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HSDL2_MOUSE
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   03-AUG-2022, entry version 119.
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; 27.
DR   IntAct; Q2TPA8; 1.
DR   MINT; Q2TPA8; -.
DR   STRING; 10090.ENSMUSP00000030078; -.
DR   iPTMnet; Q2TPA8; -.
DR   PhosphoSitePlus; Q2TPA8; -.
DR   SwissPalm; Q2TPA8; -.
DR   REPRODUCTION-2DPAGE; Q2TPA8; -.
DR   EPD; Q2TPA8; -.
DR   jPOST; Q2TPA8; -.
DR   MaxQB; Q2TPA8; -.
DR   PaxDb; Q2TPA8; -.
DR   PeptideAtlas; Q2TPA8; -.
DR   PRIDE; Q2TPA8; -.
DR   ProteomicsDB; 273388; -.
DR   Antibodypedia; 29681; 155 antibodies from 25 providers.
DR   DNASU; 72479; -.
DR   Ensembl; ENSMUST00000030078; ENSMUSP00000030078; ENSMUSG00000028383.
DR   GeneID; 72479; -.
DR   KEGG; mmu:72479; -.
DR   UCSC; uc008szy.3; mouse.
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; KFGMSLC; -.
DR   OrthoDB; 1361949at2759; -.
DR   PhylomeDB; Q2TPA8; -.
DR   TreeFam; TF101523; -.
DR   BioGRID-ORCS; 72479; 3 hits in 72 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 252 other 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   Gene3D; 3.30.1050.10; -; 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   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF02036; SCP2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF55718; SSF55718; 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
 
 
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