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D42E1_MOUSE
ID   D42E1_MOUSE             Reviewed;         394 AA.
AC   Q9D665; Q8VCV0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Short-chain dehydrogenase/reductase family 42E member 1 {ECO:0000250|UniProtKB:Q8WUS8};
DE            EC=1.1.1.-;
GN   Name=Sdr42e1;
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].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
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].
RC   STRAIN=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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH18550.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK014586; BAB29446.1; -; mRNA.
DR   EMBL; BC018550; AAH18550.1; ALT_INIT; mRNA.
DR   EMBL; BC038819; AAH38819.1; -; mRNA.
DR   CCDS; CCDS22701.1; -.
DR   RefSeq; NP_083001.1; NM_028725.3.
DR   RefSeq; XP_006531470.2; XM_006531407.3.
DR   RefSeq; XP_006531471.1; XM_006531408.2.
DR   RefSeq; XP_006531472.1; XM_006531409.2.
DR   AlphaFoldDB; Q9D665; -.
DR   SMR; Q9D665; -.
DR   STRING; 10090.ENSMUSP00000044457; -.
DR   iPTMnet; Q9D665; -.
DR   PhosphoSitePlus; Q9D665; -.
DR   MaxQB; Q9D665; -.
DR   PaxDb; Q9D665; -.
DR   PRIDE; Q9D665; -.
DR   ProteomicsDB; 285410; -.
DR   Antibodypedia; 3063; 22 antibodies from 13 providers.
DR   DNASU; 74032; -.
DR   Ensembl; ENSMUST00000037955; ENSMUSP00000044457; ENSMUSG00000034308.
DR   Ensembl; ENSMUST00000173522; ENSMUSP00000133782; ENSMUSG00000034308.
DR   GeneID; 74032; -.
DR   KEGG; mmu:74032; -.
DR   UCSC; uc009npd.1; mouse.
DR   CTD; 93517; -.
DR   MGI; MGI:1921282; Sdr42e1.
DR   VEuPathDB; HostDB:ENSMUSG00000034308; -.
DR   eggNOG; KOG1430; Eukaryota.
DR   GeneTree; ENSGT00940000158070; -.
DR   InParanoid; Q9D665; -.
DR   OMA; GAYKRSK; -.
DR   OrthoDB; 992332at2759; -.
DR   PhylomeDB; Q9D665; -.
DR   TreeFam; TF313574; -.
DR   BioGRID-ORCS; 74032; 4 hits in 73 CRISPR screens.
DR   ChiTaRS; Sdr42e1; mouse.
DR   PRO; PR:Q9D665; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9D665; protein.
DR   Bgee; ENSMUSG00000034308; Expressed in urinary bladder urothelium and 124 other tissues.
DR   ExpressionAtlas; Q9D665; baseline and differential.
DR   Genevisible; Q9D665; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Membrane; NAD; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..394
FT                   /note="Short-chain dehydrogenase/reductase family 42E
FT                   member 1"
FT                   /id="PRO_0000331756"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   394 AA;  43894 MW;  B1FB024CED5D1D15 CRC64;
     MDSPRFPEET VLITGGGGYF GFRLGCALNQ KGARVILFDI TQPAQNLPEG IKFVCGDIRC
     LADVETAFQD AEKVACVFHV ASYGMSGREQ LNKTQIEEVN VGGTENILRA CLERGVPRLV
     YTSTFNVIFG GQVIRNGDES LPYLPLHLHP DHYSRTKSIA EKKVLEANGL AFKQGDGILR
     TCAIRPAGIY GAGEQRHLPR IVSYIERGLF RFVYGDPQSL VEFVHVDNLA KAHILASEAL
     KADKGHVASG QPYFISDGRP VNNFEFFRPL VEGLGYTFPS TRLPLTLIYC LAFLVEMTHF
     IVGRLYNFQP FLTRTEVYKT GVTHYFSLEK AKKELGFEPQ PFDLQEVVEW FKAHGHGRGA
     AGQDSEFMLW DGILILLLAL SVLTWILPST TLSI
 
 
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