HACDB_ORYSJ
ID HACDB_ORYSJ Reviewed; 221 AA.
AC Q5ZEJ0; A0A0P0UY45; A2ZPA6; B9ESW4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PASTICCINO 2B {ECO:0000305};
DE EC=4.2.1.134 {ECO:0000250|UniProtKB:Q8VZB2};
DE AltName: Full=3-hydroxyacyl-CoA dehydratase PASTICCINO 2B;
DE Short=HACD;
DE Short=PAS2B;
DE AltName: Full=Protein tyrosine phosphatase-like protein;
GN Name=PAS2B; OrderedLocusNames=Os01g0150200, LOC_Os01g05694;
GN ORFNames=OsJ_000378, OsJ_00388, P0009G03.5;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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 an anti-
CC phosphatase that prevents CDKA-1 dephosphorylation and activation.
CC Involved in the hormonal control of cell division and differentiation.
CC Required for proliferation control of meristematic and non-meristematic
CC cells. Negative regulator of the cell cycle.
CC {ECO:0000250|UniProtKB:Q8VZB2}.
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:0000250|UniProtKB:Q8VZB2};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q8VZB2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEE53880.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002522; BAD61100.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF03946.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS70413.1; -; Genomic_DNA.
DR EMBL; CM000138; EEE53880.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK060935; BAG87629.1; -; mRNA.
DR EMBL; AK099465; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q5ZEJ0; -.
DR STRING; 4530.OS01T0150200-01; -.
DR PaxDb; Q5ZEJ0; -.
DR PRIDE; Q5ZEJ0; -.
DR EnsemblPlants; Os01t0150200-01; Os01t0150200-01; Os01g0150200.
DR EnsemblPlants; Os01t0150200-02; Os01t0150200-02; Os01g0150200.
DR Gramene; Os01t0150200-01; Os01t0150200-01; Os01g0150200.
DR Gramene; Os01t0150200-02; Os01t0150200-02; Os01g0150200.
DR eggNOG; KOG3187; Eukaryota.
DR HOGENOM; CLU_034302_0_0_1; -.
DR InParanoid; Q5ZEJ0; -.
DR OMA; TKLYLFA; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q5ZEJ0; OS.
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; IBA:GO_Central.
DR GO; GO:0102158; F:very-long-chain 3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR11035; PTHR11035; 1.
DR Pfam; PF04387; PTPLA; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Lyase;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..221
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT PASTICCINO 2B"
FT /id="PRO_0000372482"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..51
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..100
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..184
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 147
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 154
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT CONFLICT 31
FT /note="A -> T (in Ref. 6; AK099465)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 25017 MW; 92C56253A92265FC CRC64;
MTGVGSAVRR LYLSVYNWAV FFGWAQVLYY AVTTLLESGH EAVYAAVERP LQFAQTAAFL
EILHGLVGLV RSPVSATLPQ IGSRLFLTWG ILWSFPETHS HILVTSLVIS WSITEIIRYS
FFGMKETFGF APSWLLWLRY STFMVLYPTG ISSEVGLIYI ALPYMKATEK YCLRMPNKWN
FSFDFSYASI LSLAVYVPGS PHMFTYMLAQ RKKALAKAKA A
