development and plays a critical role in organ
CC morphogenesis and in regulating the orientation of cell division.
CC {ECO:0000250, ECO:0000269|PubMed:11591316}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Exhibits an elevated basal enzymatic activity and
CC is not regulated by diacylglycerol, phosphatidylserine, phorbol esters
CC or calcium ions. Two specific sites, Thr-404 (activation loop of the
CC kinase domain) and Thr-556 (turn motif), need to be phosphorylated for
CC its full activation (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The C1 zinc finger does not bind the diacylglycerol (DAG).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK91291.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF390109; AAK91291.1; ALT_INIT; mRNA.
DR EMBL; BC047164; AAH47164.1; -; mRNA.
DR RefSeq; NP_571930.2; NM_131855.2.
DR AlphaFoldDB; Q90XF2; -.
DR SMR; Q90XF2; -.
DR STRING; 7955.ENSDARP00000005309; -.
DR PaxDb; Q90XF2; -.
DR PRIDE; Q90XF2; -.
DR Ensembl; ENSDART00000015723; ENSDARP00000005309; ENSDARG00000021225.
DR GeneID; 117507; -.
DR KEGG; dre:117507; -.
DR CTD; 5584; -.
DR ZFIN; ZDB-GENE-011105-1; prkci.
DR eggNOG; KOG0695; Eukaryota.
DR GeneTree; ENSGT00940000153497; -.
DR HOGENOM; CLU_000288_63_29_1; -.
DR InParanoid; Q90XF2; -.
DR OMA; RIQCFIC; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; Q90XF2; -.
DR TreeFam; TF102004; -.
DR Reactome; R-DRE-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-DRE-209543; p75NTR recruits signalling complexes.
DR Reactome; R-DRE-420029; Tight junction interactions.
DR PRO; PR:Q90XF2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 2.
DR Bgee; ENSDARG00000021225; Expressed in blastula and 33 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:HGNC.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:ZFIN.
DR GO; GO:0005634; C:nucleus; ISS:HGNC.
DR GO; GO:0005915; C:zonula adherens; IDA:ZFIN.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; ISS:HGNC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:HGNC.
DR GO; GO:0034334; P:adherens junction maintenance; IMP:ZFIN.
DR GO; GO:0034332; P:adherens junction organization; IMP:ZFIN.
DR GO; GO:0045176; P:apical protein localization; IMP:ZFIN.
DR GO; GO:0007420; P:brain development; IMP:ZFIN.
DR GO; GO:0030031; P:cell projection assembly; IMP:ZFIN.
DR GO; GO:0045217; P:cell-cell junction maintenance; IMP:ZFIN.
DR GO; GO:0045216; P:cell-cell junction organization; ISS:HGNC.
DR GO; GO:0007502; P:digestive tract mesoderm development; IMP:ZFIN.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:ZFIN.
DR GO; GO:0021744; P:dorsal motor nucleus of vagus nerve development; IMP:ZFIN.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:ZFIN.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:ZFIN.
DR GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:ZFIN.
DR GO; GO:0048699; P:generation of neurons; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:ZFIN.
DR GO; GO:0008078; P:mesodermal cell migration; IMP:ZFIN.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:ZFIN.
DR GO; GO:0001841; P:neural tube formation; IGI:ZFIN.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:ZFIN.
DR GO; GO:0007097; P:nuclear migration; IMP:ZFIN.
DR GO; GO:0042476; P:odontogenesis; IMP:ZFIN.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:ZFIN.
DR GO; GO:0035778; P:pronephric nephron tubule epithelial cell differentiation; IGI:ZFIN.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:ZFIN.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:ZFIN.
DR GO; GO:0021591; P:ventricular system development; IMP:ZFIN.
DR CDD; cd00029; C1; 1.
DR CDD; cd06404; PB1_aPKC; 1.
DR CDD; cd05618; STKc_aPKC_iota; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR034661; aPKC_iota.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR034877; PB1_aPKC.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR012233; PKC.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000554; PKC_zeta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS51745; PB1; 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; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Developmental protein; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..588
FT /note="Protein kinase C iota type"
FT /id="PRO_0000055713"
FT DOMAIN 18..101
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 246..514
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 515..586
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 133..183
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 194..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 252..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 404
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305"
FT MOD_RES 556
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 588 AA; 67322 MW; C4E93B83AE67C79B CRC64;
MPTLRDSTMS HPGENPHQVR VKAYYRGDIM ITHFEPSISY EGLCNEVRDM CSMDNDQLFT
MKWIDEEGDP CTVSSQLELE EALRLYELNK DSELIIHVFP CVPEKPGMPC PGEDKSIYRR
GARRWRKLYY ATGHAFQAKR FNRRAHCAIC TDRIWGLGRQ GYKCINCKLL VHKKCHKLVT
VECGRQVIQD PMIGRIDPGS THPEHPDQVL GKKNSTESIN HEGEEHEAVG SRESGKAVSS
LGLIDFDLLR VIGRGSYAKV LLVRLKKTER IYAMKVVKKE LVNDDEDIDW VQTEKHVFEQ
ASNHPFLVGL HSCFQTESRL FFVIEYVNGG DLMFHMQRQR KLPEEHARFY SAEISLALNY
LHERGIIYRD LKLDNVLLDS EGHIKLTDYG MCKEGLRPGD TTSTFCGTPN YIAPEILRGE
DYGFSVDWWA LGVLMFEMMA GRSPFDIVGS SDNPDQNTED YLFQVILEKQ IRIPRSLSVK
AASVLKGFLN KESKERLGCH PQTGFADIMA HPFFRNVDWD LMEQKQVVPP FKPNISGEFG
LDNFDAQFTN EPIQLTPDDD DAVKKIDQSE FEGFEYINPL LMSAEECV
