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Protein kinase C iota type (EC 2.7.11.13) (Atypical protein kinase C-lambda/iota) (aPKC-lambda/iota) (Heart and soul protein) (nPKC-iota)

 KPCI_DANRE              Reviewed;         588 AA.
Q90XF2; Q7ZU17;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 2.
07-JUN-2017, entry version 135.
RecName: Full=Protein kinase C iota type;
EC=2.7.11.13;
AltName: Full=Atypical protein kinase C-lambda/iota;
Short=aPKC-lambda/iota;
AltName: Full=Heart and soul protein;
AltName: Full=nPKC-iota;
Name=prkci; Synonyms=hal;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=11591316; DOI=10.1016/S0960-9822(01)00458-4;
Horne-Badovinac S., Lin D., Waldron S., Schwarz M., Mbamalu G.,
Pawson T., Jan Y.-N., Stainier D.Y., Abdelilah-Seyfried S.;
"Positional cloning of heart and soul reveals multiple roles for PKC
lambda in zebrafish organogenesis.";
Curr. Biol. 11:1492-1502(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=AB;
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Calcium- and diacylglycerol-independent serine/
threonine-protein kinase that plays a general protective role
against apoptotic stimuli, is involved in NF-kappa-B activation,
cell survival, differentiation and polarity, and contributes to
the regulation of microtubule dynamics in the early secretory
pathway (By similarity). Is required for the formation and
maintenance of the zonula adherens during early epithelial
development and plays a critical role in organ morphogenesis and
in regulating the orientation of cell division. {ECO:0000250,
ECO:0000269|PubMed:11591316}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Exhibits an elevated basal enzymatic activity
and is not regulated by diacylglycerol, phosphatidylserine,
phorbol esters or calcium ions. Two specific sites, Thr-404
(activation loop of the kinase domain) and Thr-556 (turn motif),
need to be phosphorylated for its full activation (By similarity).
{ECO:0000250}.
-!- DOMAIN: The C1 zinc finger does not bind the diacylglycerol (DAG).
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK91291.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF390109; AAK91291.1; ALT_INIT; mRNA.
EMBL; BC047164; AAH47164.1; -; mRNA.
RefSeq; NP_571930.2; NM_131855.2.
UniGene; Dr.2532; -.
ProteinModelPortal; Q90XF2; -.
SMR; Q90XF2; -.
STRING; 7955.ENSDARP00000005309; -.
PaxDb; Q90XF2; -.
PRIDE; Q90XF2; -.
Ensembl; ENSDART00000015723; ENSDARP00000005309; ENSDARG00000021225.
GeneID; 117507; -.
KEGG; dre:117507; -.
CTD; 5584; -.
ZFIN; ZDB-GENE-011105-1; prkci.
eggNOG; KOG0695; Eukaryota.
eggNOG; ENOG410ZMG2; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; Q90XF2; -.
KO; K06069; -.
OMA; KGDIMIT; -.
OrthoDB; EOG091G03Q9; -.
PhylomeDB; Q90XF2; -.
TreeFam; TF102004; -.
Reactome; R-DRE-209543; p75NTR recruits signalling complexes.
Reactome; R-DRE-420029; Tight junction interactions.
PRO; PR:Q90XF2; -.
Proteomes; UP000000437; Chromosome 2.
Bgee; ENSDARG00000021225; -.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:ZFIN.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005915; C:zonula adherens; IDA:ZFIN.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0034334; P:adherens junction maintenance; IMP:ZFIN.
GO; GO:0034332; P:adherens junction organization; IMP:ZFIN.
GO; GO:0007420; P:brain development; IMP:ZFIN.
GO; GO:0045217; P:cell-cell junction maintenance; IMP:ZFIN.
GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
GO; GO:0007502; P:digestive tract mesoderm development; IMP:ZFIN.
GO; GO:0048546; P:digestive tract morphogenesis; IMP:ZFIN.
GO; GO:0021744; P:dorsal motor nucleus of vagus nerve development; IMP:ZFIN.
GO; GO:0035050; P:embryonic heart tube development; IMP:ZFIN.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:ZFIN.
GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:ZFIN.
GO; GO:0048699; P:generation of neurons; IMP:ZFIN.
GO; GO:0007507; P:heart development; IMP:ZFIN.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:ZFIN.
GO; GO:0008078; P:mesodermal cell migration; IMP:ZFIN.
GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:ZFIN.
GO; GO:0001841; P:neural tube formation; IGI:ZFIN.
GO; GO:0007405; P:neuroblast proliferation; IMP:ZFIN.
GO; GO:0007097; P:nuclear migration; IMP:ZFIN.
GO; GO:0042476; P:odontogenesis; IMP:ZFIN.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:ZFIN.
GO; GO:0035778; P:pronephric nephron tubule epithelial cell differentiation; IGI:ZFIN.
GO; GO:0060041; P:retina development in camera-type eye; IMP:ZFIN.
GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:ZFIN.
GO; GO:0021591; P:ventricular system development; IMP:ZFIN.
CDD; cd00029; C1; 1.
CDD; cd06404; PB1_aPKC; 1.
CDD; cd05618; STKc_aPKC_iota; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR034661; aPKC_iota.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR034877; PB1_aPKC.
InterPro; IPR000270; PB1_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR012233; PKC.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 1.
Pfam; PF00564; PB1; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000554; PKC_zeta; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 1.
SMART; SM00666; PB1; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS51745; PB1; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Developmental protein; Kinase;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
CHAIN 1 588 Protein kinase C iota type.
/FTId=PRO_0000055713.
DOMAIN 18 101 PB1. {ECO:0000255|PROSITE-
ProRule:PRU01081}.
DOMAIN 246 514 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 515 586 AGC-kinase C-terminal.
ZN_FING 133 183 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 252 260 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 370 370 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 275 275 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 404 404 Phosphothreonine. {ECO:0000305}.
MOD_RES 556 556 Phosphothreonine. {ECO:0000305}.
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


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