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Database: UniProt
Entry: A0A2Y9KB26_ENHLU
LinkDB: A0A2Y9KB26_ENHLU
Original site: A0A2Y9KB26_ENHLU 
ID   A0A2Y9KB26_ENHLU        Unreviewed;      1848 AA.
AC   A0A2Y9KB26;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Myosin light chain kinase, smooth muscle {ECO:0000256|ARBA:ARBA00021842};
DE            EC=2.7.11.18 {ECO:0000256|ARBA:ARBA00012430};
DE   AltName: Full=Telokin {ECO:0000256|ARBA:ARBA00030959};
GN   Name=LOC111154981 {ECO:0000313|RefSeq:XP_022370656.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022370656.1};
RN   [1] {ECO:0000313|RefSeq:XP_022370656.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022370656.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR   RefSeq; XP_022370656.1; XM_022514948.1.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004687; F:myosin light chain kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd20976; IgI_4_MYLK-like; 1.
DR   CDD; cd05762; IgI_8_hMLCK_like; 1.
DR   CDD; cd20973; IgI_telokin-like; 1.
DR   CDD; cd14191; STKc_MLCK1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR015725; MLCK1_kinase_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47633; IMMUNOGLOBULIN; 1.
DR   PANTHER; PTHR47633:SF4; KETN-1; 1.
DR   Pfam; PF16620; 23ISL; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 8.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00409; IG; 8.
DR   SMART; SM00408; IGc2; 8.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 8.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 8.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Kinase {ECO:0000313|RefSeq:XP_022370656.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000313|RefSeq:XP_022370656.1}.
FT   DOMAIN          33..122
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          161..249
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          445..530
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          548..642
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          652..739
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1032..1120
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1172..1260
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1268..1361
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1398..1653
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1743..1832
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          259..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1132..1171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1347..1380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1701..1721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..879
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        993..1010
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1032
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1701..1717
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1427
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1848 AA;  203052 MW;  EDCEF4C51F203818 CRC64;
     MGDVKLAAST QVSKASISVD HSRAGSVPLT EAPAFIVPPR NLCIREGATA KFEGRVRGYP
     EPHVTWHRNG QPITSGGRFL LDCGIRGAFS LVIHAVREED KGKYTCEATN DSGARQVTVE
     LMVEGGFMKK HGQPAVSKTL GDRFSAPAVE TRPSIWGECP PKFATKLGRA IVREGQMGRF
     SCKITGRPQP QVTWLKGEVP LQPSARVSMS EKNGVQVLEI HEVSRDDVGV YTCLVVNGSG
     KASMSAELSI QGLDNANRSL VRGTKAPSSD IRKEVTNGTT QGRKVDSLES AAERRNCSSA
     QRGSSLTWAP SSQPQPLQES QPEPSEDSSR KALRSPILQK TSSTITLQAA KVQPEPRALI
     SSTLSSSGEA REWPAAHPPA THPTRQTGLG SQEVVSKVAT KKIPIESQRD STFPKFESKP
     QSQEVSEDQT VKFRCEGLAA PEVAPSFSRV LKDCTVVEGQ DFVLRCSVQG TPVPQITWLL
     NEQPIQYAHS SCEAGVAELH IQDALPEDDG IYTCLAKNTM GQVSCSARVT VHEKKSDRKS
     GSLLPAAPSK PVAPVFLQGL SDLKVMDGSH VTMTVQVSGN PPPEVVWLHD GNEIQESEDF
     HFEQRGTQHS LCIQEVFPED TGTYTCEAWN SAGEVRTQAV LMVQEPQDGT QPWFISRPRS
     VTASLGQSVL ISCAIAGDPF PTVHWLRDGK ALSKDTGHFE VLQNEGVFTL VLKNVQPWHA
     GQYEILLKNQ VGECSCQVSL MLQSNPTRAP LGREPASCEG LCSPGAGADG GGRDCYGTLR
     PGWPARGQGW PEEEDGEDVR GLLKRRVETR QHTEEAIRQQ EVEQLDFRDL LGKKVSTKTV
     SEEDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ VDFRSVLAKK GTPKTPVPEK
     APPPKPATPD FRSVLGSKKK LPAENGSNSA EALNAKAAES PKAMSNAQPL GSLKPLGNAK
     PAETLKPTPK PMGNAKPAET PKPMGNAKPA ETPKPAGKEE LKKEVKNDVN CRRGQAAATD
     NENRSENQGT APTFKEKLQD VRVTEGEKLL LQCQVSSDPP ATITWTLNGK TLKTTKFIIL
     SQEGSLCSVS IEKALPEDRG LYKCIAKNGA GQAECSCQVT VDDAPTKENV KAPEMKARRP
     KSSLPPVLGT ESDATVKKKP APKTPPKAAM PPQIIQFPED QKVRAGESVE LFGKVAGTQP
     ITCTWMKFRK QIQESEHIKV ENSENGSRLT IVAARQEHCG CYTLLVENKL GSRQAQVNLT
     VVDKPDPPAG TPCASDIRSS SLTLSWYGSS YDGGSAVQSY SVEIWDSVDK TWKELATCRS
     TSFNVQDLLP DREYKFRVRA INVYGTSEPS QESELTAVGE KPEEPKDEVE ASDDDEKEPE
     IDYRNVTVNT EQKVSDFYDI EERLGSGKFG QVFRLVEKKT GKIWAGKFFK AYSAKEKENI
     RQEISIMNCL HHPKLVQCVD AFEEKANIVM VLEIVSGGEL FERIIDEDFE LTERECIQYM
     RQISEGVEYI HKQGIVHLDL KPENIMCVNK TGTRIKLIDF GLARKLENAG SLKVLFGTPE
     FVAPEVINYE PIGYATDMWS IGVICYILVS GLSPFMGDND NETLANVTSA TWDFDDEAFD
     EISDDAKDFI SNLLKKDMKN RLDCTQCLQH PWLMKDTKNM EAKKLSKDRM KKYMARRKWQ
     KTGNAVRAIG RLSSMAMISG LSGRKSSTGS PTSPLNAEKL ESEEDVSQAF LEAVAEEKPH
     VKPYFSKTIR DLEVVEGSAA RFDCKIEGYP DPEVVWFKDD QSIRESRHFQ IDYDEDGNCS
     LIISDVCGDD DAKYTCKAVN SLGEATCTAE LIVETMEEGE GEGEEEEE
//
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