ID   SN1L2_MOUSE    STANDARD;      PRT;   931 AA.
AC   Q8CFH6;
DT   01-MAY-2005 (Rel. 47, Created)
DT   01-MAY-2005 (Rel. 47, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Serine/threonine-protein kinase SNF1-like kinase 2 (EC 2.7.1.37) (Salt
DE   inducible kinase 2).
GN   Name=Snf1lk2; Synonyms=Sik2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF LYS-49.
RC   TISSUE=Adipose tissue;
RX   MEDLINE=22625648; PubMed=12624099; DOI=10.1074/jbc.M211770200;
RA   Horike N., Takemori H., Katoh Y., Doi J., Min L., Asano T., Sun X.J.,
RA   Yamamoto H., Kasayama S., Muraoka M., Nonaka Y., Okamoto M.;
RT   "Adipose-specific expression, phosphorylation of Ser794 in insulin
RT   receptor substrate-1, and activation in diabetic animals of salt-
RT   inducible kinase-2.";
RL   J. Biol. Chem. 278:18440-18447(2003).
CC   -!- FUNCTION: Phosphorylates Ser-789 of IRS1 in insulin-stimulated
CC       adipocytes, potentially modulating the efficiency of insulin
CC       signal transduction.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Activated by phosphorylation on Thr-175 by
CC       STK11 in complex with STE20-related adapter-alpha (STRAD alpha)
CC       pseudo kinase and CAB39 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic.
CC   -!- TISSUE SPECIFICITY: Present in both white and brown adipose
CC       tissues with levels increasing during adipocyte differentiation.
CC       Lower levels observed in the testis.
CC   -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. SNF1
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 UBA domain.
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DR   EMBL; AB067780; BAC53845.1; -.
DR   HSSP; P49137; 1NY3.
DR   Ensembl; ENSMUSG00000037112; Mus musculus.
DR   MGD; MGI:2445031; Sik2.
DR   GO; GO:0005634; C:nucleus; IDA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IDA.
DR   InterPro; IPR000719; Prot_kinase.
DR   InterPro; IPR008271; Ser_thr_pkin_AS.
DR   InterPro; IPR002290; Ser_thr_pkinase.
DR   InterPro; IPR000449; UBA.
DR   Pfam; PF00069; Pkinase; 1.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Phosphorylation;
KW   Serine/threonine-protein kinase; Transferase.
FT   DOMAIN       20    271       Protein kinase.
FT   DOMAIN      295    335       UBA.
FT   NP_BIND      26     34       ATP (By similarity).
FT   BINDING      49     49       ATP.
FT   ACT_SITE    142    142       Proton acceptor (By similarity).
FT   MOD_RES     175    175       Phosphothreonine (By similarity).
FT   MUTAGEN      49     49       K->M: Loss of kinase activity.
SQ   SEQUENCE   931 AA;  104198 MW;  5CF2FB8DCDC689F4 CRC64;
     MVMADGPRHL QRGPVRVGFY DIEGTLGKGN FAVVKLGRHR TTKTEVAIKI IDKSQLDAVN
     LEKIYREVQI MKMLDHPHII KLYQVMETKS MLYLVTEYAK NGEIFDYLAN HGRLNESEAR
     RKFWQILSAV DYCHGRKVVH RDLKAENLLL DNNMNIKIAD FGFGNFFKTG ELLATWCGSP
     PYAAPEVFEG QQYEGPQLDI WSMGVVLYVL VCGALPFDGP TLPILRQRVL EGRFRIPYFM
     SEDCEHLIRR MLVLDPSKRL SIAQIKEHKW MLIEVPVQRP ILYPQEQENE PSIGEFNEQV
     LRLMHSLGID QQKTVESLQN KSYNHFAAIY FLLVERLKSH RSSFPVEQRL DGRQRRPSTI
     AEQTVAKAQT VGLPVTLHPP NVRLMRSTLL PQASNVEAFS FPTSSCQAEA AFMEEECVDT
     PKVNGCLLDP VPPVLVRKGC QSLPSSMMET SIDEGLETEG EAEEDPSQAF EAFQATRSGQ
     RRHTLSEVTN QLVVMPGAGK MFSMSDNPSL ESVDSEYDMG SAQRDLNFLE DSPSLKDIML
     ANQPSPRMTS PFISLRPANP AMQALSSQKR EAHNRSPVSF REGRRASDTS LTQGIVAFRQ
     HLQNLARTKG ILELNKVQLL YEQMGSNADP TLTSTAPQLQ DLSSSCPQEE ISQQQESVSS
     LSASMHPQLS PQQSLETQYL QHRLQKPNLL PKAQSPCPVY CKEPPRSLEQ QLQEHRLQQK
     RLFLQKQSQL QAYFNQMQIA ESSYPGPSQQ LALPHQETPL TSQQPPSFSL TQALSPVLEP
     SSEQMQFSSF LSQYPEMQLQ PLPSTPGPRA PPPLPSQLQQ HQQPPPPPPP PPPQQPGAAP
     TSLQFSYQTC ELPSTTSSVP NYPASCHYPV DGAQQSNLTG ADCPRSSGLQ DTASSYDPLA
     LSELPGLFDC EMVEAVDPQH NGVVSCLARE T
//