ID   SPEG_DANRE              Reviewed;        2995 AA.
AC   Q696W0;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Striated muscle preferentially expressed protein kinase;
DE            EC=2.7.11.1;
GN   Name=speg; Synonyms=apeg1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=15185077; DOI=10.1007/s00427-004-0413-5;
RA   Sutter S.B., Raeker M.O., Borisov A.B., Russell M.W.;
RT   "Orthologous relationship of obscurin and Unc-89: phylogeny of a novel
RT   family of tandem myosin light chain kinases.";
RL   Dev. Genes Evol. 214:352-359(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   -!- 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;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in striated muscle.
CC       {ECO:0000269|PubMed:15185077}.
CC   -!- PTM: May be autophosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; AY578914; AAT80902.1; -; mRNA.
DR   RefSeq; NP_001007110.1; NM_001007109.1.
DR   STRING; 7955.ENSDARP00000032236; -.
DR   PaxDb; Q696W0; -.
DR   PRIDE; Q696W0; -.
DR   GeneID; 570504; -.
DR   KEGG; dre:570504; -.
DR   CTD; 570504; -.
DR   ZFIN; ZDB-GENE-030131-3230; spega.
DR   eggNOG; KOG0613; Eukaryota.
DR   eggNOG; KOG4475; Eukaryota.
DR   InParanoid; Q696W0; -.
DR   OrthoDB; 12436at2759; -.
DR   PhylomeDB; Q696W0; -.
DR   Reactome; R-DRE-445355; Smooth Muscle Contraction.
DR   Reactome; R-DRE-5627123; RHO GTPases activate PAKs.
DR   PRO; PR:Q696W0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; NAS:ZFIN.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; ISS:ZFIN.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007517; P:muscle organ development; ISS:ZFIN.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.40.10; -; 9.
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; IPR015726; Ser/Thr_kin_striated-sp.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47633:SF3; PTHR47633:SF3; 3.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 6.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 7.
DR   SMART; SM00408; IGc2; 6.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF48726; SSF48726; 7.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   SUPFAM; SSF56112; SSF56112; 2.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 6.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Disulfide bond; Immunoglobulin domain; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..2995
FT                   /note="Striated muscle preferentially expressed protein
FT                   kinase"
FT                   /id="PRO_0000234340"
FT   DOMAIN          27..109
FT                   /note="Ig-like 1"
FT   DOMAIN          613..701
FT                   /note="Ig-like 2"
FT   DOMAIN          714..802
FT                   /note="Ig-like 3"
FT   DOMAIN          840..930
FT                   /note="Ig-like 4"
FT   DOMAIN          937..1035
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1135..1224
FT                   /note="Ig-like 5"
FT   DOMAIN          1255..1505
FT                   /note="Protein kinase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          2323..2413
FT                   /note="Ig-like 6"
FT   DOMAIN          2420..2513
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          2682..2934
FT                   /note="Protein kinase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          250..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          815..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1559..1582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1776..1839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2017..2058
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2163..2189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2211..2322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2574..2609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2648..2676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        384..409
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..834
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1777..1800
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1801..1821
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2017..2033
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2212..2227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2233..2252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2257..2288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2289..2309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1372
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        2801
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         1261..1269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         2688..2696
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         2711
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DISULFID        50..93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        639..691
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        861..912
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        2345..2397
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   2995 AA;  333684 MW;  7C0F6D54CB6BD34D CRC64;
     MRKVTEEKRH SSSMNSSTVE TSFIAAPPVF LRKLKWAAVA AGCDVRLRVC VGGNPRPTLH
     WYHNDDPLVI DHEDYDGLWI RDCQQADGGL YTCVAVNHLG EARTSAVLAV LDLEEDSNST
     EDESAEPHVS MEMKEQFMPP QGEAINSQPT GRGRAMLSHI PSDGLVVERE MRALGSRAPG
     LQEPLSPGRG QLDFKTSEAT PFVQTQPPHK AQASITKSDV DATIDSTATK IKGTKTAMNG
     AEVSIKSSKI TGSHQSGGLQ DPSSIQTPKV SQASSKILDR VRAFEEQSHN SNMPKVSSRL
     SWGFNRTSSC NSEDETCKAG KFQANTKSDV ALKRSFFKQK ASSLEEQSTY VQKNFQSKLS
     EELHRIKKLV GKSNIKKAFS MEQLTQTDKQ SSVSTESVPT QVIQKSEETG KHFTNLKAVP
     DAKERWTTLP KEQSSRLPKI NLADKTKQPE NETPPEMNEN QENNSKPTQL LDGQVLNEKV
     SFIPGQCSPM LPRTNVSRKW PKSPAQPMVK DGLVQAPQKP PRLLESISTP PTPFKMTIPT
     IVVENKPVDE ELDQKEGQIM RQNRDALDDF HTSVEKSIAE APMSELPRKD ALGTAGSELL
     QCIIKENTVA RAPAESLLII TRPMQDVKVK AGETALLECF IAGSQAVDVD WLANGKLIQP
     ALFDCKMQFD GHRCRLLFKS AHENDSGCYT CKLSTAKEEL ICTANLLVIP SKEPLFTRKL
     EVLEAIEGRS AQFDCKVSGC PPPEVTWTHC EKPLVESDNI HILNVNGHHS LLITHVNKES
     EGLYTAIAQN VHGKAASSAE LYVQEPRPAI STHMSRLEKM PSIPEEPEVP EGEVERRTMP
     DFIKPLSDLE VIEGKEAVLK CRVTGLPYPK ITWYHNGKKI ESTNDRKMTQ YRDVHSLVIQ
     SVCHDHSGVY KCVISNKVGK AACYAHLYVA VSLPEPPDGP PVIESVTGRM ILLSWKKPKN
     LDPSIDPASL MYVVQQQVLG STQWTTIASS LTDTSYTVTS LSKGVCYSFR VLSTTGKTLS
     KPSQPTDLVQ LVDRGEYFRK APVIIDKPDI VYAVENQPVT ITITINHVQA TCTWKRRGVV
     LVNKLGALEM TTPDDDQHAL HIAKVKSTDV GQLIFMANNQ YGSDLGTLQL VIAVPPIFET
     IMEDLDVCVG ETCHFAVVVD GKPDPDILWY KDGVLLAESS HLTFVYDDRE CSLVVLNAQP
     EDVGVYTCTA KNLAGSVSCK AELTVHTAQN VEEEEEQMED EATILRRMRM LTDYYDIHKE
     IGRGAFSYVK RVKHKNDQSF AAKFISVRAK KKTCALRELA LLAELDHKSI VRFHDAFEKR
     RVVIILTELC HEELLERITK RTTILESEVQ SIIRQLLEGI EYLHQNDIIH LDLKPENILM
     ADQKTDQIRI CDFGNALKVK PNEELYCKYG IPEFIAPEIV NQSPISKSTD IWPVGVITYL
     CLTGVSPFAG ENDRDTLLNI RNYNVAFEES MFKDLCREAK GFIIKVLVSN KLRPDATECL
     LHPWFKSLTK GKSINTTLHK QVLARRKWQC SLIRYGSKMV MRSISELLDD SSSHVSLAVP
     RNLKDGSPPP SSSSDSDEDI DELPFIPMPH TMMFSGSRMS LTEIHEVDDK VIRGSNESYK
     KNLNQLDDIP ESQIIAGQKN EDYLKNPKRT DNCLQRGSSV EVDQVASKTR RGLMRRGSSA
     DSALLLQITP EDNEIKDTTE DSQKHMKKAV SMELPHRSSS PKTAKLSKED YALKLDLMRQ
     RLLKGGTVNK NMSGLRGPLL ETLGVDDERR TSSLDRNFRN ARLNASGDSG TFNNDSSEET
     YQKPAFRKRS SLRDENSESI SLHRRSGAPL EIPSSSTGDH NVLKIKSTIL DENKANLPPL
     FPRDISSKPP TPVLENKQVS KEEANSDVLI MNSSRSAFNL EDTEIKVEEM KEQDSVPENM
     NKSTEFPLDI LPHDISSNYC SKLQANGKKA SFLTPLPTPV LKISQPNIQP TAGRPGVFAS
     AFSAHQPNLR SDIKNIDSEE IFEARFKKRE SSLAHGLKRL TRTKSEESSP VPQRKSDEVV
     YRPGPVGSPL EFGSTGLKEK SKSVQDLREV DKEVGLGLIG RFSMRARKLQ PIDKKEKKEI
     SDSVTNKRQL TWATRRSKSL DKKENFETNK ENLEKDTKKI AESPVLAVRR KFESNVSGIF
     DRVHSRSKDR KDKETKPHID AEAPNVEKQD MKKINDSPVL ALRKKFETKV SGISYRKQSQ
     SEGEGTKFEG QKTPLFSRHH RSQSDGLIHK KMDIPENQLP LQTTTISSKE TLNSSSSAHS
     IESSQTPETE IRSRWDRWGL SRGKRDRTPS NSRAPATPKE DFPPVFHIAL KDHVLLEGNP
     VTLSCLPAGS PEPKILWLKD KKPLKLCDGM NLEACPDGRQ LLMIMNISKK DAGIYECVAT
     NNLASVTTSC ILTLACIPNC PGTPEIRQIY NNTVLVQWKP SDTKVPCTYT IEKKFDGDDK
     WLTEATGVTD CFFNSSELPS GSTIRFRVAC VNKAGQSPYS NESDGVSIDT KVTPQHQPAK
     MKTHSPASFP AMTAAVATSA FSLSLPSVFS QSISPTPAQS ADVSNTFLEV QSSPKMSTPL
     DLPKPASSVN TMPPITQTQT VSPRSYTAPP SIGRSISPVP TYVPATCSLA PTPVSPSVIV
     VSSISPIGEG ASSPTPETPT GQAVSSTKSE TTLRQGVPQK PYSFLDEKAR GRFGVIRDCR
     ENATGKMFIA KIIPYDQQTK QTIIKEYEIL KSLRCERIMA LHEAYITPRY LVLITEYCSG
     KEILQNLIDR FCYSEDDVVG FIVQILQGLE YLHNCKILHL DIKPDNIMVT NLNVIKIIDF
     GSAQRFNPLS LQQCSRYLGT LEYMAPEMLK GDLVGPPADI WSLGVLSYIM LSGRHPFEDK
     DPQLTEAKIH EAKFDSTKLY PKVSQSASTF LKKILNSYPW CRPTIKDCLN HSWLHDSYLK
     KLRRQTLTFT TTRLKEFMGE HQRRCAESAT KHKVILRVYQ GGPSSPASPT KYTTQ