Q6Y1H2 (HACD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Lyase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	lyase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCAP31	P51572	4	EBI-530257,EBI-77683

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 254	254	Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase 2		PRO_0000349319
Regions
	Topological domain	1 – 41	41	Cytoplasmic Potential
	Transmembrane	42 – 60	19	Helical; Potential
	Topological domain	61 – 79	19	Lumenal Potential
	Transmembrane	80 – 97	18	Helical; Potential
	Topological domain	98 – 107	10	Cytoplasmic Potential
	Transmembrane	108 – 125	18	Helical; Potential
	Topological domain	126 – 130	5	Lumenal Potential
	Transmembrane	131 – 146	16	Helical; Potential
	Topological domain	147 – 169	23	Cytoplasmic Potential
	Transmembrane	170 – 187	18	Helical; Potential
	Topological domain	188 – 217	30	Lumenal Potential
	Transmembrane	218 – 235	18	Helical; Potential
	Topological domain	236 – 254	19	Cytoplasmic Potential
	Compositional bias	12 – 18	7	Poly-Gly
Sites
	Active site	176	1	By similarity
	Active site	183	1	By similarity
Amino acid modifications
	Glycosylation	209	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q6Y1H2 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 6B301176C696899E	FASTA	254	28,368
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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].

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.
IPI	IPI00384497.
RefSeq	NP_940684.1. NM_198402.3.
UniGene	Hs.705480.
3D structure databases
ProteinModelPortal	Q6Y1H2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6Y1H2. 1 interaction.
STRING	9606.ENSP00000373153.
PTM databases
PhosphoSite	Q6Y1H2.
Polymorphism databases
DMDM	74738322.
Proteomic databases
PaxDb	Q6Y1H2.
PRIDE	Q6Y1H2.
Protocols and materials databases
DNASU	201562.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000383657; ENSP00000373153; ENSG00000206527.
GeneID	201562.
KEGG	hsa:201562.
UCSC	uc003egj.2. human.
Organism-specific databases
CTD	201562.
GeneCards	GC03M123209.
HGNC	HGNC:9640. PTPLB.
HPA	CAB019282.
neXtProt	NX_Q6Y1H2.
PharmGKB	PA33983.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5198.
HOGENOM	HOG000190538.
HOVERGEN	HBG057518.
InParanoid	Q6Y1H2.
KO	K10703.
OMA	ATKGNGG.
OrthoDB	EOG41NTMQ.
Gene expression databases
ArrayExpress	Q6Y1H2.
Bgee	Q6Y1H2.
CleanEx	HS_PTPLB.
Genevestigator	Q6Y1H2.
Family and domain databases
InterPro	IPR007482. Tyr_Pase-like_PTPLA. [Graphical view]
PANTHER	PTHR11035. PTHR11035. 1 hit.
Pfam	PF04387. PTPLA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	201562.
NextBio	90164.

Entry information

Entry name

HACD2_HUMAN

Accession

Primary (citable) accession number: Q6Y1H2

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.