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HTD2_HUMAN
ID   HTD2_HUMAN              Reviewed;         168 AA.
AC   P86397;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Hydroxyacyl-thioester dehydratase type 2, mitochondrial {ECO:0000303|PubMed:17898086};
DE            Short=HsHTD2 {ECO:0000303|PubMed:17898086};
DE            EC=4.2.1.59 {ECO:0000269|PubMed:17898086};
DE   AltName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase {ECO:0000250|UniProtKB:P38790};
DE   Flags: Precursor;
GN   Name=HTD2 {ECO:0000303|PubMed:17898086};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION OF BICISTRONIC
RP   GENE, AND MUTAGENESIS OF ASP-62 AND HIS-67.
RC   TISSUE=Cerebellum {ECO:0000269|PubMed:17898086}, and
RC   Kidney {ECO:0000269|PubMed:17898086};
RX   PubMed=17898086; DOI=10.1096/fj.07-8986;
RA   Autio K.J., Kastaniotis A.J., Pospiech H., Miinalainen I.J.,
RA   Schonauer M.S., Dieckmann C.L., Hiltunen J.K.;
RT   "An ancient genetic link between vertebrate mitochondrial fatty acid
RT   synthesis and RNA processing.";
RL   FASEB J. 22:569-578(2008).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [3] {ECO:0000305}
RP   X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 23-168.
RG   Structural genomics consortium (SGC);
RA   Ugochukwu E., Cocking R., Burgess-Brown N., Pilka E., Muniz J., Krojer T.,
RA   Chaikuad A., Gileadi O., Bountra C., Arrowsmith C.H., Weigelt J.,
RA   Edwards A., Kavanagh K.L., Oppermann U.;
RT   "Crystal structure of human 3-hydroxyacyl-thioester dehydratase 2 (HTD2).";
RL   Submitted (AUG-2009) to the PDB data bank.
CC   -!- FUNCTION: Mitochondrial 3-hydroxyacyl-thioester dehydratase, which may
CC       be involved in fatty acid biosynthesis. {ECO:0000269|PubMed:17898086}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC         Evidence={ECO:0000269|PubMed:17898086};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458;
CC         Evidence={ECO:0000269|PubMed:17898086};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829;
CC         Evidence={ECO:0000305|PubMed:17898086};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;
CC         Evidence={ECO:0000269|PubMed:17898086};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861;
CC         Evidence={ECO:0000305|PubMed:17898086};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17898086}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart and liver. Expressed at
CC       lower levels in skeletal muscle, spleen, kidney and placenta.
CC       {ECO:0000269|PubMed:17898086}.
CC   -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC       also produces the RPP14 protein from an overlapping reading frame.
CC       {ECO:0000269|PubMed:17898086}.
CC   -!- SIMILARITY: Belongs to the HTD2 family. {ECO:0000255}.
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DR   EMBL; AC098479; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS87096.1; -.
DR   RefSeq; NP_001335641.1; NM_001348712.1.
DR   RefSeq; NP_001335642.1; NM_001348713.1.
DR   RefSeq; NP_001335643.1; NM_001348714.1.
DR   RefSeq; NP_001335644.1; NM_001348715.1.
DR   PDB; 3IR3; X-ray; 1.99 A; A/B=23-168.
DR   PDBsum; 3IR3; -.
DR   AlphaFoldDB; P86397; -.
DR   SMR; P86397; -.
DR   IntAct; P86397; 1.
DR   STRING; 9606.ENSP00000481593; -.
DR   SwissLipids; SLP:000001096; -.
DR   BioMuta; HTD2; -.
DR   DMDM; 281312149; -.
DR   EPD; P86397; -.
DR   jPOST; P86397; -.
DR   MassIVE; P86397; -.
DR   MaxQB; P86397; -.
DR   PaxDb; P86397; -.
DR   PeptideAtlas; P86397; -.
DR   PRIDE; P86397; -.
DR   ProteomicsDB; 57772; -.
DR   Antibodypedia; 69913; 17 antibodies from 4 providers.
DR   DNASU; 109703458; -.
DR   Ensembl; ENST00000461393.7; ENSP00000484277.1; ENSG00000255154.9.
DR   Ensembl; ENST00000477305.5; ENSP00000481593.1; ENSG00000255154.9.
DR   Ensembl; ENST00000481972.5; ENSP00000482940.1; ENSG00000255154.9.
DR   GeneID; 109703458; -.
DR   KEGG; hsa:109703458; -.
DR   MANE-Select; ENST00000461393.7; ENSP00000484277.1; NM_001348712.2; NP_001335641.1.
DR   UCSC; uc010hni.4; human.
DR   CTD; 109703458; -.
DR   DisGeNET; 109703458; -.
DR   GeneCards; HTD2; -.
DR   HGNC; HGNC:53111; HTD2.
DR   HPA; ENSG00000255154; Tissue enhanced (skeletal).
DR   neXtProt; NX_P86397; -.
DR   OpenTargets; ENSG00000255154; -.
DR   VEuPathDB; HostDB:ENSG00000255154; -.
DR   eggNOG; KOG1206; Eukaryota.
DR   GeneTree; ENSGT00530000065109; -.
DR   HOGENOM; CLU_094876_3_4_1; -.
DR   InParanoid; P86397; -.
DR   OMA; PGPGCIY; -.
DR   OrthoDB; 1326407at2759; -.
DR   PhylomeDB; P86397; -.
DR   BioCyc; MetaCyc:G66-33210-MON; -.
DR   PathwayCommons; P86397; -.
DR   Reactome; R-HSA-75105; Fatty acyl-CoA biosynthesis.
DR   BioGRID-ORCS; 109703458; 3 hits in 15 CRISPR screens.
DR   EvolutionaryTrace; P86397; -.
DR   GenomeRNAi; 109703458; -.
DR   Pharos; P86397; Tdark.
DR   PRO; PR:P86397; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P86397; protein.
DR   Bgee; ENSG00000255154; Expressed in muscle of leg and 110 other tissues.
DR   ExpressionAtlas; P86397; baseline and differential.
DR   Genevisible; P86397; HS.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019171; F:3-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IBA:GO_Central.
DR   GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; TAS:Reactome.
DR   GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046949; P:fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR002539; MaoC-like_dom.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   SUPFAM; SSF54637; SSF54637; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Fatty acid metabolism; Lipid metabolism; Lyase;
KW   Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:17898086"
FT   CHAIN           ?..168
FT                   /note="Hydroxyacyl-thioester dehydratase type 2,
FT                   mitochondrial"
FT                   /evidence="ECO:0000269|PubMed:17898086"
FT                   /id="PRO_0000390489"
FT   DOMAIN          41..146
FT                   /note="MaoC-like"
FT   MUTAGEN         62
FT                   /note="D->A: Abolishes ability to complement a htd2-delta
FT                   mutant yeast."
FT                   /evidence="ECO:0000269|PubMed:17898086"
FT   MUTAGEN         67
FT                   /note="H->A: Abolishes ability to complement a htd2-delta
FT                   mutant yeast."
FT                   /evidence="ECO:0000269|PubMed:17898086"
FT   STRAND          41..47
FT                   /evidence="ECO:0007829|PDB:3IR3"
FT   HELIX           50..60
FT                   /evidence="ECO:0007829|PDB:3IR3"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:3IR3"
FT   HELIX           85..98
FT                   /evidence="ECO:0007829|PDB:3IR3"
FT   STRAND          106..113
FT                   /evidence="ECO:0007829|PDB:3IR3"
FT   STRAND          123..134
FT                   /evidence="ECO:0007829|PDB:3IR3"
FT   STRAND          137..146
FT                   /evidence="ECO:0007829|PDB:3IR3"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:3IR3"
FT   STRAND          152..161
FT                   /evidence="ECO:0007829|PDB:3IR3"
SQ   SEQUENCE   168 AA;  18559 MW;  6AAB9445C17F4FD7 CRC64;
     MFPLISSHHL WWGGLRRTVC LNLPVLTLQH FQHMHIKVGD RAELRRAFTQ TDVATFSELT
     GDVNPLHLNE DFAKHTKFGN TIVHGVLING LISALLGTKM PGPGCVFLSQ EISFPAPLYI
     GEVVLASAEV KKLKRFIAII AVSCSVIESK KTVMEGWVKV MVPEASKS
 
 
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