ID Q803H3_DANRE Unreviewed; 463 AA.
AC Q803H3; B2GS18;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 158.
DE SubName: Full=Serine/threonine kinase 38-like {ECO:0000313|EMBL:AAH44485.1, ECO:0000313|Ensembl:ENSDARP00000149642};
DE SubName: Full=Serine/threonine-protein kinase 38-like {ECO:0000313|RefSeq:NP_957276.1};
DE EC=2.7.11.1 {ECO:0000313|RefSeq:NP_957276.1};
DE SubName: Full=Stk38l protein {ECO:0000313|EMBL:AAI65343.1};
GN Name=stk38l {ECO:0000313|EMBL:AAI65343.1,
GN ECO:0000313|Ensembl:ENSDARP00000149642,
GN ECO:0000313|ZFIN:ZDB-GENE-040426-798};
GN Synonyms=zgc:55777 {ECO:0000313|RefSeq:NP_957276.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI65343.1};
RN [1] {ECO:0000313|RefSeq:NP_957276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AB {ECO:0000313|RefSeq:NP_957276.1};
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.D., Sun X.J., Deng M., Zhang G.W., Zhou Y., Wu X.Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.L., Fan H.Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2] {ECO:0000313|EMBL:AAI65343.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB {ECO:0000313|EMBL:AAH44485.1};
RC TISSUE=PCR rescue {ECO:0000313|EMBL:AAI65343.1}, and Whole body
RC {ECO:0000313|EMBL:AAH44485.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSDARP00000149642, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000149642};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4] {ECO:0000313|RefSeq:NP_957276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AB {ECO:0000313|RefSeq:NP_957276.1};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [5] {ECO:0000313|RefSeq:NP_957276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AB {ECO:0000313|RefSeq:NP_957276.1};
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [6] {ECO:0000313|RefSeq:NP_957276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AB {ECO:0000313|RefSeq:NP_957276.1};
RX PubMed=27935819; DOI=10.1242/dmm.026500;
RA Mayrhofer M., Gourain V., Reischl M., Affaticati P., Jenett A., Joly J.S.,
RA Benelli M., Demichelis F., Poliani P.L., Sieger D., Mione M.;
RT "A novel brain tumour model in zebrafish reveals the role of YAP activation
RT in MAPK- and PI3K-induced malignant growth.";
RL Dis. Model. Mech. 10:15-28(2017).
RN [7] {ECO:0000313|RefSeq:NP_957276.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AB {ECO:0000313|RefSeq:NP_957276.1};
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [8] {ECO:0000313|Ensembl:ENSDARP00000149642}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000149642};
RG Ensembl;
RL Submitted (APR-2018) to UniProtKB.
RN [9] {ECO:0000313|RefSeq:NP_957276.1}
RP IDENTIFICATION.
RC STRAIN=AB {ECO:0000313|RefSeq:NP_957276.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC {ECO:0000256|RuleBase:RU000304}.
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DR EMBL; BX649380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX855588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044485; AAH44485.1; -; mRNA.
DR EMBL; BC165343; AAI65343.1; -; mRNA.
DR RefSeq; NP_957276.1; NM_200982.1.
DR Ensembl; ENSDART00000193353.1; ENSDARP00000149642.1; ENSDARG00000045482.6.
DR Ensembl; ENSDART00000193655.1; ENSDARP00000149794.1; ENSDARG00000045482.6.
DR GeneID; 393957; -.
DR KEGG; dre:393957; -.
DR AGR; ZFIN:ZDB-GENE-040426-798; -.
DR CTD; 23012; -.
DR ZFIN; ZDB-GENE-040426-798; stk38l.
DR OrthoDB; 988261at2759; -.
DR Proteomes; UP000000437; Chromosome 4.
DR Bgee; ENSDARG00000045482; Expressed in blastula and 34 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05627; STKc_NDR2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF160; SERINE_THREONINE-PROTEIN KINASE 38-LIKE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AAH44485.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 90..383
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 384..452
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 463 AA; 53810 MW; A8FB353E2A035D3C CRC64;
MAMTGGMAAP LPMSNHTRER VTVAKLTLEH FYSTLLTQHE EREMRQKKLE KVMDEEGLPD
EEKSMRRSLH ARKETEFLRL KRTRLGLDDF ESLKVIGRGA FGEVRLVQKK DTGHIYAMKI
LRKADMLEKE QVAHIRAERD ILVEADGAWV VKMFYSFQDK RNLYLIMEFL PGGDMMTLLM
KKDTLSEEAT QFYIAETVLA IDSIHQLGFI HRDIKPDNLL LDSRGHVKLS DFGLCTGLKK
AHRTEFYRNL THNPPSDFSF QNMNSKRKAE TWKKNRRQLA YSTVGTPDYI APEVFMQTGY
NKLCDWWSLG VIMYEMLIGY PPFCSETPQE TYRKVMNWRE TLTFPPEVPI SERAKELILR
YCTDAENRIG SGSVDEIKSH PFFESVDWEH IRERPAAISI DIKSIDDTSN FDDFPESDIL
QPANVTESDF KSKDWVFLNY TYKRFEGLTQ RGTIPTYMKA GKA
//
