ID   J3KS69_HUMAN            Unreviewed;       174 AA.
AC   J3KS69;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   22-NOV-2017, entry version 30.
DE   RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase {ECO:0000256|RuleBase:RU363109};
DE            EC=4.2.1.134 {ECO:0000256|RuleBase:RU363109};
DE   Flags: Fragment;
GN   Name=HACD1 {ECO:0000313|Ensembl:ENSP00000462336};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000462336, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Proteomes:UP000005640}
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.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R., Hubbard T.,
RA   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   [2] {ECO:0000313|Ensembl:ENSP00000462336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [3] {ECO:0000313|Ensembl:ENSP00000462336}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2012) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the third of the four reactions of the long-
CC       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.
CC       This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA
CC       intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty
CC       acid elongation. Thereby, it participates to the production of
CC       VLCFAs of different chain lengths that are involved in multiple
CC       biological processes as precursors of membrane lipids and lipid
CC       mediators. {ECO:0000256|RuleBase:RU363109}.
CC   -!- CATALYTIC ACTIVITY: A very-long-chain (3R)-3-hydroxyacyl-CoA = a
CC       very-long-chain trans-2,3-dehydroacyl-CoA + H(2)O.
CC       {ECO:0000256|RuleBase:RU363109}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|RuleBase:RU363109}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU363109}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU363109}.
CC   -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase
CC       HACD family. {ECO:0000256|RuleBase:RU363109}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|RuleBase:RU363109}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSP00000462336}.
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DR   EMBL; AC069542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; J3KS69; -.
DR   PaxDb; J3KS69; -.
DR   PeptideAtlas; J3KS69; -.
DR   Ensembl; ENST00000466335; ENSP00000462336; ENSG00000165996.
DR   UCSC; uc057sbo.1; human.
DR   EuPathDB; HostDB:ENSG00000165996.13; -.
DR   HGNC; HGNC:9639; HACD1.
DR   OpenTargets; ENSG00000165996; -.
DR   eggNOG; KOG3187; Eukaryota.
DR   eggNOG; COG5198; LUCA.
DR   GeneTree; ENSGT00530000062962; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   Bgee; ENSG00000165996; -.
DR   ExpressionAtlas; J3KS69; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0102158; F:very-long-chain 3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR   PANTHER; PTHR11035; PTHR11035; 1.
DR   Pfam; PF04387; PTPLA; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU363109};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU363109};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU363109};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU363109};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU363109};
KW   Lyase {ECO:0000256|RuleBase:RU363109};
KW   Membrane {ECO:0000256|RuleBase:RU363109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Transmembrane {ECO:0000256|RuleBase:RU363109};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363109}.
FT   TRANSMEM     42     65       Helical. {ECO:0000256|RuleBase:RU363109}.
FT   TRANSMEM     86    106       Helical. {ECO:0000256|RuleBase:RU363109}.
FT   NON_TER       1      1       {ECO:0000313|Ensembl:ENSP00000462336}.
SQ   SEQUENCE   174 AA;  19719 MW;  64B1506E9B193B80 CRC64;
     XCAATMASSD EDGTNGGASE AGEDREAPGE RRRLGVLATA WLTFYDIAMT AGWLVLAIAM
     VRFYMEKGTH RGLYKSIQKT LKFFQTFALL EIVHCLIGIV PTSVIVTGVQ VSSRIFMVWL
     ITHSIKPIQN EESVVLFLVA WTVTEITRYS FYTFSLLDHL PYFIKWARWR YLAV
//