ID A0A132AMA7_SARSC Unreviewed; 276 AA.
AC A0A132AMA7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase {ECO:0000256|ARBA:ARBA00013122};
DE EC=4.2.1.134 {ECO:0000256|ARBA:ARBA00013122};
DE AltName: Full=Protein-tyrosine phosphatase-like A domain-containing protein 1 {ECO:0000256|ARBA:ARBA00030687};
GN ORFNames=QR98_0103100 {ECO:0000313|EMBL:KPM11735.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM11735.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM11735.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM11735.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the p23/wos2 family.
CC {ECO:0000256|ARBA:ARBA00025733}.
CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD
CC family. {ECO:0000256|ARBA:ARBA00007811}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPM11735.1}.
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DR EMBL; JXLN01017772; KPM11735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132AMA7; -.
DR VEuPathDB; VectorBase:SSCA001874; -.
DR OMA; DYEMINM; -.
DR OrthoDB; 2881070at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000616769; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:InterPro.
DR GO; GO:0102158; F:very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR045250; p23-like.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR22932:SF1; CO-CHAPERONE PROTEIN DAF-41; 1.
DR PANTHER; PTHR22932; TELOMERASE-BINDING PROTEIN P23 HSP90 CO-CHAPERONE; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF04387; PTPLA; 1.
DR SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR PROSITE; PS51203; CS; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 167..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 276 AA; 32333 MW; 6DFD7964C5F3033D CRC64;
MKKISSSLSP FVYWGQTSDS ITLIVDLKNV KSPKINLEDK SLDFQAVGLG AKGLNEYEIS
IVLHSEVVPE KSFYKITDRN VEFVLRKKMM ILWPKLLESN SKPQWLKVDF DRIKQDELET
TSNDESDLED ELNQFSSEFS SSRSRLYKDR NFGRGRKKRV QDFTTSYLFL YNLFQFVGFI
YIFVIILIHY LKEGPETIKT IYPSLKNPIK FLNLMQILEI LHPLFGYSSG SPMLPLFQLI
GRTFYLFILI DCNAELQSHW ATFYLLLIYT CSELFR
//
