HIBC4_ARATH
ID HIBC4_ARATH Reviewed; 401 AA.
AC Q5XF59; Q2V3M8; Q9M208;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=3-hydroxyisobutyryl-CoA hydrolase-like protein 1, mitochondrial;
DE EC=3.1.2.-;
DE Flags: Precursor;
GN OrderedLocusNames=At3g60510; ORFNames=T8B10.170;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY.
RX PubMed=11404361; DOI=10.1074/jbc.m104679200;
RA Zolman B.K., Monroe-Augustus M., Thompson B., Hawes J.W., Krukenberg K.A.,
RA Matsuda S.P., Bartel B.;
RT "chy1, an Arabidopsis mutant with impaired beta-oxidation, is defective in
RT a peroxisomal beta-hydroxyisobutyryl-CoA hydrolase.";
RL J. Biol. Chem. 276:31037-31046(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP CYS-26.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:25732537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5XF59-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XF59-2; Sequence=VSP_038865, VSP_038866;
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81837.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL138646; CAB81837.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80071.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80072.1; -; Genomic_DNA.
DR EMBL; BT015757; AAU90047.1; -; mRNA.
DR EMBL; BT020182; AAV43784.1; -; mRNA.
DR EMBL; AK229190; BAF01060.1; -; mRNA.
DR PIR; T47862; T47862.
DR RefSeq; NP_001030902.1; NM_001035825.2. [Q5XF59-2]
DR RefSeq; NP_191610.3; NM_115915.5. [Q5XF59-1]
DR AlphaFoldDB; Q5XF59; -.
DR SMR; Q5XF59; -.
DR STRING; 3702.AT3G60510.3; -.
DR PRIDE; Q5XF59; -.
DR ProteomicsDB; 230206; -. [Q5XF59-1]
DR EnsemblPlants; AT3G60510.1; AT3G60510.1; AT3G60510. [Q5XF59-1]
DR EnsemblPlants; AT3G60510.2; AT3G60510.2; AT3G60510. [Q5XF59-2]
DR GeneID; 825222; -.
DR Gramene; AT3G60510.1; AT3G60510.1; AT3G60510. [Q5XF59-1]
DR Gramene; AT3G60510.2; AT3G60510.2; AT3G60510. [Q5XF59-2]
DR KEGG; ath:AT3G60510; -.
DR Araport; AT3G60510; -.
DR eggNOG; KOG1684; Eukaryota.
DR HOGENOM; CLU_009834_22_1_1; -.
DR InParanoid; Q5XF59; -.
DR OMA; CFRMELA; -.
DR PhylomeDB; Q5XF59; -.
DR BioCyc; ARA:AT3G60510-MON; -.
DR PRO; PR:Q5XF59; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q5XF59; baseline and differential.
DR Genevisible; Q5XF59; AT.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR045004; ECH_dom.
DR InterPro; IPR032259; HIBYL-CoA-H.
DR PANTHER; PTHR43176; PTHR43176; 1.
DR Pfam; PF16113; ECH_2; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 27..401
FT /note="3-hydroxyisobutyryl-CoA hydrolase-like protein 1,
FT mitochondrial"
FT /id="PRO_0000392980"
FT VAR_SEQ 316..317
FT /note="IR -> LL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038865"
FT VAR_SEQ 318..401
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038866"
SQ SEQUENCE 401 AA; 44763 MW; E4FB069151825ED1 CRC64;
MHNAKGLLGR IVRDKLWRFG YRRSLCSLKL TSEDLDYQVL VEGSGCSRTA ILNRPPALNA
LTTHMGYRLQ KLYKNWEEDP NIGFVMMKGS GRAFCAGGDI VSLYHLRTRG SPDAIREFFS
SLYSFIYLLG TYLKPHVAIL NGVTMGGGTG VSIPGTFRVA TDRTIFATPE TIIGFHPDAG
ASFNLSHLPG RLGEYLGLTG LKLSGAEMLA CGLATHYIRS EEVPVMEEQL KKLLTDDPSV
VESCLEKCAE VAHPEKTGVI RRIDLLEKCF SHDTVEEIID SLEIEASRRK DTWCITTLRR
LKESSPLSLK VALRSIREGR LQTLDQCLIR EYRMSLQGLI GPMSGNFCEG VRARLIDKDE
APKWDPPSLE KVSEDMVDDY FCALTPTEPD LDLPVKLRES I
