CDK16_RAT
ID CDK16_RAT Reviewed; 496 AA.
AC Q63686; Q63687;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cyclin-dependent kinase 16;
DE EC=2.7.11.22;
DE AltName: Full=Cell division protein kinase 16;
DE AltName: Full=PCTAIRE-motif protein kinase 1;
DE AltName: Full=Serine/threonine-protein kinase PCTAIRE-1;
GN Name=Cdk16; Synonyms=Pctaire1, Pctk1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=New England Deaconess Hospital; TISSUE=Adrenal medulla;
RX PubMed=8918260; DOI=10.1016/0378-1119(96)83274-4;
RA Gao C.Y., Chauthaiwale V.M., Rampalli A.M., Zelenka P.S.;
RT "Expression of alternatively spliced PCTAIRE-1 mRNA in PC12 cells and
RT neonatal rat brain.";
RL Gene 176:243-247(1996).
RN [2]
RP IDENTIFICATION IN A COMPLEX WITH CDK17 AND TDRD7.
RX PubMed=10727952; DOI=10.1046/j.1432-1327.2000.01218.x;
RA Hirose T., Kawabuchi M., Tamaru T., Okumura N., Nagai K., Okada M.;
RT "Identification of tudor repeat associator with PCTAIRE 2 (Trap). A novel
RT protein that interacts with the N-terminal domain of PCTAIRE 2 in rat
RT brain.";
RL Eur. J. Biochem. 267:2113-2121(2000).
RN [3]
RP CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH NSF, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=16461345; DOI=10.1074/jbc.m513496200;
RA Liu Y., Cheng K., Gong K., Fu A.K., Ip N.Y.;
RT "Pctaire1 phosphorylates N-ethylmaleimide-sensitive fusion protein:
RT implications in the regulation of its hexamerization and exocytosis.";
RL J. Biol. Chem. 281:9852-9858(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-95; SER-110 AND
RP SER-155, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Protein kinase that plays a role in vesicle-mediated
CC transport processes and exocytosis. Can phosphorylate CCNY at 'Ser-336'
CC (in vitro) Plays a role in the regulation of insulin secretion in
CC response to changes in blood glucose levels. Regulates GH1 release by
CC brain neurons. Required for normal spermatogenesis. Regulates neuron
CC differentiation and dendrite development (By similarity).
CC Phosphorylates NSF, and thereby regulates NSF oligomerization.
CC {ECO:0000250, ECO:0000269|PubMed:16461345}.
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=2.7.11.22;
CC Evidence={ECO:0000269|PubMed:16461345};
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=2.7.11.22; Evidence={ECO:0000269|PubMed:16461345};
CC -!- SUBUNIT: Interacts with BRSK2. Interacts with CCNY; this increases the
CC CDK16 kinase activity (By similarity). Found in a complex containing
CC CABLES1, CDK17 and TDRD7. Interacts with YWHAH, YWHAQ and YWHAZ.
CC Interacts with NSF. Identified in a complex with NSF, syntaxin-1,
CC synaptotagmin, SYN1, SYP and CDK5R1. {ECO:0000250,
CC ECO:0000269|PubMed:10727952, ECO:0000269|PubMed:16461345}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC secretory vesicle {ECO:0000269|PubMed:16461345}. Synapse, synaptosome
CC {ECO:0000269|PubMed:16461345}. Note=Colocalizes with insulin in
CC pancreas islets. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PCTAIRE-1a;
CC IsoId=Q63686-1; Sequence=Displayed;
CC Name=2; Synonyms=PCTAIRE-1b;
CC IsoId=Q63686-2; Sequence=VSP_010639;
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level). Isoform 1 and
CC isoform 2 are expressed in brain, kidney, lung, heart and lens fiber.
CC {ECO:0000269|PubMed:16461345, ECO:0000269|PubMed:8918260}.
CC -!- PTM: Phosphorylation at Ser-153 inhibits kinase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; U36444; AAC52912.1; -; mRNA.
DR EMBL; U36444; AAC52913.1; -; mRNA.
DR PIR; JC5110; JC5110.
DR PIR; JC5111; JC5111.
DR RefSeq; NP_112339.1; NM_031077.1. [Q63686-2]
DR AlphaFoldDB; Q63686; -.
DR SMR; Q63686; -.
DR IntAct; Q63686; 1.
DR STRING; 10116.ENSRNOP00000060222; -.
DR iPTMnet; Q63686; -.
DR PhosphoSitePlus; Q63686; -.
DR jPOST; Q63686; -.
DR PaxDb; Q63686; -.
DR PRIDE; Q63686; -.
DR GeneID; 81741; -.
DR KEGG; rno:81741; -.
DR UCSC; RGD:620584; rat. [Q63686-1]
DR CTD; 5127; -.
DR RGD; 620584; Cdk16.
DR eggNOG; KOG0594; Eukaryota.
DR InParanoid; Q63686; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; Q63686; -.
DR PRO; PR:Q63686; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; ISS:UniProtKB.
DR GO; GO:0030252; P:growth hormone secretion; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Cytoplasmic vesicle;
KW Differentiation; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Spermatogenesis;
KW Synapse; Synaptosome; Transferase.
FT CHAIN 1..496
FT /note="Cyclin-dependent kinase 16"
FT /id="PRO_0000086486"
FT DOMAIN 165..446
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 171..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 12
FT /note="Phosphoserine; by BRSK2"
FT /evidence="ECO:0000250|UniProtKB:Q00536"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00536"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00536"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00536"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00536"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00536"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..64
FT /note="MDRMKKIKRQLSMTLRGGRGIDKTNGVPEQIGLDESGGGGGMTLGEAPTRVA
FT PGELRSIRGPLS -> MYTNGYDEEIYYIGGKRVFLTPKAWPFPH (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:8918260"
FT /id="VSP_010639"
SQ SEQUENCE 496 AA; 55765 MW; 8E77DB7551A84329 CRC64;
MDRMKKIKRQ LSMTLRGGRG IDKTNGVPEQ IGLDESGGGG GMTLGEAPTR VAPGELRSIR
GPLSSAPEIV HEDMKMGSDG ESDQASATSS DEVQSPVRVR MRNHPPRKIS TEDINKCLSL
PADIRLPEGY LEKLTLNSPI GDKPLSRRLR PVSLSEIGFG KLETYIKLDK LGEGTYATVY
KGKSKLTDNL VALKEIRLEH EEGAPCTAIR EVSLLKDLKH ANIVTLHDII HTEKSLTLVF
EYLDKDLKQY LDDCGNVINM HNVKLFLFQL LRGLAYCHRQ KVLHRDLKPQ NLLINERGEL
KLADFGLAYA KSIPTKTYSN EVVTLWYRPP DILLGSTDYS GQIDMWGVGC IFYEMATGRP
LFPGSTVEEQ LHFIFRILGT PTEDTWPGIL SNEEFRTYNY PKYRAEALLR HAPRLECDGA
DLLTKLLQFE GRNRISAEDA MKHPFFLSLG ERIHKLPDTT SIFALKEVQL QKEANIRSTS
MPDSGRPAFR VVDTEF
