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   27-MAR-2024, entry version 170.
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; P13569: CFTR; NbExp=15; IntAct=EBI-359013, EBI-349854;
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; 243.
DR   IntAct; Q9P035; 90.
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; 9606-ENSP00000261875; -.
DR   PeptideAtlas; Q9P035; -.
DR   ProteomicsDB; 4949; -.
DR   ProteomicsDB; 83540; -. [Q9P035-1]
DR   Pumba; Q9P035; -.
DR   TopDownProteomics; Q9P035-1; -. [Q9P035-1]
DR   Antibodypedia; 7067; 126 antibodies from 19 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   AGR; HGNC:24175; -.
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; 2881070at2759; -.
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 1067 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 192 other cell types or tissues.
DR   ExpressionAtlas; Q9P035; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IBA:GO_Central.
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 (3R)-3-hydroxyacyl-CoA dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0007249; P:canonical NF-kappaB signal transduction; TAS:ProtInc.
DR   GO; GO:0030497; P:fatty acid elongation; IDA:UniProtKB.
DR   GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR   GO; GO:1902532; P:negative regulation of intracellular signal transduction; 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   CDD; cd06465; p23_hB-ind1_like; 1.
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; VERY-LONG-CHAIN (3R)-3-HYDROXYACYL-COA DEHYDRATASE; 1.
DR   PANTHER; PTHR11035:SF20; VERY-LONG-CHAIN (3R)-3-HYDROXYACYL-COA DEHYDRATASE 3; 1.
DR   Pfam; PF04387; PTPLA; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   PROSITE; PS51203; CS; 1.
DR   Genevisible; Q9P035; HS.
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
//