HACD3_HUMAN
ID HACD3_HUMAN Reviewed; 362 AA.
AC Q9P035; A0PJA1; B4DRF4; Q280Z3; Q6PD63; Q8IUI5; Q8NC86; Q8NCB1; Q96T12;
AC Q9NQA7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 {ECO:0000305};
DE EC=4.2.1.134 {ECO:0000269|PubMed:18554506};
DE AltName: Full=3-hydroxyacyl-CoA dehydratase 3 {ECO:0000303|PubMed:18554506};
DE Short=HACD3 {ECO:0000303|PubMed:18554506};
DE AltName: Full=Butyrate-induced protein 1 {ECO:0000303|PubMed:10747961};
DE Short=B-ind1 {ECO:0000303|PubMed:10747961};
DE Short=hB-ind1 {ECO:0000303|PubMed:10747961};
DE AltName: Full=Protein-tyrosine phosphatase-like A domain-containing protein 1 {ECO:0000312|HGNC:HGNC:24175};
GN Name=HACD3 {ECO:0000303|PubMed:18554506, ECO:0000312|HGNC:HGNC:24175};
GN Synonyms=BIND1 {ECO:0000303|PubMed:10747961}, PTPLAD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RAC1,
RP AND TISSUE SPECIFICITY.
RX PubMed=10747961; DOI=10.1074/jbc.m000887200;
RA Courilleau D., Chastre E., Sabbah M., Redeuilh G., Atfi A., Mester J.;
RT "B-ind1, a novel mediator of Rac1 signaling cloned from sodium butyrate-
RT treated fibroblasts.";
RL J. Biol. Chem. 275:17344-17348(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell, Duodenum, Eye, and Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=16516406; DOI=10.1016/j.gene.2006.01.022;
RA Sabbah M., Saucier C., Redeuilh G.;
RT "Human B-ind1 gene promoter: cloning and regulation by histone deacetylase
RT inhibitors.";
RL Gene 374:128-133(2006).
RN [7]
RP INDUCTION BY AKAP12.
RX PubMed=16638134; DOI=10.1186/1471-2407-6-105;
RA Liu Y., Gao L., Gelman I.H.;
RT "SSeCKS/Gravin/AKAP12 attenuates expression of proliferative and angiogenic
RT genes during suppression of v-Src-induced oncogenesis.";
RL BMC Cancer 6:105-105(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INTERACTION WITH
RP ELOVL FAMILY.
RX PubMed=18554506; DOI=10.1016/j.febslet.2008.06.007;
RA Ikeda M., Kanao Y., Yamanaka M., Sakuraba H., Mizutani Y., Igarashi Y.,
RA Kihara A.;
RT "Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved
RT in very long-chain fatty acid synthesis.";
RL FEBS Lett. 582:2435-2440(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7; SER-114 AND SER-135, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP FUNCTION, AND SUBUNIT.
RX PubMed=25687571; DOI=10.1074/mcp.m114.047159;
RA Boutchueng-Djidjou M., Collard-Simard G., Fortier S., Hebert S.S.,
RA Kelly I., Landry C.R., Faure R.L.;
RT "The last enzyme of the de novo purine synthesis pathway 5-aminoimidazole-
RT 4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC)
RT plays a central role in insulin signaling and the Golgi/endosomes protein
RT network.";
RL Mol. Cell. Proteomics 14:1079-1092(2015).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Catalyzes the third of the four reactions of the long-chain
CC fatty acids elongation cycle. This endoplasmic reticulum-bound
CC enzymatic process, allows the addition of two carbons to the chain of
CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme
CC catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into
CC trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation.
CC Thereby, it participates in the production of VLCFAs of different chain
CC lengths that are involved in multiple biological processes as
CC precursors of membrane lipids and lipid mediators. May be involved in
CC Rac1-signaling pathways leading to the modulation of gene expression.
CC Promotes insulin receptor/INSR autophosphorylation and is involved in
CC INSR internalization (PubMed:25687571). {ECO:0000269|PubMed:10747961,
CC ECO:0000269|PubMed:18554506, ECO:0000269|PubMed:25687571}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain
CC (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:45812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:83728, ChEBI:CHEBI:85440; EC=4.2.1.134;
CC Evidence={ECO:0000269|PubMed:18554506};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45813;
CC Evidence={ECO:0000305|PubMed:18554506};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39159, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:74278; Evidence={ECO:0000269|PubMed:18554506};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39160;
CC Evidence={ECO:0000305|PubMed:18554506};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=49.5 uM for 3-hydroxypalmitoyl-CoA (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18554506};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:18554506}.
CC -!- SUBUNIT: May interact with enzymes of the ELO family (including
CC ELOVL1); with those enzymes that mediate condensation, the first of the
CC four steps of the reaction cycle responsible for fatty acids
CC elongation, may be part of a larger fatty acids elongase complex
CC (PubMed:18554506). Interacts with RAC1 (PubMed:10747961). Associates
CC with internalized insulin receptor/INSR complexes on Golgi/endosomal
CC membranes; HACD3/PTPLAD1 together with ATIC and PRKAA2/AMPK2 is
CC proposed to be part of a signaling network regulating INSR
CC autophosphorylation and endocytosis (PubMed:25687571).
CC {ECO:0000269|PubMed:10747961, ECO:0000269|PubMed:18554506,
CC ECO:0000269|PubMed:25687571}.
CC -!- INTERACTION:
CC Q9P035; PRO_0000278740 [Q03463]; Xeno; NbExp=2; IntAct=EBI-359013, EBI-8803426;
CC Q9P035; PRO_0000045602 [Q99IB8]; Xeno; NbExp=2; IntAct=EBI-359013, EBI-6927873;
CC Q9P035; PRO_0000037551 [Q9WMX2]; Xeno; NbExp=3; IntAct=EBI-359013, EBI-6863748;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18554506}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18554506}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P035-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P035-2; Sequence=VSP_056070;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, kidney, brain, liver
CC and weakly in skeletal muscle, spleen and heart. No expression detected
CC in leukocytes. {ECO:0000269|PubMed:10747961,
CC ECO:0000269|PubMed:18554506}.
CC -!- INDUCTION: By AKAP12 and histone deacetylase inhibitors such as sodium
CC butyrate. {ECO:0000269|PubMed:16638134}.
CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD
CC family. {ECO:0000305}.
CC -!- CAUTION: Shares some similarity with tyrosine phosphatase proteins but
CC it has probably no phosphatase activity. {ECO:0000250|UniProtKB:Q6Y1H2,
CC ECO:0000305|PubMed:18554506}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF29085.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC11249.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ271091; CAB69070.1; -; mRNA.
DR EMBL; AF161470; AAF29085.1; ALT_FRAME; mRNA.
DR EMBL; AK027421; BAB55101.1; -; mRNA.
DR EMBL; AK074857; BAC11249.1; ALT_FRAME; mRNA.
DR EMBL; AK074898; BAC11277.1; -; mRNA.
DR EMBL; AK299234; BAG61266.1; -; mRNA.
DR EMBL; AC011846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019873; AAH19873.1; -; mRNA.
DR EMBL; BC035508; AAH35508.1; -; mRNA.
DR EMBL; BC047685; AAH47685.1; -; mRNA.
DR EMBL; BC058912; AAH58912.1; -; mRNA.
DR EMBL; DQ251107; ABB83547.1; -; Genomic_DNA.
DR CCDS; CCDS45282.1; -. [Q9P035-1]
DR RefSeq; NP_057479.2; NM_016395.2. [Q9P035-1]
DR AlphaFoldDB; Q9P035; -.
DR SMR; Q9P035; -.
DR BioGRID; 119570; 198.
DR IntAct; Q9P035; 79.
DR MINT; Q9P035; -.
DR STRING; 9606.ENSP00000261875; -.
DR SwissLipids; SLP:000000439; -.
DR GlyGen; Q9P035; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P035; -.
DR PhosphoSitePlus; Q9P035; -.
DR SwissPalm; Q9P035; -.
DR BioMuta; HACD3; -.
DR DMDM; 166199462; -.
DR EPD; Q9P035; -.
DR jPOST; Q9P035; -.
DR MassIVE; Q9P035; -.
DR MaxQB; Q9P035; -.
DR PaxDb; Q9P035; -.
DR PeptideAtlas; Q9P035; -.
DR PRIDE; Q9P035; -.
DR ProteomicsDB; 4949; -.
DR ProteomicsDB; 83540; -. [Q9P035-1]
DR TopDownProteomics; Q9P035-1; -. [Q9P035-1]
DR Antibodypedia; 7067; 117 antibodies from 18 providers.
DR DNASU; 51495; -.
DR Ensembl; ENST00000261875.10; ENSP00000261875.5; ENSG00000074696.13. [Q9P035-1]
DR Ensembl; ENST00000442729.6; ENSP00000392491.2; ENSG00000074696.13. [Q9P035-2]
DR GeneID; 51495; -.
DR KEGG; hsa:51495; -.
DR MANE-Select; ENST00000261875.10; ENSP00000261875.5; NM_016395.4; NP_057479.2.
DR UCSC; uc002apc.4; human. [Q9P035-1]
DR CTD; 51495; -.
DR DisGeNET; 51495; -.
DR GeneCards; HACD3; -.
DR HGNC; HGNC:24175; HACD3.
DR HPA; ENSG00000074696; Low tissue specificity.
DR MIM; 615940; gene.
DR neXtProt; NX_Q9P035; -.
DR OpenTargets; ENSG00000074696; -.
DR PharmGKB; PA142671113; -.
DR VEuPathDB; HostDB:ENSG00000074696; -.
DR eggNOG; KOG3187; Eukaryota.
DR GeneTree; ENSGT00530000062962; -.
DR HOGENOM; CLU_046712_0_0_1; -.
DR InParanoid; Q9P035; -.
DR OMA; SYLVMSH; -.
DR OrthoDB; 1458293at2759; -.
DR PhylomeDB; Q9P035; -.
DR TreeFam; TF313326; -.
DR PathwayCommons; Q9P035; -.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SABIO-RK; Q9P035; -.
DR SignaLink; Q9P035; -.
DR SIGNOR; Q9P035; -.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 51495; 5 hits in 1019 CRISPR screens.
DR ChiTaRS; HACD3; human.
DR GeneWiki; PTPLAD1; -.
DR GenomeRNAi; 51495; -.
DR Pharos; Q9P035; Tbio.
DR PRO; PR:Q9P035; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9P035; protein.
DR Bgee; ENSG00000074696; Expressed in pons and 190 other tissues.
DR ExpressionAtlas; Q9P035; baseline and differential.
DR Genevisible; Q9P035; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0102343; F:3-hydroxy-arachidoyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0102344; F:3-hydroxy-behenoyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0102345; F:3-hydroxy-lignoceroyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0102158; F:very-long-chain 3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0030497; P:fatty acid elongation; IDA:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:ProtInc.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; IMP:AgBase.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IMP:AgBase.
DR GO; GO:0016601; P:Rac protein signal transduction; NAS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:ProtInc.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR11035; PTHR11035; 1.
DR Pfam; PF04387; PTPLA; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..362
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT 3"
FT /id="PRO_0000313724"
FT TOPO_DOM 1..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..185
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..241
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..322
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 5..94
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT COILED 111..136
FT /evidence="ECO:0000255"
FT ACT_SITE 286
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 293
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 69..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056070"
FT VARIANT 56
FT /note="E -> K (in dbSNP:rs11632737)"
FT /id="VAR_037712"
FT VARIANT 269
FT /note="M -> L (in dbSNP:rs2279854)"
FT /id="VAR_037713"
FT CONFLICT 60
FT /note="E -> K (in Ref. 3; BAB55101)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="F -> I (in Ref. 3; BAC11277)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="W -> G (in Ref. 5; AAH35508)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="A -> V (in Ref. 2; AAF29085)"
FT /evidence="ECO:0000305"
FT CONFLICT 352..362
FT /note="RRYGQKKKKIH -> LKMRAGAVAHACDPSALGG (in Ref. 1;
FT CAB69070)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="I -> K (in Ref. 5; AAH35508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 43160 MW; 1B3591E88DD85D16 CRC64;
MENQVLTPHV YWAQRHRELY LRVELSDVQN PAISITENVL HFKAQGHGAK GDNVYEFHLE
FLDLVKPEPV YKLTQRQVNI TVQKKVSQWW ERLTKQEKRP LFLAPDFDRW LDESDAEMEL
RAKEEERLNK LRLESEGSPE TLTNLRKGYL FMYNLVQFLG FSWIFVNLTV RFCILGKESF
YDTFHTVADM MYFCQMLAVV ETINAAIGVT TSPVLPSLIQ LLGRNFILFI IFGTMEEMQN
KAVVFFVFYL WSAIEIFRYS FYMLTCIDMD WKVLTWLRYT LWIPLYPLGC LAEAVSVIQS
IPIFNETGRF SFTLPYPVKI KVRFSFFLQI YLIMIFLGLY INFRHLYKQR RRRYGQKKKK
IH
