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Protein

Hydroxyacyl-thioester dehydratase type 2, mitochondrial

Gene

RPP14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial 3-hydroxyacyl-thioester dehydratase, which may be involved in fatty acid biosynthesis.1 Publication

Catalytic activityi

(3R)-hydroxyacyl-CoA = trans-2-enoyl-CoA + H2O.1 Publication
(3R)-hydroxyacyl-[acyl-carrier-protein] = trans-2-enoyl-[acyl-carrier-protein] + H2O.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Chemistry

SwissLipidsiSLP:000001096.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxyacyl-thioester dehydratase type 2, mitochondrial1 Publication (EC:4.2.1.-)
Short name:
HsHTD21 Publication
Alternative name(s):
3-hydroxyacyl-[acyl-carrier-protein] dehydrataseBy similarity
Gene namesi
Name:RPP141 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:30327. RPP14.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 621D → A: Abolishes ability to complement a htd2-delta mutant yeast. 1 Publication
Mutagenesisi67 – 671H → A: Abolishes ability to complement a htd2-delta mutant yeast. 1 Publication

Polymorphism and mutation databases

DMDMi281312149.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 168Hydroxyacyl-thioester dehydratase type 2, mitochondrial1 PublicationPRO_0000390489
Transit peptidei1 – ?Mitochondrion1 Publication

Proteomic databases

MaxQBiP86397.
PaxDbiP86397.
PRIDEiP86397.

Expressioni

Tissue specificityi

Highly expressed in heart and liver. Expressed at lower levels in skeletal muscle, spleen, kidney and placenta.1 Publication

Gene expression databases

ExpressionAtlasiP86397. baseline and differential.
GenevisibleiP86397. HS.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000437142.

Structurei

Secondary structure

1
168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 477Combined sources
Helixi50 – 6011Combined sources
Helixi66 – 683Combined sources
Helixi85 – 9814Combined sources
Beta strandi106 – 1138Combined sources
Beta strandi123 – 13412Combined sources
Beta strandi137 – 14610Combined sources
Turni147 – 1493Combined sources
Beta strandi152 – 16110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IR3X-ray1.99A/B23-168[»]
ProteinModelPortaliP86397.
SMRiP86397. Positions 34-167.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP86397.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 146106MaoC-likeAdd
BLAST

Sequence similaritiesi

Belongs to the HTD2 family.Sequence analysis
Contains 1 MaoC-like domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1206. Eukaryota.
COG2030. LUCA.
GeneTreeiENSGT00530000065109.
InParanoidiP86397.
OMAiRFPAPLY.
PhylomeDBiP86397.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR002539. MaoC_dom.
[Graphical view]
PfamiPF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P86397-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFPLISSHHL WWGGLRRTVC LNLPVLTLQH FQHMHIKVGD RAELRRAFTQ
60 70 80 90 100
TDVATFSELT GDVNPLHLNE DFAKHTKFGN TIVHGVLING LISALLGTKM
110 120 130 140 150
PGPGCVFLSQ EISFPAPLYI GEVVLASAEV KKLKRFIAII AVSCSVIESK
160
KTVMEGWVKV MVPEASKS
Length:168
Mass (Da):18,559
Last modified:December 15, 2009 - v1
Checksum:i6AAB9445C17F4FD7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC098479 mRNA. No translation available.
UniGeneiHs.446320.
Hs.700016.

Genome annotation databases

UCSCiuc010hni.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC098479 mRNA. No translation available.
UniGeneiHs.446320.
Hs.700016.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IR3X-ray1.99A/B23-168[»]
ProteinModelPortaliP86397.
SMRiP86397. Positions 34-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000437142.

Chemistry

SwissLipidsiSLP:000001096.

Polymorphism and mutation databases

DMDMi281312149.

Proteomic databases

MaxQBiP86397.
PaxDbiP86397.
PRIDEiP86397.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc010hni.4. human.

Organism-specific databases

GeneCardsiRPP14.
H-InvDBHIX0200536.
HGNCiHGNC:30327. RPP14.
neXtProtiNX_P86397.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1206. Eukaryota.
COG2030. LUCA.
GeneTreeiENSGT00530000065109.
InParanoidiP86397.
OMAiRFPAPLY.
PhylomeDBiP86397.

Miscellaneous databases

ChiTaRSiRPP14. human.
EvolutionaryTraceiP86397.

Gene expression databases

ExpressionAtlasiP86397. baseline and differential.
GenevisibleiP86397. HS.

Family and domain databases

Gene3Di3.10.129.10. 1 hit.
InterProiIPR029069. HotDog_dom.
IPR002539. MaoC_dom.
[Graphical view]
PfamiPF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
SUPFAMiSSF54637. SSF54637. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An ancient genetic link between vertebrate mitochondrial fatty acid synthesis and RNA processing."
    Autio K.J., Kastaniotis A.J., Pospiech H., Miinalainen I.J., Schonauer M.S., Dieckmann C.L., Hiltunen J.K.
    FASEB J. 22:569-578(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION OF BICISTRONIC GENE, MUTAGENESIS OF ASP-62 AND HIS-67.
    Tissue: Cerebellum1 Publication and Kidney1 Publication.
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Crystal structure of human 3-hydroxyacyl-thioester dehydratase 2 (HTD2)."
    Structural genomics consortium (SGC)
    Ugochukwu E., Cocking R., Burgess-Brown N., Pilka E., Muniz J., Krojer T., Chaikuad A., Gileadi O., Bountra C., Arrowsmith C.H., Weigelt J., Edwards A., Kavanagh K.L., Oppermann U.
    Submitted (AUG-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 23-168.

Entry informationi

Entry nameiHTD2_HUMAN
AccessioniPrimary (citable) accession number: P86397
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2009
Last sequence update: December 15, 2009
Last modified: June 8, 2016
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

This protein is produced by a bicistronic gene which also produces the RPP14 protein from an overlapping reading frame.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.