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Database: UniProt
Entry: F1SCG1_PIG
LinkDB: F1SCG1_PIG
Original site: F1SCG1_PIG 
ID   F1SCG1_PIG              Unreviewed;       944 AA.
AC   F1SCG1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 3.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE            EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN   Name=PKN1 {ECO:0000313|Ensembl:ENSSSCP00000014650.3,
GN   ECO:0000313|VGNC:VGNC:91481};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000014650.3, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000014650.3, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000014650.3,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000014650.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}.
CC       Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Midbody
CC       {ECO:0000256|ARBA:ARBA00004214}. 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}.
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DR   RefSeq; XP_005661290.2; XM_005661233.2.
DR   AlphaFoldDB; F1SCG1; -.
DR   PaxDb; 9823-ENSSSCP00000014650; -.
DR   PeptideAtlas; F1SCG1; -.
DR   Ensembl; ENSSSCT00000015055.5; ENSSSCP00000014650.3; ENSSSCG00000013779.5.
DR   GeneID; 100515528; -.
DR   CTD; 5585; -.
DR   VGNC; VGNC:91481; PKN1.
DR   eggNOG; KOG0694; Eukaryota.
DR   GeneTree; ENSGT00940000154990; -.
DR   HOGENOM; CLU_030188_0_0_1; -.
DR   OrthoDB; 5400441at2759; -.
DR   TreeFam; TF102005; -.
DR   ChiTaRS; LOC100516063; pig.
DR   Proteomes; UP000008227; Chromosome 2.
DR   Bgee; ENSSSCG00000013779; Expressed in blood and 42 other cell types or tissues.
DR   ExpressionAtlas; F1SCG1; baseline and differential.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd08687; C2_PKN-like; 1.
DR   CDD; cd11630; HR1_PKN1_2; 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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_dom.
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; IPR017892; Pkinase_C.
DR   InterPro; IPR037317; PKN1_HR1_2.
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   PANTHER; PTHR24351:SF229; PROTEIN KINASE C; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF02185; HR1; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 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; 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; PS51860; REM_1; 3.
PE   1: Evidence at protein level;
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
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   Proteomics identification {ECO:0007829|PeptideAtlas:F1SCG1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          25..100
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          113..194
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          200..281
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          308..471
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          617..876
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          877..944
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          363..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          904..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          32..59
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        576..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         646
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   944 AA;  104240 MW;  746669E123D6E094 CRC64;
     MASDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLRREIRKEL KLKEGAENLR
     RATTDLGRSL GPVELVLRGS SRRLDLLHQQ LQELHAHVVL PDPAATAHDA PQSPGAGGPT
     CSATNLSLVA GLEKQLAIEL KVKQGAENMI QTYSNGSTKD RKLLLTAQQM LQDSKTKIDI
     IRMQLRRALQ ACQLESQAAP DEAQGSPDLG AVELRIEELR HHFRVEHAVA EGAKNVLRLL
     SAPKTPDRKA LSEAQEKLTE SNQKLGLLRE ALERRLGELP ADHPKGRLLR EELAAATSAA
     FSARLAGPFP ATHYSTLCKP APLTGTLEVR VVGCRDLPET IPWNPSPSVG GPGTPESRTP
     FLSRPARGLY SRSGSLSGRS SLKAEAENTS EVSTVLKLDN TVVGQTSWKP CGPNTWDQSF
     TLELERAREL ELAVFWRDQR GLCALKFLKL EDFLDNERHE VQLDMEPQGC LVAEVTFRNP
     VIERIPRLRR QKKIFSKQQG KAFQRARQMN IDVATWVRLL RRLIPNPSAI GTFSPGASPG
     PEARSTGDIS VEKLNLGTDL DGSPQKSPLG PPSSPSSLSS PIQETSTTPQ LPSETQETPG
     PTLCSPLRKS PLTLEDFKFL AVLGRGHFGK VLLSEFRPSG ELFAIKALKK GDIVARDEVE
     SLMCEKRILA AVTSAGHPFL VNLFGCFQTP EHVCFVMEYS AGGDLMLHIH SDVFSEPRAV
     FYSACVVLGL QFLHEHKIVY RDLKLDNLLL DTEGYVKIAD FGLCKEGMGY GDRTSTFCGT
     PEFLAPEVLT DTSYTRAVDW WGLGVLLYEM LVGESPFPGD DEEEVFDSIV NDEVRYPRFL
     SAEAISIMRR LLRRNPERRL GSSERDAEDV KKQPFFRTLG WDALLARRLP PPFVPTLSGR
     TDVSNFDEEF TGESPTLSPP RDARPLTATE QAAFRDFDFV AGSC
//
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