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Protein

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2

Gene

PTPLB

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

Functioni

Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.1 Publication

Catalytic activityi

A very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H2O.1 Publication

Kineticsi

  1. KM=121.7 µM for 3-hydroxypalmitoyl-CoA (at 37 degrees Celsius)1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei176 – 1761By similarity
Active sitei183 – 1831By similarity

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydratase activity Source: UniProtKB
  2. enzyme binding Source: UniProtKB

GO - Biological processi

  1. fatty acid elongation Source: UniProtKB
  2. sphingolipid biosynthetic process Source: UniProtKB
  3. very long-chain fatty acid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2Curated (EC:4.2.1.1341 Publication)
Alternative name(s):
3-hydroxyacyl-CoA dehydratase 21 Publication
Short name:
HACD21 Publication
Protein-tyrosine phosphatase-like member BImported
Gene namesi
Name:PTPLBImported
Synonyms:HACD21 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9640. PTPLB.

Subcellular locationi

Endoplasmic reticulum membrane 2 Publications; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 4140CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei42 – 6019HelicalSequence AnalysisAdd
BLAST
Topological domaini61 – 7919LumenalSequence AnalysisAdd
BLAST
Transmembranei80 – 9718HelicalSequence AnalysisAdd
BLAST
Topological domaini98 – 10710CytoplasmicSequence Analysis
Transmembranei108 – 12518HelicalSequence AnalysisAdd
BLAST
Topological domaini126 – 1305LumenalSequence Analysis
Transmembranei131 – 14616HelicalSequence AnalysisAdd
BLAST
Topological domaini147 – 16923CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei170 – 18718HelicalSequence AnalysisAdd
BLAST
Topological domaini188 – 21730LumenalSequence AnalysisAdd
BLAST
Transmembranei218 – 23518HelicalSequence AnalysisAdd
BLAST
Topological domaini236 – 25419CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011P → R: Does not restore any protein tyrosine phosphatase activity. 1 Publication

Organism-specific databases

PharmGKBiPA33983.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 254253Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2PRO_0000349319Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiQ6Y1H2.
PaxDbiQ6Y1H2.
PRIDEiQ6Y1H2.

PTM databases

PhosphoSiteiQ6Y1H2.

Expressioni

Tissue specificityi

Highly expressed in testis, spleen, prostate, colon and heart, followed by moderate expression in thymus, ovary, small intestine, peripheral blood leukocytes, liver, skeletal muscle and pancreas. Weakly detected in kidney, placenta, brain and lung.1 Publication

Gene expression databases

BgeeiQ6Y1H2.
CleanExiHS_PTPLB.
ExpressionAtlasiQ6Y1H2. baseline and differential.
GenevestigatoriQ6Y1H2.

Organism-specific databases

HPAiCAB019282.

Interactioni

Subunit structurei

May interact with enzymes of the ELO family (including ELOVL1); with those enzymes that mediate condensation, the first of the four steps of the reaction cycle responsible for fatty acids elongation, may be part of a larger fatty acids elongase complex (PubMed:18554506). Interacts with BCAP31 (PubMed:15024066).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAP31P515724EBI-530257,EBI-77683

Protein-protein interaction databases

BioGridi128393. 7 interactions.
IntActiQ6Y1H2. 1 interaction.
STRINGi9606.ENSP00000373153.

Structurei

3D structure databases

ProteinModelPortaliQ6Y1H2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi12 – 187Poly-Gly

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5198.
GeneTreeiENSGT00530000062962.
HOGENOMiHOG000190538.
HOVERGENiHBG057518.
InParanoidiQ6Y1H2.
KOiK10703.
OMAiVREVQSE.
OrthoDBiEOG7X6M18.
PhylomeDBiQ6Y1H2.
TreeFamiTF313326.

Family and domain databases

InterProiIPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERiPTHR11035. PTHR11035. 1 hit.
PfamiPF04387. PTPLA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6Y1H2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVAATAAA KGNGGGGGRA GAGDASGTRK KKGPGPLATA YLVIYNVVMT
60 70 80 90 100
AGWLVIAVGL VRAYLAKGSY HSLYYSIEKP LKFFQTGALL EILHCAIGIV
110 120 130 140 150
PSSVVLTSFQ VMSRVFLIWA VTHSVKEVQS EDSVLLFVIA WTITEIIRYS
160 170 180 190 200
FYTFSLLNHL PYLIKWARYT LFIVLYPMGV SGELLTIYAA LPFVRQAGLY
210 220 230 240 250
SISLPNKYNF SFDYYAFLIL IMISYIPIFP QLYFHMIHQR RKILSHTEEH

KKFE
Length:254
Mass (Da):28,368
Last modified:July 5, 2004 - v1
Checksum:i6B301176C696899E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY191814 mRNA. Translation: AAP20101.1.
AK289983 mRNA. Translation: BAF82672.1.
AC020631 Genomic DNA. No translation available.
AC023165 Genomic DNA. No translation available.
AC025571 Genomic DNA. No translation available.
AC084039 Genomic DNA. No translation available.
BC049369 mRNA. Translation: AAH49369.1.
BC060839 mRNA. Translation: AAH60839.1.
CCDSiCCDS46895.1.
RefSeqiNP_940684.1. NM_198402.3.
UniGeneiHs.705480.

Genome annotation databases

EnsembliENST00000383657; ENSP00000373153; ENSG00000206527.
GeneIDi201562.
KEGGihsa:201562.
UCSCiuc003egj.2. human.

Polymorphism databases

DMDMi74738322.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY191814 mRNA. Translation: AAP20101.1.
AK289983 mRNA. Translation: BAF82672.1.
AC020631 Genomic DNA. No translation available.
AC023165 Genomic DNA. No translation available.
AC025571 Genomic DNA. No translation available.
AC084039 Genomic DNA. No translation available.
BC049369 mRNA. Translation: AAH49369.1.
BC060839 mRNA. Translation: AAH60839.1.
CCDSiCCDS46895.1.
RefSeqiNP_940684.1. NM_198402.3.
UniGeneiHs.705480.

3D structure databases

ProteinModelPortaliQ6Y1H2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128393. 7 interactions.
IntActiQ6Y1H2. 1 interaction.
STRINGi9606.ENSP00000373153.

PTM databases

PhosphoSiteiQ6Y1H2.

Polymorphism databases

DMDMi74738322.

Proteomic databases

MaxQBiQ6Y1H2.
PaxDbiQ6Y1H2.
PRIDEiQ6Y1H2.

Protocols and materials databases

DNASUi201562.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000383657; ENSP00000373153; ENSG00000206527.
GeneIDi201562.
KEGGihsa:201562.
UCSCiuc003egj.2. human.

Organism-specific databases

CTDi201562.
GeneCardsiGC03M123209.
HGNCiHGNC:9640. PTPLB.
HPAiCAB019282.
MIMi615939. gene.
neXtProtiNX_Q6Y1H2.
PharmGKBiPA33983.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5198.
GeneTreeiENSGT00530000062962.
HOGENOMiHOG000190538.
HOVERGENiHBG057518.
InParanoidiQ6Y1H2.
KOiK10703.
OMAiVREVQSE.
OrthoDBiEOG7X6M18.
PhylomeDBiQ6Y1H2.
TreeFamiTF313326.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

GenomeRNAii201562.
NextBioi90164.
PROiQ6Y1H2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6Y1H2.
CleanExiHS_PTPLB.
ExpressionAtlasiQ6Y1H2. baseline and differential.
GenevestigatoriQ6Y1H2.

Family and domain databases

InterProiIPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERiPTHR11035. PTHR11035. 1 hit.
PfamiPF04387. PTPLA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The yeast split-ubiquitin membrane protein two-hybrid screen identifies BAP31 as a regulator of the turnover of endoplasmic reticulum-associated protein tyrosine phosphatase-like B."
    Wang B., Pelletier J., Massaad M.J., Herscovics A., Shore G.C.
    Mol. Cell. Biol. 24:2767-2778(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH BCAP31, MUTAGENESIS OF PRO-101, CAUTION.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Testis.
  5. "Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis."
    Ikeda M., Kanao Y., Yamanaka M., Sakuraba H., Mizutani Y., Igarashi Y., Kihara A.
    FEBS Lett. 582:2435-2440(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHACD2_HUMAN
AccessioniPrimary (citable) accession number: Q6Y1H2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 5, 2004
Last modified: March 4, 2015
This is version 99 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

Turns over rapidly through degradation by the proteasome system.1 Publication

Caution

Shares some similarity with tyrosine phosphatase proteins but it has probably no phosphatase activity.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.