ID I3MJ24_ICTTR Unreviewed; 3263 AA.
AC I3MJ24;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Striated muscle enriched protein kinase {ECO:0000313|Ensembl:ENSSTOP00000011105.3};
GN Name=SPEG {ECO:0000313|Ensembl:ENSSTOP00000011105.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000011105.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000011105.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR EMBL; AGTP01062695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01062696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 43179.ENSSTOP00000011105; -.
DR Ensembl; ENSSTOT00000012395.3; ENSSTOP00000011105.3; ENSSTOG00000012359.3.
DR eggNOG; KOG0032; Eukaryota.
DR eggNOG; KOG0613; Eukaryota.
DR GeneTree; ENSGT00940000161126; -.
DR HOGENOM; CLU_000381_0_0_1; -.
DR InParanoid; I3MJ24; -.
DR TreeFam; TF331962; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd20975; IgI_APEG-1_like; 1.
DR CDD; cd14108; STKc_SPEG_rpt1; 1.
DR CDD; cd14111; STKc_SPEG_rpt2; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 11.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
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 PANTHER; PTHR47633:SF7; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47633; IMMUNOGLOBULIN; 1.
DR Pfam; PF07679; I-set; 9.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF16650; SPEG_u2; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 9.
DR SMART; SM00408; IGc2; 9.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 9.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 8.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 47..128
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 729..817
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 876..965
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 970..1064
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1071..1159
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1195..1285
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1292..1389
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1492..1580
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1608..1861
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 2589..2679
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2686..2780
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2962..3214
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1915..1959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1985..2067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2081..2243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2262..2329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2342..2553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2760..2900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2911..2930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..690
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2184..2232
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2358..2377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2468..2487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2517..2546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2771..2788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2808..2822
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2823..2841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2853..2900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2913..2927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 3263 AA; 353902 MW; BC70AD6B83462DB4 CRC64;
MQKARGTRGE DVGTRAPPSP GVPPKRAKVG AGGGAPAAGA GAGAGAPVFL RPLKNAAVCA
GGDVRLRVVV SGTPQPSLSW FRDGQLLPAP VPEPSCLWLR SCGAQDAGVY SCRAQNERGR
ASCEAVLTVL EVGDSETAED DISDVQGTQR LELRDDGAFS TPTGGSDTLV GTSLDTPPTS
VTGTSEEQVS WWGSGQTVLE QEAGSGGGTR RLPGSPRQAQ ATGAGPRHLG VEPLVRASRA
NLVGASWGSE DSLSVASDLY GSAFSLYRGR ALSIHVSIPQ SGLRREEPDL QPQQASEAPR
PRPAPPPPSK SALLPPPSPR VGKRAPPGPS AQPPATPTSL HRRTQEPELP EDTTAEEKRG
KKSKSSGPSL AGTTESRPQT PLSEASGRLS ALGRSPRLVR AGSRILDKLQ FFEERRRSLE
RSDSPPAPLR PWVPLRKARS LEQPKSVGDA AWGIPGASQE ELQAPQGSVA ERRRLFQQKA
ASLDERTRQR SPASDLELRF AQELGRIRRS TSREELVRSH ESLRATLQRA PSPREPGEPP
LFSRPSTPKT PRAVSPAATQ PPPPSIVGKS VEEPGRPRSR GPLGRTEPGE GPQQEVRRRR
DQFPLTRGRA IQECRSPVPP HNADLPEAQT KAPSGRKREP PAQAVRFLPW ATPGLEGAAV
PQTLEKNRAG PEAEKRLRRG PEEDGPWGAW DRRGPRSQGK GRRVRPTSPE LESSDDSYVS
AGEEPLEAPV FEIPLQNAVV APGADVLLKC IITANPPPQV SWLKDGSTLH SEGRLLIRAE
GERHTLLLRE AQEADAGSYM ATAINELGQA SCAASLAVRP GGSTSPFSSP ITSDEEYLSP
PEEFPEPGET WPGTPTMQLS PSQNHRSSDA GSKAPPTFKV SLMDQSVREG QDVIMSIRVQ
GEPKPVVSWL RNRQPVRPDQ RRFAEEAEGG LCRLRILAAE RGDAGFYTCK AVNEYGARQC
EARLEVRAHP ESRSLAVLAP LQDVNVGAGE MALFECLVAG PADVEVDWLC RGRLLQPALL
KCKMHFDGRK CKLLLTSVHE DDSGVYTCKL STAKDELTCS ARLTVRPSLA PLFTRLLEDV
EVLEGRAARF DCKISGTPPP SVTWTHFGHP VEESENLRLR QEGGLHSLHI AHVGSEDEGL
YAVSATNTHG QANCSAQLYV EEPRTAASSP SSKLEKMPSI PEEPEQGELE RLSIPDFLRP
LQDLEVGLAK EAMLECQVTG LPYPTISWFH NGHRIQSSDD RRMTQYRDVH HLVFPAVGPQ
HAGVYKSVIA NKLGKAACYA HLYVTDVVPG PPDGAPQVVA VTGRMVTLTW NPPRSLDMAI
DPDSLTYTVQ HQVLGSDQWT ALATGLREPR WAATGLRKGL QHVFRVLSTT GKSSSKPSPP
SEPTQLLEHG PPLEEAPAVL DKPDIVYVVE GQPAHVTITF NHVEAQVVWR SCRGALLEAR
TGVYELSQPD DDQYSLRICR VSRRDVGSLT CTARNRHGTQ ACSVTLELAE APRFESIMED
VEVGAGETAR FAVVVEGKPL PDITWYKDEV LLAESSHVSF VYEENECSLV VLSTGTQDGG
VYTCTARNLA GEVSCKAELA VHSAQTAMEV EGVGEDGEHR GRRLSDFYDI HQEIGRGAFS
YLRRVVERSS GLEFAAKFIP SQAKPKASAR REARLLARLQ HDCIVYFHEA FERRRGLVIV
TELCTEELLE RMARKPTVCE SEIRAYMRQV LEGICYLHQS QVLHLDVKPE NLLVWDGADG
EEQVRICDFG NAQELTPGEP QYCQYGTPEF VAPEIVNQSP VSGVTDIWPV GVIAFLCLTG
ISPFVGENDR TTLMNIRNYN VAFEETTFLS LSREARGFLI KVLVQDQMRP TAEETLEHPW
FKTQAKGAEV STDHLKLFLS RRRWQRSQIS YKCHLVLRPI PELLRAPPER VWVAMPRRTP
PSGGLSSSSD SEEEELEELP TVPRPLQPEF SGSRVSLTDI PTEDEALGTP EAGAATPMDW
QELGRAPSQD QEVPSPQALP SPRQEPPAGS SPRRGELRRG SSAESALPRA GPREPGRGLH
KAASVELPQR RSPSPGATRL ARGGLGEGEY AQRLQALRQR LLRGGPEDGK VSGLRGPLLE
SLGGRARDPR MARAASSEAA PHHQPPPETR GLQKSSSFSQ GEAEPRGRHR RAGAPLEIPV
ARLGARRLQE SPSLSALSEA QPPSPARPSV PKPSIPKPKE PATATPGGSP QPSAPLPTPE
KAPEPTPEPG RASRPAQLPV ALQTPALPLT PYAQIMQSLQ LAGHAQPLQS PPSPSSEPKP
HAAVFARVAS PPPGVPEKRL PSPRAPPVLV EKARVPTVPP RPGSSLSSSI ENLESEAVFE
AKFKRSRESP LSRGLRLLSR SRSEERGPFR GAEDEDGMYR PSPAGTPLEL VRRPERSRSV
QDLRAVGEPG LVRRLSLSLS QKLRRTPPSQ RHPAWEARGG DGESSEGGSS ARGSPVLAVR
RRLSSTLERL SSRLQRSGSS EDSGGASGRS TPLFGRLRRA TSEGESLRRL GIPHNQLASQ
AGATTPSAES LGSEASATSG SSAPGESRSR LRWGFSRTRK DKGLSQPNLS ASIQEDLGHQ
YVPSESDFPP VFHIKLKDQV LLEGEAATLL CLPAACPAPR ISWMKDKQSL QSEPSVVIVS
CKDGRQLLSI PRAGKRHAGL YECSATNVLG SITSSCTVAV ARVPGKLAPP EVPQTYQDTA
LVLWKPGDSR APCTYTLERR VDGESTWHPV SSGIPDCYYN VTHLPIGVTV RFRVACANRA
GQGPFSNPSE KVLVRGTQDS SARPSAAHQD APVTSGPARA QPPDSPTSLT LTPAPPAPQS
ASFSPSAPLT PPSQAWSSLK AVGPPPQTPP RKHRGLQATQ QPEPTLPSAQ VTLSEPKSFV
PDTGTGTPTS TPQAVKPASS STPLYMVTSF VSAPPAPEPP APEPPPELTK VTVRSLSPGK
EVVSSPTPEG TTLRQGLPQK PYTFLEEKAR GRFGVVRACR ENATGRTFVA KIVPYAAEGK
RQVLQEYEVL RTLHHERLMS LHEAYITPRY LVLIAESCGN RELLCGLSDR FRYSEDDVAT
YVVQLLQGLD YLHGRHVLHL DIKPDNLLLA PDNTLKIVDF GSAQPYNPQA LRPLGHRTGT
LEFMAPEMVK GEPIGSATDI WGAGVLTYIM LSGHSPFYEP DPKETEARIV GGRFDAFQLY
PNTSQSATLF LRKVLSVHPW SRPSLQDCLA HPWLQDAYLM KLRRQTLTFT TNRLKEFLGE
QRRRRAEAAT HHKVLLRSYP GSP
//
