ID A0A498MGP1_LABRO Unreviewed; 1237 AA.
AC A0A498MGP1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN ORFNames=ROHU_007303 {ECO:0000313|EMBL:RXN19300.1}, ROHU_031629
GN {ECO:0000313|EMBL:RXN08687.1}, ROHU_031667
GN {ECO:0000313|EMBL:RXN08725.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN19300.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN19300.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN19300.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN19300.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN19300.1}.
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DR EMBL; QBIY01013300; RXN08687.1; -; Genomic_DNA.
DR EMBL; QBIY01013300; RXN08725.1; -; Genomic_DNA.
DR EMBL; QBIY01012674; RXN19300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MGP1; -.
DR STRING; 84645.A0A498MGP1; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08687; C2_PKN-like; 1.
DR CDD; cd11622; HR1_PKN_1; 1.
DR CDD; cd05589; STKc_PKN; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037784; C2_PKN.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR037313; PKN_HR1_1.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR005331; Sulfotransferase.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF322; SERINE_THREONINE-PROTEIN KINASE N2; 1.
DR Pfam; PF02185; HR1; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR Pfam; PF03567; Sulfotransfer_2; 1.
DR SMART; SM00742; Hr1; 3.
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; SSF46585; HR1 repeat; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RXN19300.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 342..418
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 433..513
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 519..598
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 910..1169
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1170..1237
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 792..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 24..51
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 939
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1237 AA; 142405 MW; B911278E9F46CF54 CRC64;
MGLLRLKMPP KFQLLALLAF AIAMIFLENQ IQKLEESRGK LERAIARHEV REIEQRHIQE
GAKETLVEED DLVVIYNRVP KTASTSFTNI AYDLCNKNHY HVLHINTTKN NPVMSLQDQV
RFVKNVTLWK EMKPAFYHGH VSFLDFTKFG VKKKPIYINV IRDPIERLVS YYYFLRFGDD
YRPGLRRRKQ GDKKTFDECV AAGGSDCAPE KLWLQIPFFC GHYSECWNIG SRWALEQAKY
NLVNEYMLVG VTEELEDFVM MLEAALPRFF KGATELYRTG KKSHLRKTSE KKPPTKESIA
RLQQSDIWKM ENEFYEFALE QFQYVRAHAA HMVSDRLGLG HNLDLSDTMV QQKLDEIKEQ
IKREIRKELK IKEGVENLRK VTTEKKRLAY VDNMLKKSNK KLEELHQELQ ELNAHIVVKD
PEDLLLECPL TLDSPKSEAR TCTISSRLAA LKKQNDIELK VKQGAENMIQ MYSNGSSKDR
KLLATAQQML QDSKTKIEFI RMQILKASQT SELSFDNNDV IAKPIISPLD LRVEELCHHT
RIEYAVAEGA KNVMKLLGSG KLAEKRAHSE AQARFNESSQ KLDLLKYSLE QRLNELPKNH
PKSSLIMEEL SLMSSPALSP RQSFISTQNH NSTVKNQYST KPAALTDEIS AVLKLDNTVV
GQTSWKPVSN QSWDQKFTLE LDRSRELEIS VYWRDWRSLC AVKFLRLEDF LDNQRHGMCL
YLEPQGTLFA EVTFFNPVIE RRTKLQRQKK IFSKQQGKPF LRAPQMSIGT WGRLVRRAIP
SPNNSFSPQV AELAAETGHS SHPGTPALRS DPIVTKLDFD KDATPKHYSP VSIREVLPED
KIPNKEQEQD ALTSFDYRND RNSIIVQSEL AEVVEHETQP SALQLITVQK STEIRDEEEE
EQFHFSLKDF KCVAVLGRGH FGKVLLAEYS ITGEMFAIKA LKKGDIVARD EVESLMCEKR
IFETVNSVRH PFLVNLFACF QTKEHVCFVM EYAAGGDLMM HIHADVFSEP RATFYAACVV
LGLQFLHEHK IVYRDLKLDN LLLDTEGFVK IADFGLCKEG MGYRDRTSTF CGTPEFLAPE
VLTETSYTRA VDWWGLGVLI FEMLVGESPF PGDDEEEVFD SIVNDEVRYP RFLSTEAISI
MRRLLRRNPE RRLGAGERDA EDVKKHLFFR NIDWDGLLAK KAKPPFVPTI QSSSDVSNFD
DEFTSEAPVL TPPREPRPLT QHEQDLFADF DYIADWC
//
