PCK1_SCHPO
ID PCK1_SCHPO Reviewed; 988 AA.
AC P36582; Q9UTU9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Protein kinase C-like 1;
DE EC=2.7.11.13;
GN Name=pck1; ORFNames=SPAC17G8.14c, SPAC22H10.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8491190; DOI=10.1002/j.1460-2075.1993.tb05848.x;
RA Toda T., Shimanuki M., Yanagida M.;
RT "Two novel protein kinase C-related genes of fission yeast are essential
RT for cell viability and implicated in cell shape control.";
RL EMBO J. 12:1987-1995(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 318-535.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Involved in the control of the cell shape. Target of the
CC inhibitor staurosporine.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Cell
CC septum {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
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DR EMBL; D14337; BAA03267.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93697.1; -; Genomic_DNA.
DR EMBL; AB027982; BAA87286.1; -; Genomic_DNA.
DR PIR; S35362; S35362.
DR RefSeq; NP_593737.2; NM_001019168.2.
DR AlphaFoldDB; P36582; -.
DR SMR; P36582; -.
DR BioGRID; 278761; 111.
DR STRING; 4896.SPAC17G8.14c.1; -.
DR iPTMnet; P36582; -.
DR MaxQB; P36582; -.
DR PaxDb; P36582; -.
DR PRIDE; P36582; -.
DR EnsemblFungi; SPAC17G8.14c.1; SPAC17G8.14c.1:pep; SPAC17G8.14c.
DR GeneID; 2542293; -.
DR KEGG; spo:SPAC17G8.14c; -.
DR PomBase; SPAC17G8.14c; pck1.
DR VEuPathDB; FungiDB:SPAC17G8.14c; -.
DR eggNOG; KOG0694; Eukaryota.
DR HOGENOM; CLU_000288_54_0_1; -.
DR InParanoid; P36582; -.
DR OMA; QIMRCAV; -.
DR PhylomeDB; P36582; -.
DR BRENDA; 2.7.11.13; 5613.
DR Reactome; R-SPO-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-SPO-114516; Disinhibition of SNARE formation.
DR Reactome; R-SPO-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-SPO-1489509; DAG and IP3 signaling.
DR Reactome; R-SPO-202424; Downstream TCR signaling.
DR Reactome; R-SPO-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-SPO-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-SPO-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-SPO-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-SPO-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-SPO-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-SPO-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-SPO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-SPO-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-SPO-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-SPO-76005; Response to elevated platelet cytosolic Ca2+.
DR Reactome; R-SPO-8980692; RHOA GTPase cycle.
DR Reactome; R-SPO-9013026; RHOB GTPase cycle.
DR Reactome; R-SPO-9013106; RHOC GTPase cycle.
DR Reactome; R-SPO-9634635; Estrogen-stimulated signaling through PRKCZ.
DR PRO; PR:P36582; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
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:0004699; F:calcium-independent protein kinase C activity; EXP:PomBase.
DR GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0090334; P:regulation of cell wall (1->3)-beta-D-glucan biosynthetic process; IMP:PomBase.
DR CDD; cd00029; C1; 2.
DR Gene3D; 2.60.40.150; -; 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; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
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; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00742; Hr1; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46585; SSF46585; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
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; PS51860; REM_1; 2.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding; Cell shape; Coiled coil; Cytoplasm; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..988
FT /note="Protein kinase C-like 1"
FT /id="PRO_0000055740"
FT DOMAIN 1..68
FT /note="REM-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 107..182
FT /note="REM-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 189..315
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 664..923
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 924..988
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 413..461
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 480..530
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 64..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 789
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 670..678
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 693
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 27..35
FT /note="AMVASTKNP -> SNGGFDGES (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 988 AA; 111784 MW; 0969BDEC1AB43C4E CRC64;
MVQLDDALQD AYKKVEREES LILGAKAMVA STKNPEVKRR LESNIAVSEN NIKYLRERID
ALKVESGSER ESQSDKDSSK KYSDSAKSTN SDDHLLSYNR SAFDLFNSEK PLSPEKISTM
LQHLQMRLSI EQQCVSGIEK IMSLYSKEQK DKTDVIIKLK EGKQKVNLLK RSLKRYNELH
IPFDISTPSS EEKQQASGLN FRGLAKPISG TLKVTIHSLR NIEHTSFLQT HSFTMPSYAV
LYVDDAQVAK SRISQTDTWD ETFIFDVHRA KEFQIIIYEK KKDFDIPIAL ILIPTTIIAE
ELRRKRNIQE MSETSWKPSI AESASRSDEK GSKSDPINAP NSSSSISTNS PLAPTAYYKL
LSKSWLSLEP VGQICISLSF SKRTTKRQFP ETGLGRQGAI RQKKEDVVAS QVGHQFVQRQ
FYQIMRCAVC AELFSYSPGL QCENCSFVCH KKCVTKVLAS CIAQSNSEKS DFGGLRYRIP
HRFEPFNSLG AQWCAHCGFF LPLRRKDCFK CVECGITCHG QCAHLIPDYC GMSNDLKHQL
LTELEVSKRP KKPELPNQEN KTTNEKVYRK PLSSQNTFDT LPTISQGLLA ATQPVTSVLN
TSPLPKTPEK DRSLNVTPSS STPTPASVLA PPSSASLSSS KDANRSVPES PRREKKNRVT
LDDFTFLAVL GKGNFGKVML AEYKVNKKFY AIKVLKKEAI LKNEELESLK TEKHVFEVAN
KEKHPFLLNL FASFQTSTRV YFVMEYILGG DLMVHIQRQQ FSVKRARFYG AEVCLALKYF
HENGIAYRDL KLDNILLCPD GHIRIADYGL CKENMLLGNT TSTFCGTPEF MAPEILLEQQ
YSKDVDWWAF GVLMYQMLLG QSPFKGEDEE EIFDAILSDE PLFPINMPAD AVSLLRGLLT
RDPNQRLGSG PKDANEVMAH PFFASIVWDD LYNKLYEPSY KPLINDPRDL NNFDEEFTSA
CPTLTPVNTV LTRQQQECFR GFSSFATE
