UniProt: W5MUI1

Database: UniProt
Entry: W5MUI1_LEPOC

LinkDB:  W5MUI1_LEPOC 
Original site:  W5MUI1_LEPOC

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
DNA sequence (4)   
   EMBL (4)   
Protein domain (34)   
   InterPro (14)   
   Pfam (6)   
   PROSITE (9)   
   SMART (5)   
All databases (51)   

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ID   W5MUI1_LEPOC            Unreviewed;      1628 AA.
AC   W5MUI1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000012040.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000012040.1}
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};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC       {ECO:0000256|ARBA:ARBA00004510}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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DR   EMBL; AHAT01003829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01003830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01003831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01003832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7918.ENSLOCP00000012040; -.
DR   Ensembl; ENSLOCT00000012061.1; ENSLOCP00000012040.1; ENSLOCG00000009847.1.
DR   eggNOG; KOG0612; Eukaryota.
DR   GeneTree; ENSGT01030000234517; -.
DR   HOGENOM; CLU_000288_140_3_1; -.
DR   InParanoid; W5MUI1; -.
DR   OMA; CGRSHHV; -.
DR   Proteomes; UP000018468; Linkage group LG7.
DR   Bgee; ENSLOCG00000009847; Expressed in camera-type eye and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00132; CRIB; 1.
DR   CDD; cd01243; PH_MRCK; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR031597; KELK.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR   PANTHER; PTHR22988:SF34; SERINE_THREONINE-PROTEIN KINASE MRCK BETA; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF08826; DMPK_coil; 1.
DR   Pfam; PF15796; KELK; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          18..284
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          285..355
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          1014..1064
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1084..1229
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1255..1528
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   DOMAIN          1604..1617
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   REGION          861..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          373..572
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1628 AA;  184114 MW;  1B62D172FF829685 CRC64;
     VKPFTTVVKE MRLHRDDFEM LKVIGRGAFG EVAVVKMKHT ERVYAMKILN KWEMLKRAET
     ACFREERNVL VNGDCQWITT LHYAFQDDNY LYLVMDYYVG GDLLTLLSKF EDRLPEDMAK
     FYLAEMVLAI HSIHQQHYVH RDIKPDNVLL DMNGHIRLAD FGSCLKMMED GTVQSSVAVG
     TPDYISPEIL QAMEDGMGKY GPECDWWSLG VCMYEMLYGE TPFYAESLVE TYGKIMNHEE
     RFQFPSHITD VSEDAKDLIQ RLICSRERRL GQNGIEDFKK HPFFSGIEWD NIRSTEAPYI
     PDVSSPSDTS NFDVDDDVLK NPDIVPPVSH TGFSGLHLPF VGFTYTTDSC FSDRGSLKRV
     LLSGGLDSDV QRDVENSLQV EAYERRIKRL EQEKLELSRK LQESTQAVQT LHGSGRGLGT
     ANRDKEIKKL NEEIERLKKK LADSDRLEHQ LEEAVTLRQE YETSSTKLKA LEKQVRALRQ
     EKEEIHKPCQ LKAQQLVESL ERQKSQTKEL KDAHQQRKLA MQEFSELNER MAELRSQKQK
     LSRQLRDKEE EMEVVMQKIE SMRQEIRKTE KARKEVTPKS SSRWVVSLQV MSAPERLTSA
     QSKNLKHASP ALLQLCTFVD KLTAQNRQLE DELQDLAAKK ESVAHWEAQI AEIIQWYCFQ
     LRRDCFLTGL KRSLNSISKV CSAGRRACCV TPVHVMPPPP HRVSDEKDAR GYLQALASKM
     TEELESLRNS SLGSRPLPAS TGMKEPPLPM SSLSLKWFSF FFELSPEAAN ILISLRFSAD
     SRVMDFITPN ISQPFHIMSS LKDPLWKVRR SQKLDMSARL ELQSALDAEI RAKQLVQEEL
     RKVKAANISL ESKLKESEVK NREMAEQVDN MKRDLEESRS RSDKGLKLPD FQESIFEYFN
     TSPFAQDLTF RTQLSLGEKL GNTASSVKSF PAFSPICFLE SSLRHCSSHN CFAHSASTDP
     LTRAYIWTTN TSVRGVGSMK RGRNPFLMEI ARSKLFLALN RVKNNRKPAL SPKAHQLSIK
     TFSSPAQCTH CTSLMVGLIR QGYACEVCSF ICHVTCKDHA PQVCPIPPEQ AKRPLGIDVQ
     RGIGTAYKGF VRIPKPTGVK KGWQRAYAVV CDCKLFLYDV PEGKSTQPGV VASQVLDLRD
     EEFSVSSVLA SDVIHATRKD VPCIFSVVVL RCLGLMLLMT GLSIPPSHCP PQVTSSLLSS
     PPRTCSLLIL AESETEKRKW VGILEGLQSI LNKNRLKNRV VHVLQEAYDS TLPAIKSTLS
     AAIIDRERIA LGTEEGLYVV EVTRDVIVRA ADCKKVHQIE LIPKEKIVVL LCGRNRHVHL
     HPWAALDGAE TNFDIKLPET KGCQALTTGI LRQGGPPCLL VAVKRQVLCY EIYRTKPYHK
     RVWEVQAPGV VQWLGQLWER LCVGYPSGFS LLSVQGEAPP VGLVSPSDPS LSFLSQQPLD
     ALHALEVGSG EALLCFSQLG VYVDTQGRRS RTQELMWPAT PLACSSSSSY LTVYSDYGID
     VFDVNTLEWV QTVSLRKIRP LNVEGTLNLL GSEQPRLIFF SNSSSSESQL CSVTTEVADL
     AIPETSDNSR KLMVRTRSKR KFLFKVPEEE REMLRDPELR SKMISNPTNF NHVAHMGPGD
     GMQVLMDL
//

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