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DOHH_CAEEL
ID   DOHH_CAEEL              Reviewed;         298 AA.
AC   Q17949;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Deoxyhypusine hydroxylase {ECO:0000255|HAMAP-Rule:MF_03101};
DE            Short=DOHH {ECO:0000255|HAMAP-Rule:MF_03101};
DE            EC=1.14.99.29 {ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine dioxygenase {ECO:0000255|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine monooxygenase {ECO:0000255|HAMAP-Rule:MF_03101};
GN   Name=dohh-1 {ECO:0000255|HAMAP-Rule:MF_03101};
GN   Synonyms=tag-242 {ECO:0000312|WormBase:C14A4.1};
GN   ORFNames=C14A4.1 {ECO:0000312|WormBase:C14A4.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=24832488; DOI=10.1242/dmm.014449;
RA   Sievert H., Paellmann N., Miller K.K., Hermans-Borgmeyer I., Venz S.,
RA   Sendoel A., Preukschas M., Schweizer M., Boettcher S., Janiesch P.C.,
RA   Streichert T., Walther R., Hengartner M.O., Manz M.G., Bruemmendorf T.H.,
RA   Bokemeyer C., Braig M., Hauber J., Duncan K.E., Balabanov S.;
RT   "A novel mouse model for inhibition of DOHH-mediated hypusine modification
RT   reveals a crucial function in embryonic development, proliferation and
RT   oncogenic transformation.";
RL   Dis. Model. Mech. 7:963-976(2014).
CC   -!- FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-
CC       lysine intermediate produced by deoxyhypusine synthase/DHPS on a
CC       critical lysine of the eukaryotic translation initiation factor 5A/eIF-
CC       5A. This is the second step of the post-translational modification of
CC       that lysine into an unusual amino acid residue named hypusine.
CC       Hypusination is unique to mature eIF-5A factor and is essential for its
CC       function. {ECO:0000250|UniProtKB:Q99LN9, ECO:0000255|HAMAP-
CC       Rule:MF_03101}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-
CC         hypusine + A + H2O; Xref=Rhea:RHEA:14101, Rhea:RHEA-COMP:10144,
CC         Rhea:RHEA-COMP:12592, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:82657,
CC         ChEBI:CHEBI:91175; EC=1.14.99.29;
CC         Evidence={ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
CC         Rule:MF_03101};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q9BU89,
CC         ECO:0000255|HAMAP-Rule:MF_03101};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9BU89,
CC       ECO:0000255|HAMAP-Rule:MF_03101};
CC   -!- PATHWAY: Protein modification; eIF5A hypusination.
CC       {ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-Rule:MF_03101}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethal with the production of
CC       multinucleated cells from the one-cell stage of embryogenesis leading
CC       to the in utero accumulation of abnormal and enlarged embryos.
CC       {ECO:0000269|PubMed:24832488}.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03101}.
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DR   EMBL; Z49909; CAA90105.1; -; Genomic_DNA.
DR   PIR; T19243; T19243.
DR   RefSeq; NP_496279.1; NM_063878.3.
DR   AlphaFoldDB; Q17949; -.
DR   SMR; Q17949; -.
DR   BioGRID; 532896; 7.
DR   STRING; 6239.C14A4.1; -.
DR   EPD; Q17949; -.
DR   PaxDb; Q17949; -.
DR   PeptideAtlas; Q17949; -.
DR   EnsemblMetazoa; C14A4.1.1; C14A4.1.1; WBGene00007555.
DR   GeneID; 3565578; -.
DR   KEGG; cel:CELE_C14A4.1; -.
DR   UCSC; C14A4.1.1; c. elegans.
DR   CTD; 3565578; -.
DR   WormBase; C14A4.1; CE02138; WBGene00007555; dohh-1.
DR   eggNOG; KOG0567; Eukaryota.
DR   GeneTree; ENSGT00940000165304; -.
DR   HOGENOM; CLU_053974_0_0_1; -.
DR   InParanoid; Q17949; -.
DR   OMA; CIQILNR; -.
DR   OrthoDB; 1441854at2759; -.
DR   PhylomeDB; Q17949; -.
DR   Reactome; R-CEL-204626; Hypusine synthesis from eIF5A-lysine.
DR   UniPathway; UPA00354; -.
DR   PRO; PR:Q17949; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00007555; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IC:WormBase.
DR   GO; GO:0019135; F:deoxyhypusine monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 2.
DR   HAMAP; MF_03101; Deoxyhypusine_hydroxylase; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR027517; Deoxyhypusine_hydroxylase.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   Pfam; PF03130; HEAT_PBS; 1.
DR   SMART; SM00567; EZ_HEAT; 6.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   3: Inferred from homology;
KW   Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Repeat.
FT   CHAIN           1..298
FT                   /note="Deoxyhypusine hydroxylase"
FT                   /id="PRO_0000248581"
FT   REPEAT          28..54
FT                   /note="HEAT-like PBS-type 1"
FT   REPEAT          59..85
FT                   /note="HEAT-like PBS-type 2"
FT   REPEAT          92..118
FT                   /note="HEAT-like PBS-type 3"
FT   REPEAT          178..204
FT                   /note="HEAT-like PBS-type 4"
FT   REPEAT          210..236
FT                   /note="HEAT-like PBS-type 5"
FT   REPEAT          243..269
FT                   /note="HEAT-like PBS-type 6"
FT   REGION          140..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         61
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
FT   BINDING         95
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
FT   BINDING         212
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
FT   BINDING         245
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
FT   BINDING         246
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
SQ   SEQUENCE   298 AA;  33240 MW;  D92C75F3F63811CB CRC64;
     MVASQKFSDA EIDSFGEALN DTKKPLKARF RALFILRNIG CDRSVDWIGK CLNDESALLK
     HELAYCLGQM QNKHAIPTLV SVLEDEKQEP MVRHEAGEAL GAIADPSVKD VLRKYAQDPC
     PEVSETCQIA LGRVEWVEKS GKDTNSPYDS VDPTPSASTS DVEELAATLI DASLPLFDRY
     RAMFSLRNIK TDKSIKALAQ GLYCEDSALF RHEVAYVLGQ LQSPVATQEL KDRLLLSTEN
     CMVRHECAEA LGAIANEECT EILKQYVNDE ERVVRESCEV ALDMAEYENS DDLQYAHV
 
 
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