ID   D6RH37_MOUSE            Unreviewed;       796 AA.
AC   D6RH37;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   SubName: Full=Protein kinase N1 {ECO:0000313|Ensembl:ENSMUSP00000115054.2};
GN   Name=Pkn1 {ECO:0000313|Ensembl:ENSMUSP00000115054.2,
GN   ECO:0000313|MGI:MGI:108022};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000115054.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000115054.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000115054.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000115054.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000115054.2};
RG   Ensembl;
RL   Submitted (NOV-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}.
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DR   AlphaFoldDB; D6RH37; -.
DR   SMR; D6RH37; -.
DR   IntAct; D6RH37; 1.
DR   MaxQB; D6RH37; -.
DR   PeptideAtlas; D6RH37; -.
DR   ProteomicsDB; 346839; -.
DR   Antibodypedia; 1296; 301 antibodies from 34 providers.
DR   Ensembl; ENSMUST00000132945.8; ENSMUSP00000115054.2; ENSMUSG00000057672.17.
DR   AGR; MGI:108022; -.
DR   MGI; MGI:108022; Pkn1.
DR   VEuPathDB; HostDB:ENSMUSG00000057672; -.
DR   GeneTree; ENSGT00940000154990; -.
DR   ChiTaRS; Pkn1; mouse.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000057672; Expressed in granulocyte and 231 other cell types or tissues.
DR   ExpressionAtlas; D6RH37; baseline and differential.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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: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   Gene3D; 1.10.287.160; HR1 repeat; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR037317; PKN1_HR1_2.
DR   InterPro; IPR037313; PKN_HR1_1.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR24356:SF246; SERINE_THREONINE-PROTEIN KINASE N1; 1.
DR   Pfam; PF02185; HR1; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00742; Hr1; 3.
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; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS51860; REM_1; 3.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Proteomics identification {ECO:0007829|EPD:D6RH37,
KW   ECO:0007829|MaxQB:D6RH37};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          37..112
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          126..205
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          214..295
FT                   /note="REM-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51860"
FT   DOMAIN          322..485
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          631..796
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          357..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          44..71
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        570..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         660
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   796 AA;  87195 MW;  F772A7521BB81523 CRC64;
     MACRPCRGAG RIWCCRSHKS EPRSWSLLEQ LGLAGADLAA PGVQQQLELE RERLKREIRK
     ELKLKEGAEN LRRATTDLGR SLAPVELLLR GSARRLDLLH QQLQELHAHV VLPDPAAGSD
     ATQSLAEGSP ICSSTNLSRV AGLEKQLAIE LKVKQGAENM IQTYSNGSSK DRKLLLTAQQ
     MLQDSKTKID IIRMQLRRAL QALQAGELES QAAPDEAQGD PELGAVELRI EELRHHFRVE
     HAVAEGAKNV LRLLSGAKAP DRKAVSEAQE KLTESNQKLG LLRESLERRL GELPADHPKG
     RLLREELTAA SSSAFSAILP GPFPATHYST LSKPAPLTGT LEVRVVGCKN LPETIPWSPP
     PSVGASGTPE SRTPFLSRPA RGLYSRSGSL SGRSSLRGEA ENATEVSTVL KLDNTVVGQT
     AWKPCGPNAW DQSFTLELER ARELELAVFW RDQRGLCALK FLKLEDFLDN ERHEVQLDME
     PQGCLVAEVT FRNPIIERIP RLQRQKKIFS KQQGKAFQRA RQMNIDVATW VRLLRRLIPS
     AVATGTFSPN ASPGAEIRHT GDISMEKLNL GADSDSSSQK SPPGLPSTSC SLSSPTHEST
     TSPELPSETQ ETPGPGLCSP LRKSPLTLED FKFLAVLGRG HFGKVLLSEF RSSGELFAIK
     ALKKGDIVAR DEVESLMCEK RILAAVTRAG HPFLVNLFGC FQTPEHVCFV MEYSAGGDLM
     LHIHSDVFSE PRAVFYSACV VLGLQFLHEH KIVYRDGLWG PDQHVLRNSG VPGAGSAHRH
     ILHASSGLVG TGRAAL
//