ST32A_MOUSE
ID ST32A_MOUSE Reviewed; 398 AA.
AC Q8BGW6; Q7TPQ4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Serine/threonine-protein kinase 32A;
DE EC=2.7.11.1;
GN Name=Stk32a {ECO:0000312|MGI:MGI:2442403};
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC29366.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29366.1};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC29366.1}, and
RC Retina {ECO:0000312|EMBL:BAC31941.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH55002.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Olfactory epithelium {ECO:0000312|EMBL:AAH55002.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q60592};
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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q60592};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q60592};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q8WU08}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8BGW6-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q8BGW6-2; Sequence=VSP_051996;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AK036266; BAC29366.1; -; mRNA.
DR EMBL; AK042599; BAC31302.1; -; mRNA.
DR EMBL; AK044474; BAC31941.1; -; mRNA.
DR EMBL; BC055002; AAH55002.1; -; mRNA.
DR CCDS; CCDS29218.1; -. [Q8BGW6-1]
DR RefSeq; NP_848864.1; NM_178749.3. [Q8BGW6-1]
DR AlphaFoldDB; Q8BGW6; -.
DR SMR; Q8BGW6; -.
DR STRING; 10090.ENSMUSP00000038471; -.
DR iPTMnet; Q8BGW6; -.
DR PhosphoSitePlus; Q8BGW6; -.
DR MaxQB; Q8BGW6; -.
DR PaxDb; Q8BGW6; -.
DR PeptideAtlas; Q8BGW6; -.
DR PRIDE; Q8BGW6; -.
DR ProteomicsDB; 257429; -. [Q8BGW6-1]
DR ProteomicsDB; 257430; -. [Q8BGW6-2]
DR Antibodypedia; 27607; 235 antibodies from 27 providers.
DR DNASU; 269019; -.
DR Ensembl; ENSMUST00000045477; ENSMUSP00000038471; ENSMUSG00000039954. [Q8BGW6-1]
DR Ensembl; ENSMUST00000237797; ENSMUSP00000158482; ENSMUSG00000039954. [Q8BGW6-2]
DR GeneID; 269019; -.
DR KEGG; mmu:269019; -.
DR UCSC; uc008eue.1; mouse. [Q8BGW6-1]
DR UCSC; uc012bcj.1; mouse. [Q8BGW6-2]
DR CTD; 202374; -.
DR MGI; MGI:2442403; Stk32a.
DR VEuPathDB; HostDB:ENSMUSG00000039954; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000158185; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; Q8BGW6; -.
DR OMA; MRITTMA; -.
DR OrthoDB; 668916at2759; -.
DR PhylomeDB; Q8BGW6; -.
DR TreeFam; TF313395; -.
DR BioGRID-ORCS; 269019; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Stk32a; mouse.
DR PRO; PR:Q8BGW6; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8BGW6; protein.
DR Bgee; ENSMUSG00000039954; Expressed in caudate-putamen and 100 other tissues.
DR ExpressionAtlas; Q8BGW6; baseline and differential.
DR Genevisible; Q8BGW6; MM.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell membrane; Kinase; Lipoprotein;
KW Magnesium; Membrane; Metal-binding; Myristate; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..398
FT /note="Serine/threonine-protein kinase 32A"
FT /id="PRO_0000232412"
FT DOMAIN 23..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 379..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 29..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q60592,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q8WU08"
FT VAR_SEQ 158..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051996"
SQ SEQUENCE 398 AA; 46509 MW; 689BCA5B25CF18BB CRC64;
MGANTSSKAP VFDENEDVNF DHFEILRAIG KGSFGKVCIV RKNDTKKMYA MKYMNKQKCV
ERNEVRNVFK ELQIMQGLEH PFLVNLWYSF QDEEDMFMVV DLLLGGDLRY HLQQNVHFQE
DTVKLFICEL AMALDYLQSQ RIIHRDMKPD NILLDEHGHV HITDFNIAAM LPKETRITTV
AGTKPYMAPE MFTSRKETGY SFAVDWWSLG VTAYELLRGR RPYHIRSSTS SKEIVNMFET
AIVTYPSAWS QEMVSLLKKL LEPNPDQRFS HLTDIQNFPY MSDMNWDAVL QKRLIPGFIP
TKGRLNCDPT FELEEMILES KPLHKKKKRL AKREKEMKKS DSSQTCLLQE HLDAVQKEFI
IFNREKVKSD FNQRQANLAL EQTKNNTEEE EDGQNNNL
