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
//