HACL2_MOUSE
ID HACL2_MOUSE Reviewed; 632 AA.
AC Q8BU33; Q3UNZ4; Q3UZY5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=2-hydroxyacyl-CoA lyase 2;
DE EC=4.1.2.- {ECO:0000250|UniProtKB:A1L0T0};
DE AltName: Full=Acetolactate synthase-like protein;
DE AltName: Full=IlvB-like protein;
GN Name=Ilvbl; Synonyms=Hacl2 {ECO:0000250|UniProtKB:A1L0T0};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, Liver, Pituitary, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the
CC cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a
CC thiamine pyrophosphate (TPP)-dependent manner. Involved in the
CC phytosphingosine degradation pathway. {ECO:0000250|UniProtKB:A1L0T0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyoctadecanoyl-CoA = formyl-CoA + heptadecanal;
CC Xref=Rhea:RHEA:55196, ChEBI:CHEBI:57376, ChEBI:CHEBI:74116,
CC ChEBI:CHEBI:138631; Evidence={ECO:0000250|UniProtKB:A1L0T0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55197;
CC Evidence={ECO:0000250|UniProtKB:A1L0T0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-hydroxyhexadecanoyl-CoA = formyl-CoA + pentadecanal;
CC Xref=Rhea:RHEA:55212, ChEBI:CHEBI:17302, ChEBI:CHEBI:57376,
CC ChEBI:CHEBI:138654; Evidence={ECO:0000250|UniProtKB:A1L0T0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55213;
CC Evidence={ECO:0000250|UniProtKB:A1L0T0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8CHM7};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8CHM7};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:A1L0T0};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:A1L0T0}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BU33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BU33-2; Sequence=VSP_030393, VSP_030395;
CC Name=3;
CC IsoId=Q8BU33-3; Sequence=VSP_030392, VSP_030394;
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AK087956; BAC40057.1; -; mRNA.
DR EMBL; AK133553; BAE21720.1; -; mRNA.
DR EMBL; AK143918; BAE25603.1; -; mRNA.
DR EMBL; AK146075; BAE26879.1; -; mRNA.
DR EMBL; BC056459; AAH56459.1; -; mRNA.
DR CCDS; CCDS23966.1; -. [Q8BU33-1]
DR CCDS; CCDS88046.1; -. [Q8BU33-3]
DR RefSeq; NP_776112.1; NM_173751.4. [Q8BU33-1]
DR RefSeq; XP_011241702.1; XM_011243400.2. [Q8BU33-1]
DR RefSeq; XP_011241703.1; XM_011243401.1.
DR AlphaFoldDB; Q8BU33; -.
DR SMR; Q8BU33; -.
DR BioGRID; 229702; 4.
DR STRING; 10090.ENSMUSP00000101023; -.
DR iPTMnet; Q8BU33; -.
DR PhosphoSitePlus; Q8BU33; -.
DR SwissPalm; Q8BU33; -.
DR EPD; Q8BU33; -.
DR jPOST; Q8BU33; -.
DR MaxQB; Q8BU33; -.
DR PaxDb; Q8BU33; -.
DR PeptideAtlas; Q8BU33; -.
DR PRIDE; Q8BU33; -.
DR ProteomicsDB; 267127; -. [Q8BU33-1]
DR ProteomicsDB; 267128; -. [Q8BU33-2]
DR ProteomicsDB; 267129; -. [Q8BU33-3]
DR Antibodypedia; 26957; 334 antibodies from 22 providers.
DR DNASU; 216136; -.
DR Ensembl; ENSMUST00000105384; ENSMUSP00000101023; ENSMUSG00000032763. [Q8BU33-1]
DR Ensembl; ENSMUST00000218271; ENSMUSP00000151480; ENSMUSG00000032763. [Q8BU33-3]
DR Ensembl; ENSMUST00000218885; ENSMUSP00000151263; ENSMUSG00000032763. [Q8BU33-1]
DR Ensembl; ENSMUST00000220430; ENSMUSP00000151674; ENSMUSG00000032763. [Q8BU33-2]
DR GeneID; 216136; -.
DR KEGG; mmu:216136; -.
DR UCSC; uc007fxv.2; mouse. [Q8BU33-1]
DR UCSC; uc007fxw.1; mouse. [Q8BU33-2]
DR CTD; 10994; -.
DR MGI; MGI:1351911; Ilvbl.
DR VEuPathDB; HostDB:ENSMUSG00000032763; -.
DR eggNOG; KOG1185; Eukaryota.
DR GeneTree; ENSGT00940000158035; -.
DR HOGENOM; CLU_013748_3_3_1; -.
DR InParanoid; Q8BU33; -.
DR OMA; CFGTSGP; -.
DR OrthoDB; 1132247at2759; -.
DR PhylomeDB; Q8BU33; -.
DR TreeFam; TF354221; -.
DR BioGRID-ORCS; 216136; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q8BU33; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BU33; protein.
DR Bgee; ENSMUSG00000032763; Expressed in jejunum and 244 other tissues.
DR ExpressionAtlas; Q8BU33; baseline and differential.
DR Genevisible; Q8BU33; MM.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; ISS:UniProtKB.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Fatty acid metabolism;
KW Lipid metabolism; Lyase; Magnesium; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Thiamine pyrophosphate; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..632
FT /note="2-hydroxyacyl-CoA lyase 2"
FT /id="PRO_0000314826"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 470..550
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 98
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 521
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT BINDING 547
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P40149"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 396..401
FT /note="GDVGSF -> AGPASP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030392"
FT VAR_SEQ 397..416
FT /note="DVGSFMIKLVEGLQGQMWSS -> ECTPRDPTMCMVSSSCLCCI (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030393"
FT VAR_SEQ 402..632
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030394"
FT VAR_SEQ 417..632
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030395"
SQ SEQUENCE 632 AA; 68156 MW; 02B5C5ED36ECDE89 CRC64;
METSAAAASA GGFFPSFLLL AFGTLVAAVL GVAHRLGLFY QLMHKVDKTS IRHGGESVAA
VLRAHGVRFV FTLVGGHISP LLVACEKLGI RVVDTRHEVT AVFAADAVAR LTGTVGVAAV
TAGPGLTNTV TAVKNAQVAQ SPVLLLGGAA STLLQKRGAL QAIDQMSLFR PLCKFCASVR
RVRDIVPTLR TAIAAAQSGT PGPVFVELPL DVLYPYFMVE KEMIPTKLPN SLMGRVVVWY
LQNCLANLFV GAWEPRPEGP LPLDIPQASP QQVQRCVEIL SRAKRPLLVL GSQALLPPTP
ANKLRAAVET LGVPCFLGGM SRGLLGRNHP LHIRQNRSAA LKKADVVVLA GAVCDFRLSY
GRVLNRKSSI IIVNRNRDDL LLNSDIFWKP QEAVQGDVGS FMIKLVEGLQ GQMWSSDWAE
ELRKADQQKE QTYRDKALMP VLQHLNPVWV LQQVEETLPD NALLVVDGGD FVATAAYLVQ
PRGPLRWLDP GAFGTLGVGA GFALGAKLCQ PEAEVWCLFG DGAFGYSLIE FDTFVRHKVP
VIALVGNDAG WTQISREQVP RLGSDVACSL AYTDYHKAAM GLGAQGLILS RDNKDQVVKV
LREGQQLCQD GHAVVVNILI GRTDFRDGSI SV
