ID HSDL2_MOUSE Reviewed; 490 AA.
AC Q2TPA8; Q3ULY5; Q3UVZ3; Q8C3H3; Q99LV2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=Hydroxysteroid dehydrogenase-like protein 2;
DE EC=1.-.-.-;
GN Name=Hsdl2;
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 [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J;
RX PubMed=16240713;
RA Dai J., Li P., Ji C., Feng C., Gui M., Sun Y., Zhang J., Zhu J., Dou C.,
RA Gu S.;
RT "Cloning and characterization of a novel mouse short-chain
RT dehydrogenase/reductases cDNA mHsdl2, encoding a protein with a SDR domain
RT and a SCP2 domain.";
RL Mol. Biol. (Mosk.) 39:799-805(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Heart, and Mammary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-390, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Has apparently no steroid dehydrogenase activity.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16240713}.
CC -!- INDUCTION: Up-regulated by cholesterol-rich food.
CC {ECO:0000269|PubMed:16240713}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39563.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY725196; AAU11505.1; -; mRNA.
DR EMBL; AK085899; BAC39563.1; ALT_FRAME; mRNA.
DR EMBL; AK136773; BAE23126.1; -; mRNA.
DR EMBL; AK145230; BAE26313.1; -; mRNA.
DR EMBL; AL806512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002211; AAH02211.1; -; mRNA.
DR CCDS; CCDS38772.1; -.
DR RefSeq; NP_077217.2; NM_024255.3.
DR AlphaFoldDB; Q2TPA8; -.
DR SMR; Q2TPA8; -.
DR BioGRID; 215391; 28.
DR IntAct; Q2TPA8; 1.
DR MINT; Q2TPA8; -.
DR STRING; 10090.ENSMUSP00000030078; -.
DR GlyGen; Q2TPA8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q2TPA8; -.
DR PhosphoSitePlus; Q2TPA8; -.
DR SwissPalm; Q2TPA8; -.
DR REPRODUCTION-2DPAGE; Q2TPA8; -.
DR EPD; Q2TPA8; -.
DR jPOST; Q2TPA8; -.
DR MaxQB; Q2TPA8; -.
DR PaxDb; 10090-ENSMUSP00000030078; -.
DR PeptideAtlas; Q2TPA8; -.
DR ProteomicsDB; 273388; -.
DR Pumba; Q2TPA8; -.
DR Antibodypedia; 29681; 175 antibodies from 24 providers.
DR DNASU; 72479; -.
DR Ensembl; ENSMUST00000030078.12; ENSMUSP00000030078.6; ENSMUSG00000028383.18.
DR GeneID; 72479; -.
DR KEGG; mmu:72479; -.
DR UCSC; uc008szy.3; mouse.
DR AGR; MGI:1919729; -.
DR CTD; 84263; -.
DR MGI; MGI:1919729; Hsdl2.
DR VEuPathDB; HostDB:ENSMUSG00000028383; -.
DR eggNOG; KOG0725; Eukaryota.
DR eggNOG; KOG4170; Eukaryota.
DR GeneTree; ENSGT00940000156729; -.
DR HOGENOM; CLU_010194_25_0_1; -.
DR InParanoid; Q2TPA8; -.
DR OMA; WWSSVAN; -.
DR OrthoDB; 4594at2759; -.
DR PhylomeDB; Q2TPA8; -.
DR TreeFam; TF101523; -.
DR BioGRID-ORCS; 72479; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Hsdl2; mouse.
DR PRO; PR:Q2TPA8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q2TPA8; Protein.
DR Bgee; ENSMUSG00000028383; Expressed in cardiac muscle of left ventricle and 256 other cell types or tissues.
DR ExpressionAtlas; Q2TPA8; baseline and differential.
DR Genevisible; Q2TPA8; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd09762; HSDL2_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003033; SCP2_sterol-bd_dom.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR42808; HYDROXYSTEROID DEHYDROGENASE-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR42808:SF3; HYDROXYSTEROID DEHYDROGENASE-LIKE PROTEIN 2; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF02036; SCP2; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55718; SCP-like; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydroxylation; NADP; Oxidoreductase; Peroxisome;
KW Reference proteome.
FT CHAIN 1..490
FT /note="Hydroxysteroid dehydrogenase-like protein 2"
FT /id="PRO_0000319889"
FT DOMAIN 380..487
FT /note="SCP2"
FT REGION 282..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 17..23
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q6YN16"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 390
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 307
FT /note="L -> V (in Ref. 2; BAE23126)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="K -> KPQLQEKPQLQEQ (in Ref. 2; BAE26313)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="E -> EQPQLQQ (in Ref. 4; AAH02211)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="Q -> K (in Ref. 2; BAE26313)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="P -> Q (in Ref. 2; BAE26313)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 54208 MW; 700958CDA46905DB CRC64;
MLPNTGKLAG CTVFITGASR GIGKAIALKA AKDGANIVIA AKTTQKHPKL LGTIYTAAEE
IEAAGGTALP CVVDVRDEQQ INSAVEKAVE KFGGIDILVN NASAISLTNT LDTPTKRVDL
MMNVNTRGTY LTSKACIPFL KKSKVGHILN LSPPLNLNPL WFKQHCAYTI AKYGMSMCVL
GMAEEFRGEI AVNALWPRTA IHTAAMDMLG GSGVENQCRK VDIIADAAYS IFKRPKSFTG
NFIIDENILK EEGIKNFDVY AIAPGHPLLP DFFLDEHPDA VMEEKESNDS VPEVKEEKLQ
LQEESQLQKQ PQLQEQPQLQ EKPQLQEKPQ LQEQPQLQEK PQLQEQPQQR EQPQLQQQPR
PRQQPQPFVQ SMLPQKPHFG AVEETFRIVK DSLSDEVVRA TQAVYQFELS GEDGGTWFLD
LKSKGGKVGH GEPSDRADVV MSMATDDFVK MFSGKLKPTM AFMSGKLKIK GNIALAIKLE
KLMTQMNSRL
//
