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MDH1B_MOUSE
ID   MDH1B_MOUSE             Reviewed;         500 AA.
AC   Q5F204; Q80YT6; Q9D988;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Putative malate dehydrogenase 1B;
DE            EC=1.1.1.-;
GN   Name=Mdh1b;
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 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-500.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
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).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH50786.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB24922.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL732462; CAI51863.1; -; Genomic_DNA.
DR   EMBL; AL645534; CAI51863.1; JOINED; Genomic_DNA.
DR   EMBL; AL645534; CAI51917.1; -; Genomic_DNA.
DR   EMBL; AC099637; CAI51917.1; JOINED; Genomic_DNA.
DR   EMBL; BC050786; AAH50786.1; ALT_INIT; mRNA.
DR   EMBL; AK007262; BAB24922.1; ALT_INIT; mRNA.
DR   CCDS; CCDS15000.2; -.
DR   RefSeq; NP_083972.3; NM_029696.4.
DR   AlphaFoldDB; Q5F204; -.
DR   SMR; Q5F204; -.
DR   STRING; 10090.ENSMUSP00000109728; -.
DR   iPTMnet; Q5F204; -.
DR   PhosphoSitePlus; Q5F204; -.
DR   PaxDb; Q5F204; -.
DR   PRIDE; Q5F204; -.
DR   ProteomicsDB; 295984; -.
DR   Antibodypedia; 34182; 93 antibodies from 19 providers.
DR   Ensembl; ENSMUST00000114094; ENSMUSP00000109728; ENSMUSG00000025963.
DR   GeneID; 76668; -.
DR   KEGG; mmu:76668; -.
DR   UCSC; uc007bgj.1; mouse.
DR   CTD; 130752; -.
DR   MGI; MGI:1923918; Mdh1b.
DR   VEuPathDB; HostDB:ENSMUSG00000025963; -.
DR   eggNOG; KOG1496; Eukaryota.
DR   GeneTree; ENSGT00530000063410; -.
DR   HOGENOM; CLU_040727_2_3_1; -.
DR   InParanoid; Q5F204; -.
DR   OMA; QHPDVWE; -.
DR   OrthoDB; 588276at2759; -.
DR   PhylomeDB; Q5F204; -.
DR   TreeFam; TF329007; -.
DR   BioGRID-ORCS; 76668; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q5F204; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q5F204; protein.
DR   Bgee; ENSMUSG00000025963; Expressed in spermatocyte and 53 other tissues.
DR   Genevisible; Q5F204; MM.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
DR   GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.90.110.10; -; 1.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..500
FT                   /note="Putative malate dehydrogenase 1B"
FT                   /id="PRO_0000331436"
FT   REGION          465..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..492
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        10
FT                   /note="A -> E (in Ref. 2; AAH50786)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  56297 MW;  9D7DB6688A93B9CF CRC64;
     MAKFVIAGKA NCPYYAKAEL LADYLQKNLP DFRIFKITQH PDKWEDWVED VCERNMWDHR
     TSPIIWRELL DRGGRGLLLG GYNEFLEHAQ LYYGVTSNMT TELMMVIAKE NMQTHTEQQL
     DKETMKDLIS PLQVWIASAG TYVCCHLIPL LLSGEVFGMH TEISLTLFDQ EQREDCLRSI
     VMETQDLASP VLRTVSFCTT VKEAFLQAQV IIILDDSTEE EVYSLESCLR SRVPLCRLYG
     YLIEKNAHKS VKVIVGGKNF VNLKTTLLMQ YAPNIASNII AVALGVEGQA KAVLARKMKT
     TSANIKDVII WGNITGNNYV DLRKAKVYNY ESAVKGPPGH YHSVLSLIFD REWITKEFVQ
     TLKILSSTGK QFGGILAAHS IATTLKYWYH GSPPGEIVSL GVMSEGQFDI PEGIVFSMPV
     KFENGTWVVL TDLEDISLSE KTLSRLTGDL IQEKLVACGD LLTFQPIEED PKDNEPSNTG
     MNEEKEQPGS DDSDEKNEDQ
 
 
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