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Database: UniProt
Entry: A0A3B1IFX1_ASTMX
LinkDB: A0A3B1IFX1_ASTMX
Original site: A0A3B1IFX1_ASTMX 
ID   A0A3B1IFX1_ASTMX        Unreviewed;       802 AA.
AC   A0A3B1IFX1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=MARK4 {ECO:0000313|Ensembl:ENSAMXP00000028848.1};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000028848.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000028848.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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, dendrite
CC       {ECO:0000256|ARBA:ARBA00004279}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
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DR   AlphaFoldDB; A0A3B1IFX1; -.
DR   STRING; 7994.ENSAMXP00000028848; -.
DR   Ensembl; ENSAMXT00000052042.1; ENSAMXP00000028848.1; ENSAMXG00000009077.2.
DR   GeneTree; ENSGT00940000159555; -.
DR   InParanoid; A0A3B1IFX1; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000009077; Expressed in camera-type eye and 14 other cell types or tissues.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd12197; MARK4_C; 1.
DR   CDD; cd14072; STKc_MARK; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR001772; KA1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR   PANTHER; PTHR24346:SF28; MAP/MICROTUBULE AFFINITY-REGULATING KINASE 4; 1.
DR   Pfam; PF02149; KA1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF103243; KA1-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50032; KA1; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          64..315
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          334..373
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          751..802
FT                   /note="KA1"
FT                   /evidence="ECO:0000259|PROSITE:PS50032"
FT   REGION          375..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..470
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..695
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..714
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   802 AA;  88416 MW;  CC5CED45EB757684 CRC64;
     MSSRAALQPG NDRNSDHLPA VIMHASLSSS RSEKGSAWSN RSLGARCRNS IASCSDEHPH
     IGNYRLLKTI GKGNFAKVKL ARHILTGREV AIKIIDKTQL NPTSLQKLFR EVRIMKGLNH
     PNIVQLFEVI ETEKTLYLIM EYASGGEVFD YLVAHGRMKE KEARAKFRQI VSAVHYCHQK
     NIVHRDLKAE NLLLDADSNI KIADFGFSNE FTLGNKLDTF CGSPPYAAPE LFQGKKYDGP
     EVDIWSLGVI LYTLVSGSLP FDGQNLKELR ERVLRGKYRV PFYMSTDCEG ILRRFLVLNP
     TKRCTLEQIM KDKWMNVGHE GDELKPHVEP VENYNDPDRI DVMIGMGYSR EEIREALTTQ
     KYNEITATYL LLGRKSEDGS ESRSSSSLSL ARVRPSPITN GTSKHSSTST SSSASASTST
     HSKTQRSAST YHRQRRHSDF CGPAVPTAHP KRSPTSAGDS DLKEERLTTR KTSCSVVGSR
     SIPPSSPMVS TANNPNKSEI PDRRKEVTVT TNNIPASAMT RRNTYVCTDR SSTDRHSLLQ
     NGKENSSLSH RLPPASPSTH SIAGAGVASS SSAERSRLTR GSTVRSTFHG GQLRERRTPT
     HAPPTSPTLS HDASPLPHAR SRATSNLFSK LTSKLTRRVN LDPSKRQNSN KSVSGCPLPH
     GSKTVRSQTN LRESADLRSQ APEAKSQVKN TSRHLSGHQK AAEPRTPRCG WDVRVRSPRD
     PAEVVLALRE AAQGCGCQVH QAGPFLLSCT HGAAGSRVAF EAEVCHLPAG PTETSGVRFR
     RLWGAPLAFR DIATKVSKEL EL
//
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