Q9P035 (HACD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase 3
EC=4.2.1.134

Alternative name(s):
3-hydroxyacyl-CoA dehydratase 3
Short name=HACD3
Butyrate-induced protein 1
Short name=B-ind1
Short name=hB-ind1
Protein tyrosine phosphatase-like protein PTPLAD1
Protein-tyrosine phosphatase-like A domain-containing protein 1

Gene names

Name:	PTPLAD1
Synonyms:	BIND1, HACD3

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	362 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. Involved in Rac1-signaling pathways leading to the modulation of gene expression. Ref.1 Ref.8
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.8
Subunit structure	Interacts with the condensation enzymes of the ELOVL family. Interacts with RAC1. Ref.1 Ref.8
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.8.
Tissue specificity	Highly expressed in testis, kidney, brain, liver and weakly in skeletal muscle, spleen and heart. No expression detected in leukocytes. Ref.1 Ref.8
Induction	By AKAP12 and histone deacetylase inhibitors such as sodium butyrate. Ref.6
Sequence similarities	Belongs to the very long-chain fatty acids dehydratase HACD family. Contains 1 CS domain.
Sequence caution	The sequence AAF29085.1 differs from that shown. Reason: Frameshift at position 356. The sequence BAC11249.1 differs from that shown. Reason: Frameshift at position 359.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil Transmembrane Transmembrane helix
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	I-kappaB kinase/NF-kappaB cascade Traceable author statement Ref.1. Source: ProtInc Rac protein signal transduction Non-traceable author statement Ref.1. Source: UniProtKB Rho protein signal transduction Inferred from electronic annotation. Source: Compara activation of JUN kinase activity Traceable author statement Ref.1. Source: ProtInc 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	GTPase activator activity Traceable author statement Ref.1. Source: ProtInc lyase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 362	362	Very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase 3		PRO_0000313724
Regions
	Topological domain	1 – 149	149	Cytoplasmic Potential
	Transmembrane	150 – 170	21	Helical; Potential
	Topological domain	171 – 185	15	Lumenal Potential
	Transmembrane	186 – 207	22	Helical; Potential
	Topological domain	208 – 217	10	Cytoplasmic Potential
	Transmembrane	218 – 235	18	Helical; Potential
	Topological domain	236 – 241	6	Lumenal Potential
	Transmembrane	242 – 256	15	Helical; Potential
	Topological domain	257 – 279	23	Cytoplasmic Potential
	Transmembrane	280 – 298	19	Helical; Potential
	Topological domain	299 – 322	24	Lumenal Potential
	Transmembrane	323 – 343	21	Helical; Potential
	Topological domain	344 – 362	19	Cytoplasmic Potential
	Domain	5 – 94	90	CS
	Coiled coil	111 – 136	26	Potential
	Compositional bias	350 – 353	4	Poly-Arg
	Compositional bias	357 – 360	4	Poly-Lys
Sites
	Active site	286	1	By similarity
	Active site	293	1	By similarity
Amino acid modifications
	Modified residue	114	1	Phosphoserine Ref.7 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17
Natural variations
	Natural variant	56	1	E → K. Corresponds to variant rs11632737 [ dbSNP | Ensembl ].		VAR_037712
	Natural variant	269	1	M → L. Corresponds to variant rs2279854 [ dbSNP | Ensembl ].		VAR_037713
Experimental info
	Sequence conflict	60	1	E → K in BAB55101. Ref.3
	Sequence conflict	245	1	F → I in BAC11277. Ref.3
	Sequence conflict	282	1	W → G in AAH35508. Ref.4
	Sequence conflict	292	1	A → V in AAF29085. Ref.2
	Sequence conflict	352 – 362	11	RRYGQKKKKIH → LKMRAGAVAHACDPSALGG in CAB69070. Ref.1
	Sequence conflict	361	1	I → K in AAH35508. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9P035 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: 1B3591E88DD85D16	FASTA	362	43,160
	10 20 30 40 50 60 MENQVLTPHV YWAQRHRELY LRVELSDVQN PAISITENVL HFKAQGHGAK GDNVYEFHLE 70 80 90 100 110 120 FLDLVKPEPV YKLTQRQVNI TVQKKVSQWW ERLTKQEKRP LFLAPDFDRW LDESDAEMEL 130 140 150 160 170 180 RAKEEERLNK LRLESEGSPE TLTNLRKGYL FMYNLVQFLG FSWIFVNLTV RFCILGKESF 190 200 210 220 230 240 YDTFHTVADM MYFCQMLAVV ETINAAIGVT TSPVLPSLIQ LLGRNFILFI IFGTMEEMQN 250 260 270 280 290 300 KAVVFFVFYL WSAIEIFRYS FYMLTCIDMD WKVLTWLRYT LWIPLYPLGC LAEAVSVIQS 310 320 330 340 350 360 IPIFNETGRF SFTLPYPVKI KVRFSFFLQI YLIMIFLGLY INFRHLYKQR RRRYGQKKKK IH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"B-ind1, a novel mediator of Rac1 signaling cloned from sodium butyrate-treated fibroblasts." Courilleau D., Chastre E., Sabbah M., Redeuilh G., Atfi A., Mester J. J. Biol. Chem. 275:17344-17348(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAC1, TISSUE SPECIFICITY.
[2]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[3]	"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].
[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: B-cell, Duodenum, Eye and Urinary bladder.
[5]	"Human B-ind1 gene promoter: cloning and regulation by histone deacetylase inhibitors." Sabbah M., Saucier C., Redeuilh G. Gene 374:128-133(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[6]	"SSeCKS/Gravin/AKAP12 attenuates expression of proliferative and angiogenic genes during suppression of v-Src-induced oncogenesis." Liu Y., Gao L., Gelman I.H. BMC Cancer 6:105-105(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY AKAP12.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: Liver.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY.
[14]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ271091 mRNA. Translation: CAB69070.1. AF161470 mRNA. Translation: AAF29085.1. Frameshift. AK027421 mRNA. Translation: BAB55101.1. AK074857 mRNA. Translation: BAC11249.1. Frameshift. AK074898 mRNA. Translation: BAC11277.1. BC019873 mRNA. Translation: AAH19873.1. BC035508 mRNA. Translation: AAH35508.1. BC047685 mRNA. Translation: AAH47685.1. BC058912 mRNA. Translation: AAH58912.1. DQ251107 Genomic DNA. Translation: ABB83547.1.
IPI	IPI00008998.
RefSeq	NP_057479.2. NM_016395.2.
UniGene	Hs.512973.
3D structure databases
ProteinModelPortal	Q9P035.
SMR	Q9P035. Positions 5-158.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9P035. 10 interactions.
MINT	MINT-1135933.
PTM databases
PhosphoSite	Q9P035.
Polymorphism databases
DMDM	166199462.
Proteomic databases
PaxDb	Q9P035.
PRIDE	Q9P035.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261875; ENSP00000261875; ENSG00000074696.
GeneID	51495.
KEGG	hsa:51495.
UCSC	uc002apc.3. human.
Organism-specific databases
CTD	51495.
GeneCards	GC15P065822.
H-InvDB	HIX0012353.
HGNC	HGNC:24175. PTPLAD1.
HPA	HPA014837.
neXtProt	NX_Q9P035.
PharmGKB	PA142671113.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5198.
HOVERGEN	HBG108301.
InParanoid	Q9P035.
OMA	LRYTLWI.
OrthoDB	EOG4JHCG0.
Gene expression databases
ArrayExpress	Q9P035.
Bgee	Q9P035.
CleanEx	HS_PTPLAD1.
Genevestigator	Q9P035.
Family and domain databases
InterPro	IPR007052. CS-like_domain. IPR017447. CS_domain. IPR008978. HSP20-like_chaperone. IPR007482. Tyr_Pase-like_PTPLA. [Graphical view]
PANTHER	PTHR11035. PTHR11035. 1 hit.
Pfam	PF04969. CS. 1 hit. PF04387. PTPLA. 1 hit. [Graphical view]
SUPFAM	SSF49764. HSP20_chap. 1 hit.
PROSITE	PS51203. CS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PTPLAD1. human.
GenomeRNAi	51495.
NextBio	55161.

Entry information

Entry name

HACD3_HUMAN

Accession

Primary (citable) accession number: Q9P035
Secondary accession number(s): A0PJA1 , Q280Z3, Q6PD63, Q8IUI5, Q8NC86, Q8NCB1, Q96T12, Q9NQA7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	April 3, 2013
This is version 84 of the entry and version 2 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.