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Q6Y1H2 (HACD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase 2

EC=4.2.1.134
Alternative name(s):
3-hydroxyacyl-CoA dehydratase 2
Short name=HACD2
Protein-tyrosine phosphatase-like member B
Gene names
Name:PTPLB
Synonyms:HACD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the dehydration step in very long-chain fatty acid (VLCFA) synthesis. Ref.5

Catalytic activity

A very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] = a very-long-chain trans-2,3-dehydroacyl-[acyl-carrier protein] + H2O. Ref.5

Subunit structure

Interacts with the condensation enzymes of the ELOVL family. Interacts with BCAP31. Ref.1 Ref.5

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1 Ref.5.

Tissue specificity

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. Ref.1 Ref.5

Miscellaneous

Turns over rapidly through degradation by the proteasome system.

Sequence similarities

Belongs to the very long-chain fatty acids dehydratase HACD family.

Caution

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCAP31P515724EBI-530257,EBI-77683

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 254253Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase 2
PRO_0000349319

Regions

Topological domain2 – 4140Cytoplasmic Potential
Transmembrane42 – 6019Helical; Potential
Topological domain61 – 7919Lumenal Potential
Transmembrane80 – 9718Helical; Potential
Topological domain98 – 10710Cytoplasmic Potential
Transmembrane108 – 12518Helical; Potential
Topological domain126 – 1305Lumenal Potential
Transmembrane131 – 14616Helical; Potential
Topological domain147 – 16923Cytoplasmic Potential
Transmembrane170 – 18718Helical; Potential
Topological domain188 – 21730Lumenal Potential
Transmembrane218 – 23518Helical; Potential
Topological domain236 – 25419Cytoplasmic Potential
Compositional bias12 – 187Poly-Gly

Sites

Active site1761 By similarity
Active site1831 By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.6
Glycosylation2091N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q6Y1H2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6B301176C696899E

FASTA25428,368
        10         20         30         40         50         60 
MAAVAATAAA KGNGGGGGRA GAGDASGTRK KKGPGPLATA YLVIYNVVMT AGWLVIAVGL 

        70         80         90        100        110        120 
VRAYLAKGSY HSLYYSIEKP LKFFQTGALL EILHCAIGIV PSSVVLTSFQ VMSRVFLIWA 

       130        140        150        160        170        180 
VTHSVKEVQS EDSVLLFVIA WTITEIIRYS FYTFSLLNHL PYLIKWARYT LFIVLYPMGV 

       190        200        210        220        230        240 
SGELLTIYAA LPFVRQAGLY SISLPNKYNF SFDYYAFLIL IMISYIPIFP QLYFHMIHQR 

       250 
RKILSHTEEH KKFE 

« Hide

References

« Hide 'large scale' references
[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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH BCAP31.
[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. expand/collapse author list , 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(2004) [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. expand/collapse author list , 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].
[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(2004) [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(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INTERACTION WITH ELOVL FAMILY.
[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(2009) [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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_940684.1. NM_198402.3.
UniGeneHs.705480.

3D structure databases

ProteinModelPortalQ6Y1H2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128393. 3 interactions.
IntActQ6Y1H2. 1 interaction.
STRING9606.ENSP00000373153.

PTM databases

PhosphoSiteQ6Y1H2.

Polymorphism databases

DMDM74738322.

Proteomic databases

PaxDbQ6Y1H2.
PRIDEQ6Y1H2.

Protocols and materials databases

DNASU201562.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000383657; ENSP00000373153; ENSG00000206527.
GeneID201562.
KEGGhsa:201562.
UCSCuc003egj.2. human.

Organism-specific databases

CTD201562.
GeneCardsGC03M123209.
HGNCHGNC:9640. PTPLB.
HPACAB019282.
neXtProtNX_Q6Y1H2.
PharmGKBPA33983.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5198.
HOGENOMHOG000190538.
HOVERGENHBG057518.
InParanoidQ6Y1H2.
KOK10703.
OMAVREVQSE.
OrthoDBEOG7X6M18.
PhylomeDBQ6Y1H2.
TreeFamTF313326.

Gene expression databases

ArrayExpressQ6Y1H2.
BgeeQ6Y1H2.
CleanExHS_PTPLB.
GenevestigatorQ6Y1H2.

Family and domain databases

InterProIPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERPTHR11035. PTHR11035. 1 hit.
PfamPF04387. PTPLA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi201562.
NextBio90164.
PROQ6Y1H2.

Entry information

Entry nameHACD2_HUMAN
AccessionPrimary (citable) accession number: Q6Y1H2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM