HACD1_HUMAN
ID HACD1_HUMAN Reviewed; 288 AA.
AC B0YJ81; B0YJ80; Q6JIC5; Q96FW7; Q9HB93; Q9UHX2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1 {ECO:0000305};
DE EC=4.2.1.134 {ECO:0000269|PubMed:18554506, ECO:0000269|PubMed:23933735};
DE AltName: Full=3-hydroxyacyl-CoA dehydratase 1 {ECO:0000303|PubMed:18554506};
DE Short=HACD1 {ECO:0000303|PubMed:15164054};
DE AltName: Full=Cementum-attachment protein {ECO:0000303|PubMed:22067203};
DE Short=CAP {ECO:0000303|PubMed:22067203};
DE AltName: Full=Protein-tyrosine phosphatase-like member A {ECO:0000312|HGNC:HGNC:9639};
GN Name=HACD1 {ECO:0000303|PubMed:15164054, ECO:0000312|HGNC:HGNC:9639};
GN Synonyms=PTPLA;
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 [GENOMIC DNA], VARIANTS LYS-64; GLN-64; PHE-70 AND
RP TYR-227, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11054553; DOI=10.1016/s0378-1119(00)00347-4;
RA Li D., Gonzalez O., Bachinski L.L., Roberts R.;
RT "Human protein tyrosine phosphatase-like gene: expression profile, genomic
RT structure, and mutation analysis in families with ARVD.";
RL Gene 256:237-243(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LYS-64 AND TYR-227.
RX PubMed=10644438; DOI=10.1006/geno.1999.5950;
RA Uwanogho D.A., Hardcastle Z., Balogh P., Mirza G., Thornburg K.L.,
RA Ragoussis J., Sharpe P.T.;
RT "Molecular cloning, chromosomal mapping, and developmental expression of a
RT novel protein tyrosine phosphatase-like gene.";
RL Genomics 62:406-416(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), AND TISSUE
RP SPECIFICITY.
RX PubMed=22067203; DOI=10.1177/0022034511428155;
RA Valdes De Hoyos A., Hoz-Rodriguez L., Arzate H., Narayanan A.S.;
RT "Isolation of protein-tyrosine phosphatase-like member-a variant from
RT cementum.";
RL J. Dent. Res. 91:203-209(2012).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LYS-64 AND
RP PHE-70.
RC TISSUE=Skeletal muscle;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-288 (ISOFORM 1).
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP 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 [10]
RP INVOLVEMENT IN CFTD, GLYCOSYLATION, AND CATALYTIC ACTIVITY.
RX PubMed=23933735; DOI=10.1093/hmg/ddt380;
RA Muhammad E., Reish O., Ohno Y., Scheetz T., Deluca A., Searby C., Regev M.,
RA Benyamini L., Fellig Y., Kihara A., Sheffield V.C., Parvari R.;
RT "Congenital myopathy is caused by mutation of HACD1.";
RL Hum. Mol. Genet. 22:5229-5236(2013).
RN [11]
RP FUNCTION (ISOFORM 2), AND SUBUNIT (ISOFORM 2).
RX PubMed=25263524; DOI=10.1016/j.bone.2014.09.014;
RA Montoya G., Arenas J., Romo E., Zeichner-David M., Alvarez M.,
RA Narayanan A.S., Velazquez U., Mercado G., Arzate H.;
RT "Human recombinant cementum attachment protein (hrPTPLa/CAP) promotes
RT hydroxyapatite crystal formation in vitro and bone healing in vivo.";
RL Bone 69:154-164(2014).
CC -!- FUNCTION: [Isoform 1]: Catalyzes the third of the four reactions of the
CC long-chain fatty acids elongation cycle. This endoplasmic reticulum-
CC bound enzymatic process, allows the addition of two carbons to the
CC chain of long- and very long-chain fatty acids/VLCFAs per cycle. This
CC enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate
CC into 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.
CC {ECO:0000269|PubMed:18554506}.
CC -!- FUNCTION: [Isoform 2]: In tooth development, may play a role in the
CC recruitment and the differentiation of cells that contribute to
CC cementum formation. May also bind hydroxyapatite and regulate its
CC crystal nucleation to form cementum. {ECO:0000269|PubMed:22067203}.
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, ECO:0000269|PubMed:23933735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45813;
CC Evidence={ECO:0000305};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyoctadecanoyl-CoA = (2E)-octadecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39155, ChEBI:CHEBI:15377, ChEBI:CHEBI:71412,
CC ChEBI:CHEBI:76374; Evidence={ECO:0000269|PubMed:18554506};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39156;
CC Evidence={ECO:0000305|PubMed:18554506};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyeicosanoyl-CoA = (2E)-eicosenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39175, ChEBI:CHEBI:15377, ChEBI:CHEBI:74691,
CC ChEBI:CHEBI:76373; Evidence={ECO:0000269|PubMed:18554506};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39176;
CC Evidence={ECO:0000305|PubMed:18554506};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxydocosanoyl-CoA = (2E)-docosenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39187, ChEBI:CHEBI:15377, ChEBI:CHEBI:74692,
CC ChEBI:CHEBI:76375; Evidence={ECO:0000269|PubMed:18554506};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39188;
CC Evidence={ECO:0000305|PubMed:18554506};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxytetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39199, ChEBI:CHEBI:15377, ChEBI:CHEBI:74693,
CC ChEBI:CHEBI:76377; Evidence={ECO:0000269|PubMed:18554506};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39200;
CC Evidence={ECO:0000305|PubMed:18554506};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexacosanoyl-CoA = (2E)-hexacosenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39211, ChEBI:CHEBI:15377, ChEBI:CHEBI:74281,
CC ChEBI:CHEBI:76378; Evidence={ECO:0000269|PubMed:18554506};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39212;
CC Evidence={ECO:0000305|PubMed:18554506};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33.6 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: Isoform 1: May interact with enzymes of the ELO family
CC (including ELOVL1); with those enzymes that mediate condensation, the
CC first of the four steps of the reaction cycle responsible for fatty
CC acids elongation, may be part of a larger fatty acids elongase complex
CC (PubMed:18554506). Isoform 2: Homooligomer. Self-assembles into spheres
CC which then aggregates to form strings and a meshwork that may support
CC hydroxyapatite crystal nucleation (PubMed:25263524).
CC {ECO:0000269|PubMed:18554506, ECO:0000269|PubMed:25263524}.
CC -!- INTERACTION:
CC B0YJ81; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-12051643, EBI-18013275;
CC B0YJ81; Q13651: IL10RA; NbExp=3; IntAct=EBI-12051643, EBI-1031656;
CC B0YJ81; Q96K19-5: RNF170; NbExp=3; IntAct=EBI-12051643, EBI-12055631;
CC B0YJ81; Q9NZ01: TECR; NbExp=3; IntAct=EBI-12051643, EBI-2877718;
CC B0YJ81; Q9BVX2: TMEM106C; NbExp=4; IntAct=EBI-12051643, EBI-2821497;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: 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=B0YJ81-1; Sequence=Displayed;
CC Name=2; Synonyms=CAP, cementum-attachment protein, PTPLA-CAP
CC {ECO:0000303|PubMed:22067203};
CC IsoId=B0YJ81-2; Sequence=VSP_035363, VSP_035364;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in the myocardium,
CC and to a lesser extent in skeletal and smooth muscular tissues
CC including those from stomach, jejunum, and bladder. Also detected in
CC gingival fibroblasts, periodontal ligament cells, osteoblasts and
CC cementoblasts (PubMed:11054553, PubMed:22067203). Isoform 2 is
CC specifically expressed by cementoblasts but also detected in
CC periodontal ligament cells, heart, liver and kidney (at protein level)
CC (PubMed:22067203). {ECO:0000269|PubMed:11054553,
CC ECO:0000269|PubMed:22067203}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is expressed in fetal heart.
CC {ECO:0000269|PubMed:11054553}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:23933735}.
CC -!- DISEASE: Myopathy, congenital, with fiber-type disproportion (CFTD)
CC [MIM:255310]: A genetically heterogeneous disorder in which there is
CC relative hypotrophy of type 1 muscle fibers compared to type 2 fibers
CC on skeletal muscle biopsy. However, these findings are not specific and
CC can be found in many different myopathic and neuropathic conditions.
CC {ECO:0000269|PubMed:23933735}. Note=The gene represented in this entry
CC may be involved in disease pathogenesis. A loss-of-function mutation
CC that segregates with the disease was found in four members of a
CC consanguineous family and not identified in unaffected controls. The
CC mutation affects the expression of the mRNA and the produced protein is
CC catalytically inactive. {ECO:0000269|PubMed:23933735}.
CC -!- MISCELLANEOUS: [Isoform 2]: Catalytically inactive since it lacks the
CC active site but may have an alternative function.
CC {ECO:0000269|PubMed:22067203}.
CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD
CC family. {ECO:0000305}.
CC -!- CAUTION: Isoform 1 shares some similarity with tyrosine phosphatase
CC proteins but it has probably no phosphatase activity.
CC {ECO:0000250|UniProtKB:Q6Y1H2, ECO:0000305|PubMed:18554506}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG10713.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACA06059.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF266852; AAG10713.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF266848; AAG10713.1; JOINED; Genomic_DNA.
DR EMBL; AF266849; AAG10713.1; JOINED; Genomic_DNA.
DR EMBL; AF266850; AAG10713.1; JOINED; Genomic_DNA.
DR EMBL; AF266851; AAG10713.1; JOINED; Genomic_DNA.
DR EMBL; AF114494; AAF21976.1; -; mRNA.
DR EMBL; AY455942; AAR22554.1; -; mRNA.
DR EMBL; EF445016; ACA06059.1; ALT_INIT; Genomic_DNA.
DR EMBL; EF445016; ACA06060.1; -; Genomic_DNA.
DR EMBL; EF445016; ACA06061.1; -; Genomic_DNA.
DR EMBL; AC069542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010353; AAH10353.1; -; mRNA.
DR EMBL; CR608689; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS7121.1; -. [B0YJ81-1]
DR RefSeq; NP_055056.3; NM_014241.3. [B0YJ81-1]
DR AlphaFoldDB; B0YJ81; -.
DR BioGRID; 114634; 26.
DR IntAct; B0YJ81; 21.
DR STRING; 9606.ENSP00000355308; -.
DR SwissLipids; SLP:000000435; -.
DR GlyGen; B0YJ81; 1 site.
DR iPTMnet; B0YJ81; -.
DR PhosphoSitePlus; B0YJ81; -.
DR BioMuta; HACD1; -.
DR EPD; B0YJ81; -.
DR jPOST; B0YJ81; -.
DR MassIVE; B0YJ81; -.
DR MaxQB; B0YJ81; -.
DR PaxDb; B0YJ81; -.
DR PeptideAtlas; B0YJ81; -.
DR PRIDE; B0YJ81; -.
DR ProteomicsDB; 2882; -. [B0YJ81-1]
DR ProteomicsDB; 2883; -. [B0YJ81-2]
DR Antibodypedia; 57457; 63 antibodies from 14 providers.
DR DNASU; 9200; -.
DR Ensembl; ENST00000361271.8; ENSP00000355308.3; ENSG00000165996.14. [B0YJ81-1]
DR GeneID; 9200; -.
DR KEGG; hsa:9200; -.
DR MANE-Select; ENST00000361271.8; ENSP00000355308.3; NM_014241.4; NP_055056.3.
DR UCSC; uc001ipg.4; human. [B0YJ81-1]
DR CTD; 9200; -.
DR DisGeNET; 9200; -.
DR GeneCards; HACD1; -.
DR HGNC; HGNC:9639; HACD1.
DR HPA; ENSG00000165996; Tissue enhanced (heart).
DR MalaCards; HACD1; -.
DR MIM; 255310; phenotype.
DR MIM; 610467; gene.
DR neXtProt; NX_B0YJ81; -.
DR OpenTargets; ENSG00000165996; -.
DR Orphanet; 2020; Congenital fiber-type disproportion myopathy.
DR PharmGKB; PA33982; -.
DR VEuPathDB; HostDB:ENSG00000165996; -.
DR eggNOG; KOG3187; Eukaryota.
DR GeneTree; ENSGT00530000062962; -.
DR HOGENOM; CLU_034302_2_0_1; -.
DR InParanoid; B0YJ81; -.
DR OMA; TKLYLFA; -.
DR OrthoDB; 1458293at2759; -.
DR PhylomeDB; B0YJ81; -.
DR TreeFam; TF313326; -.
DR PathwayCommons; B0YJ81; -.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SABIO-RK; B0YJ81; -.
DR SignaLink; B0YJ81; -.
DR SIGNOR; B0YJ81; -.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 9200; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; HACD1; human.
DR GenomeRNAi; 9200; -.
DR Pharos; B0YJ81; Tbio.
DR PRO; PR:B0YJ81; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; B0YJ81; protein.
DR Bgee; ENSG00000165996; Expressed in heart right ventricle and 178 other tissues.
DR ExpressionAtlas; B0YJ81; baseline and differential.
DR Genevisible; B0YJ81; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
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:0080023; F:3R-hydroxyacyl-CoA dehydratase activity; EXP:Reactome.
DR GO; GO:0019899; F:enzyme binding; IDA:UniProtKB.
DR GO; GO:0046848; F:hydroxyapatite binding; IDA:UniProtKB.
DR GO; GO:0102158; F:very-long-chain 3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0071529; P:cementum mineralization; IDA:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; IDA:UniProtKB.
DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IGI:UniProtKB.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR11035; PTHR11035; 1.
DR Pfam; PF04387; PTPLA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Endoplasmic reticulum;
KW Fatty acid biosynthesis; Fatty acid metabolism; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..288
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT 1"
FT /id="PRO_0000349315"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..114
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..165
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..251
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 210
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 217
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 126..140
FT /note="IVHCLIGIVPTSVIV -> VSFPSCCFSIAVIFM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:22067203"
FT /id="VSP_035363"
FT VAR_SEQ 141..288
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:22067203"
FT /id="VSP_035364"
FT VARIANT 64
FT /note="E -> K (in dbSNP:rs7895850)"
FT /evidence="ECO:0000269|PubMed:10644438,
FT ECO:0000269|PubMed:11054553, ECO:0000269|PubMed:15489334"
FT /id="VAR_046366"
FT VARIANT 64
FT /note="E -> Q (in dbSNP:rs7895850)"
FT /evidence="ECO:0000269|PubMed:11054553"
FT /id="VAR_046367"
FT VARIANT 70
FT /note="V -> F (in dbSNP:rs11254692)"
FT /evidence="ECO:0000269|PubMed:11054553,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_046368"
FT VARIANT 227
FT /note="H -> Y (in dbSNP:rs1053926)"
FT /evidence="ECO:0000269|PubMed:10644438,
FT ECO:0000269|PubMed:11054553"
FT /id="VAR_046369"
FT CONFLICT 80
FT /note="D -> N (in Ref. 2; AAF21976)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 32388 MW; 1CB64F23C3907F6E CRC64;
MGRLTEAAAA GSGSRAAGWA GSPPTLLPLS PTSPRCAATM ASSDEDGTNG GASEAGEDRE
APGERRRLGV LATAWLTFYD IAMTAGWLVL AIAMVRFYME KGTHRGLYKS IQKTLKFFQT
FALLEIVHCL IGIVPTSVIV TGVQVSSRIF MVWLITHSIK PIQNEESVVL FLVAWTVTEI
TRYSFYTFSL LDHLPYFIKW ARYNFFIILY PVGVAGELLT IYAALPHVKK TGMFSIRLPN
KYNVSFDYYY FLLITMASYI PLFPQLYFHM LRQRRKVLHG EVIVEKDD
