GenomeNet

Database: UniProt
Entry: G1P6R8_MYOLU
LinkDB: G1P6R8_MYOLU
Original site: G1P6R8_MYOLU 
ID   G1P6R8_MYOLU            Unreviewed;       862 AA.
AC   G1P6R8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=STK10 {ECO:0000313|Ensembl:ENSMLUP00000005774.2};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000005774.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000005774.2, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000005774.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; AAPE02049062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02049063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02049064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02049065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1P6R8; -.
DR   Ensembl; ENSMLUT00000006322.2; ENSMLUP00000005774.2; ENSMLUG00000006311.2.
DR   GeneTree; ENSGT00940000156818; -.
DR   HOGENOM; CLU_001965_3_0_1; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR022165; PKK.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46538:SF2; SERINE_THREONINE-PROTEIN KINASE 10; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF12474; PKK; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..240
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          107..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          835..862
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          466..610
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        233..252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..271
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        272..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..756
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   862 AA;  99651 MW;  0BB88B05CB744C2A CRC64;
     LQIMIEFCPG GAVDAIMLEL DRGLTEPQIQ VVCRQMLEAL HFLHGKKIIH RDLKAGNVLM
     TLEGDIRLAD FGVSAKNLKT LQKRDSFIGT PYWEDTEGFL CEQHPEAARA RPARRPRSGV
     STCGMSREEP GGLARSRKIN TMQTDRPPSP PRIASAPLRP RSFRHTQDFL SFLWVSLCLP
     SSPQPRQHPF VSGVTSNKAL RELVAEAKAE VMEEIEDGRE EGEEEDSVDA TSPLGDHTRT
     SSEVSQVSLD ANKPLQEPPV TPVPPSQPQD RENGPSLPSG DSSLQTTKPP DVAAGNENGL
     AVPVPLRKSR PVSMGASIQV PEEKQGADQA GDLSPTANRP RKTSQSRPVS SALETLGSEK
     LANGSLELPA PASPSKRDSD CGSLSTSESM DYSTSLSADL SLNRETGSLS IKDSRLHNKT
     LKRTRKFVVD GVEVSITTSK IISEDEKKDE EMRFLRRQEL RELRLLQKEE HRNQNQLSRK
     HELQLEQMHK RFEQEINAKK KFFDTELENL ERQQKQQVEK MEQDHAVRRR DEAKRIRLEQ
     ERDYTRFQEQ LKLMKKEVKN EVEKLPRQQR KESMKQKMEE HAQKKQHLDR DFLAKQKEDL
     ELAMKKITAD NRREICDKER ECLTRKQELL RDREAALWDM EEHHLQERHQ LVKQQLKDQY
     FLQRHELVRK HEKEREQMQR YNQRMVEQLK VRQQQEKARL PKIQRSEGKT RMAMYKKSLH
     ISGAGSAAEQ REKIKQFSQQ EEKRQKAERL QQQQKHENQM RDMAAQCESN MSELQQLQNE
     KCHLLVEHET QKLKALDESH NQNLKEWRDR LRPRKKALEE DLNQKKREQE MFFKLNEETE
     CPNPTTPNKA TKFFPYSSAD AS
//
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