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Database: UniProt
Entry: A0A096NG61_PAPAN
LinkDB: A0A096NG61_PAPAN
Original site: A0A096NG61_PAPAN 
ID   A0A096NG61_PAPAN        Unreviewed;      1914 AA.
AC   A0A096NG61;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   24-JAN-2024, entry version 54.
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=MYLK {ECO:0000313|Ensembl:ENSPANP00000011923.3};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000011923.3, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000011923.3, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000011923.3}
RP   IDENTIFICATION.
RG   Ensembl;
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   STRING; 9555.ENSPANP00000011923; -.
DR   Ensembl; ENSPANT00000008291.4; ENSPANP00000011923.3; ENSPANG00000023054.4.
DR   eggNOG; KOG0613; Eukaryota.
DR   GeneTree; ENSGT00940000157879; -.
DR   HOGENOM; CLU_000288_76_2_1; -.
DR   OMA; FKEGAPI; -.
DR   Proteomes; UP000028761; Chromosome 2.
DR   Bgee; ENSPANG00000023054; Expressed in fundus of stomach and 67 other cell types or tissues.
DR   ExpressionAtlas; A0A096NG61; baseline.
DR   GO; GO:0032154; C:cleavage furrow; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR   GO; GO:0001725; C:stress fiber; IEA:Ensembl.
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:Ensembl.
DR   GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; IEA:Ensembl.
DR   GO; GO:0032060; P:bleb assembly; IEA:Ensembl.
DR   GO; GO:0071476; P:cellular hypotonic response; IEA:Ensembl.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR   GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd20978; IgI_4_hemolin-like; 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; 10.
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; 9.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00409; IG; 9.
DR   SMART; SM00408; IGc2; 9.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 9.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 9.
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   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:UP000028761};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
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          414..503
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          514..599
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          620..711
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          721..808
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1098..1186
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1238..1326
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1334..1426
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1464..1719
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1809..1898
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          293..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          932..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1075..1098
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1193..1237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1413..1446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1767..1787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..949
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        995..1022
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1767..1783
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1493
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1914 AA;  210346 MW;  9D757F9D24416FF4 CRC64;
     MGDVKLVASS HISKTSLSVD PSRVGSMPLT EAPAFILPPR NLCIKEGATA KFEGRVRGYP
     EPQVTWHRNG QPITSGGRFL LDCGLRGTFS LVIHAVHEED RGKYTCEATN GSGARQVTVE
     LTVEGSFAKQ LGQPVVSKSL GDRFSASAVE TRPSIWGECP PKFATKLGRV VVKEGQMGRF
     SCKITGRPQP QVTWLKGNVP LQPSARVSMS EKNGMQVLEI HGVNQDDVGV YTCLVVNGSG
     KASMSAELSI QGLDSANRSF GRETKATNSD IRREVTNVIS KELKLNSLEA AAESKNCSSP
     QRGGSPAWAA NSQPQPPRES KLESCKDSPR TASQTPVLQT TSSSITLQAA RVQPEPRAPG
     LGALSPSGEE RKRPAAPRPA TFPTRQPGLG SQDVVSKAAT RRIPMEGQKD SALPKFESKP
     QSQEVRENQT VKFRCEVSGI PKPEVAWFLE GTPVRRQEGS IEVYEDAGSH YLCLLRARTR
     DSGTYSCTAS NARGQVSCSW TLQVERLAVI EVAPSFSSVL KDCTVIEGQD FVLQCSVRGT
     PVPQITWLLN GQPIQYAHST CEAGMAELHI QDALPEDHGT YTCLAENALG QVSCSARVTV
     HEKKSSGKSE YLLPVAPSKP TAPIFLQGLS DLKVMDGSQV TMTVQVSGNP PPEVIWLHNG
     NEIQESEDFH FEQRGTQHSL CIQEVFPEDT GTYTCEAWNS AGEVRTQAVL TVQEPHDGTQ
     PWFISKPRSV TASLGQSVLI SCAIAGDPFP TVHWLRDGKA LSKDTGHYEV LQNEDVFTLV
     LKKVQPWHAG RYEILLKNRV GECSCQVSLM LQNSPAGALP RGREPASCEG LCGGGVGADG
     GGSDRYGTLR PGWPARGQGW PEEEDGEDVR GVLKRRVETR QHTEEAIRQQ EVEQLDFRDL
     LGKKVSTKTL SEDDLKEIPA EQMDFRANLQ RQVKPKTVSE EERKVHSPQQ VDFRSVLAKK
     GTPKTPVPEK VPPPKPATPD FRSVLGGKKK LPAENGSSSA ETLNAKAVES SKPLSNAQPS
     GPLKPMGNAK PAETLKPMGN AKPAETLKPM GNTKPAETLK SASKEELKKD IKNDVNCKRG
     HAGTTDNEKR SESQGTAPVF KEKLQDVRVA EGEKLLLQCQ VSSDPPATVT WTLNGKTLKT
     TKFIVLSQEG SLCSVSIEKA LPEDRGLYKC VAKNDAGQAE CFCQVTVDDA PASENTKAPE
     MKSRRPKSSL PPVLGTESDA TVKKKPAPKT PPKAAMPPQI IQFPEDQKVR AGESVELLGK
     VTGTQPITCT WMKFRKQIQE SEHMKVENSE NGSKLTILAA RQEHCGCYTL LVENKLGSRQ
     AQVNLTVVDK PDPPAGTPCA SDIRSSSLTL SWYGSSYDGG SAVQSYSIEI WDSANKTWKE
     LATCRSTSFN VQDLLPDHEY KFRVRAINVY GTSEPSQESE LTTVGEKPEE PKDEVEVSDD
     DEKEPEVDYR TVTINTEQKV SDVYDIEERL GSGKFGQVFR LVEKKTRKIW AGKFFKAYSA
     KEKENIRQEI SIMNCLHHPK LVQCVDAFEE KANIVMVLEI VSGGELFERI IDEDFELTER
     ECIKYMRQIS EGVEYIHKQG IVHLDLKPEN IMCVNKTGTR IKLIDFGLAR RLENAGSLKV
     LFGTPEFVAP EVINYEPIGY ATDMWSIGVI CYILVSGLSP FMGDNDNETL ANVTSATWDF
     DDEAFDEISD DAKDFISNLL KKDMKNRLDC TQCLQHPWLM KDTKNMEAKK LSKDRMKKYM
     ARRKWQKTGN AVRAIGRLSS MAMISGLSGR KSSTGSPTSP LNAEKLESEE DVSQAFLEAV
     AEEKPHVKPY FSKTIRDLEV VEGSAARFDC KIEGYPDPEV VWFKDDQSIR ESRHFQIDYD
     EDGNCSLIIS DVCGDDDAKY TCKAVNSLGE ATCTAELIVE TMEEGEGEGE EEEE
//
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