HACD2_HUMAN
ID HACD2_HUMAN Reviewed; 254 AA.
AC Q6Y1H2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2 {ECO:0000305};
DE EC=4.2.1.134 {ECO:0000269|PubMed:18554506};
DE AltName: Full=3-hydroxyacyl-CoA dehydratase 2 {ECO:0000303|PubMed:18554506};
DE Short=HACD2 {ECO:0000303|PubMed:18554506};
DE AltName: Full=Protein-tyrosine phosphatase-like member B {ECO:0000312|HGNC:HGNC:9640};
GN Name=HACD2 {ECO:0000303|PubMed:18554506, ECO:0000312|HGNC:HGNC:9640};
GN Synonyms=PTPLB {ECO:0000305};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INTERACTION WITH BCAP31, MUTAGENESIS OF PRO-101, AND CAUTION.
RX PubMed=15024066; DOI=10.1128/mcb.24.7.2767-2778.2004;
RA Wang B., Pelletier J., Massaad M.J., Herscovics A., Shore G.C.;
RT "The yeast split-ubiquitin membrane protein two-hybrid screen identifies
RT BAP31 as a regulator of the turnover of endoplasmic reticulum-associated
RT protein tyrosine phosphatase-like B.";
RL Mol. Cell. Biol. 24:2767-2778(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
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 [5]
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP IDENTIFICATION BY 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 [10]
RP ACETYLATION AT ALA-2.
RX PubMed=25732826; DOI=10.1016/j.celrep.2015.01.053;
RA Aksnes H., Van Damme P., Goris M., Starheim K.K., Marie M., Stoeve S.I.,
RA Hoel C., Kalvik T.V., Hole K., Glomnes N., Furnes C., Ljostveit S.,
RA Ziegler M., Niere M., Gevaert K., Arnesen T.;
RT "An organellar nalpha-acetyltransferase, naa60, acetylates cytosolic N
RT termini of transmembrane proteins and maintains Golgi integrity.";
RL Cell Rep. 10:1362-1374(2015).
CC -!- FUNCTION: Catalyzes the third of the very long-chain fatty acids
CC (VLCFA) elongation four-step cycle (condensation, reduction,
CC dehydration, and reduction). This endoplasmic reticulum-elongation
CC process is characterized by the addition of two carbons to the lipid
CC chain through each cycle. This enzyme catalyzes the dehydration of the
CC 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each
CC cycle of elongation. Therefore, it participates in the production of
CC various VLCFAs involved in multiple biological processes as precursors
CC of membrane lipids and lipid mediators. {ECO:0000269|PubMed:18554506}.
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 -!- 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=121.7 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 BCAP31 (PubMed:15024066).
CC {ECO:0000269|PubMed:15024066, ECO:0000269|PubMed:18554506}.
CC -!- INTERACTION:
CC Q6Y1H2; P51572: BCAP31; NbExp=4; IntAct=EBI-530257, EBI-77683;
CC Q6Y1H2; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-530257, EBI-6942903;
CC Q6Y1H2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-530257, EBI-18304435;
CC Q6Y1H2; Q13651: IL10RA; NbExp=3; IntAct=EBI-530257, EBI-1031656;
CC Q6Y1H2; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-530257, EBI-12188413;
CC Q6Y1H2; Q9NZ01: TECR; NbExp=7; IntAct=EBI-530257, EBI-2877718;
CC Q6Y1H2; Q9Y320: TMX2; NbExp=3; IntAct=EBI-530257, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15024066, ECO:0000269|PubMed:18554506}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:15024066,
CC ECO:0000269|PubMed:18554506}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, spleen, prostate, colon
CC and heart, followed by moderate expression in thymus, ovary, small
CC intestine, peripheral blood leukocytes, liver, skeletal muscle and
CC pancreas. Weakly detected in kidney, placenta, brain and lung.
CC {ECO:0000269|PubMed:15024066}.
CC -!- MISCELLANEOUS: Turns over rapidly through degradation by the proteasome
CC system. {ECO:0000269|PubMed:15024066}.
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:0000269|PubMed:15024066}.
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DR EMBL; AY191814; AAP20101.1; -; mRNA.
DR EMBL; AK289983; BAF82672.1; -; mRNA.
DR EMBL; AC020631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049369; AAH49369.1; -; mRNA.
DR EMBL; BC060839; AAH60839.1; -; mRNA.
DR CCDS; CCDS46895.1; -.
DR RefSeq; NP_940684.1; NM_198402.4.
DR AlphaFoldDB; Q6Y1H2; -.
DR BioGRID; 128393; 90.
DR IntAct; Q6Y1H2; 35.
DR STRING; 9606.ENSP00000373153; -.
DR SwissLipids; SLP:000000438; -.
DR GlyGen; Q6Y1H2; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q6Y1H2; -.
DR PhosphoSitePlus; Q6Y1H2; -.
DR SwissPalm; Q6Y1H2; -.
DR BioMuta; HACD2; -.
DR DMDM; 74738322; -.
DR EPD; Q6Y1H2; -.
DR jPOST; Q6Y1H2; -.
DR MassIVE; Q6Y1H2; -.
DR MaxQB; Q6Y1H2; -.
DR PaxDb; Q6Y1H2; -.
DR PeptideAtlas; Q6Y1H2; -.
DR PRIDE; Q6Y1H2; -.
DR ProteomicsDB; 67831; -.
DR TopDownProteomics; Q6Y1H2; -.
DR Antibodypedia; 32955; 93 antibodies from 16 providers.
DR DNASU; 201562; -.
DR Ensembl; ENST00000383657.10; ENSP00000373153.5; ENSG00000206527.10.
DR GeneID; 201562; -.
DR KEGG; hsa:201562; -.
DR MANE-Select; ENST00000383657.10; ENSP00000373153.5; NM_198402.5; NP_940684.1.
DR UCSC; uc003egj.3; human.
DR CTD; 201562; -.
DR DisGeNET; 201562; -.
DR GeneCards; HACD2; -.
DR HGNC; HGNC:9640; HACD2.
DR HPA; ENSG00000206527; Low tissue specificity.
DR MIM; 615939; gene.
DR neXtProt; NX_Q6Y1H2; -.
DR OpenTargets; ENSG00000206527; -.
DR PharmGKB; PA33983; -.
DR VEuPathDB; HostDB:ENSG00000206527; -.
DR eggNOG; KOG3187; Eukaryota.
DR GeneTree; ENSGT00530000062962; -.
DR HOGENOM; CLU_034302_2_0_1; -.
DR InParanoid; Q6Y1H2; -.
DR OMA; RADNGYG; -.
DR OrthoDB; 1458293at2759; -.
DR PhylomeDB; Q6Y1H2; -.
DR TreeFam; TF313326; -.
DR PathwayCommons; Q6Y1H2; -.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SABIO-RK; Q6Y1H2; -.
DR SignaLink; Q6Y1H2; -.
DR SIGNOR; Q6Y1H2; -.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 201562; 31 hits in 1077 CRISPR screens.
DR ChiTaRS; HACD2; human.
DR GenomeRNAi; 201562; -.
DR Pharos; Q6Y1H2; Tbio.
DR PRO; PR:Q6Y1H2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q6Y1H2; protein.
DR Bgee; ENSG00000206527; Expressed in gingival epithelium and 206 other tissues.
DR ExpressionAtlas; Q6Y1H2; baseline and differential.
DR Genevisible; Q6Y1H2; 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: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:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
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 Acetylation; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..254
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT 2"
FT /id="PRO_0000349319"
FT TOPO_DOM 2..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..79
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..130
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..217
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 11..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 183
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:25732826,
FT ECO:0007744|PubMed:19413330"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 101
FT /note="P->R: Does not restore any protein tyrosine
FT phosphatase activity."
FT /evidence="ECO:0000269|PubMed:15024066"
SQ SEQUENCE 254 AA; 28368 MW; 6B301176C696899E CRC64;
MAAVAATAAA KGNGGGGGRA GAGDASGTRK KKGPGPLATA YLVIYNVVMT AGWLVIAVGL
VRAYLAKGSY HSLYYSIEKP LKFFQTGALL EILHCAIGIV PSSVVLTSFQ VMSRVFLIWA
VTHSVKEVQS EDSVLLFVIA WTITEIIRYS FYTFSLLNHL PYLIKWARYT LFIVLYPMGV
SGELLTIYAA LPFVRQAGLY SISLPNKYNF SFDYYAFLIL IMISYIPIFP QLYFHMIHQR
RKILSHTEEH KKFE
