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T3HPD_MOUSE
ID   T3HPD_MOUSE             Reviewed;         354 AA.
AC   Q9CXA2; B8JJ82; Q99KB5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Trans-L-3-hydroxyproline dehydratase;
DE            EC=4.2.1.77;
DE   AltName: Full=Trans-3-hydroxy-L-proline dehydratase;
GN   Name=L3hypdh;
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=Lung;
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 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   [3]
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Lung;
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   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22528483; DOI=10.1074/jbc.m112.363218;
RA   Visser W.F., Verhoeven-Duif N.M., de Koning T.J.;
RT   "Identification of a human trans-3-Hydroxy-L-proline dehydratase, the first
RT   characterized member of a novel family of proline racemase-like enzymes.";
RL   J. Biol. Chem. 287:21654-21662(2012).
CC   -!- FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline to
CC       delta-1-pyrroline-2-carboxylate (Pyr2C). {ECO:0000269|PubMed:22528483}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=trans-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O;
CC         Xref=Rhea:RHEA:10320, ChEBI:CHEBI:15377, ChEBI:CHEBI:39785,
CC         ChEBI:CHEBI:57938; EC=4.2.1.77;
CC         Evidence={ECO:0000269|PubMed:22528483};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: In contrast to the T.cruzi proline racemase enzyme,
CC       lacks the conserved Cys at position 273 which is replaced by a Thr
CC       residue, transforming the racemase activity into dehydratase activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; AK018449; BAB31217.1; -; mRNA.
DR   EMBL; CR974486; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004753; AAH04753.1; -; mRNA.
DR   CCDS; CCDS25966.1; -.
DR   RefSeq; NP_080314.1; NM_026038.2.
DR   AlphaFoldDB; Q9CXA2; -.
DR   SMR; Q9CXA2; -.
DR   BioGRID; 212023; 1.
DR   STRING; 10090.ENSMUSP00000019862; -.
DR   iPTMnet; Q9CXA2; -.
DR   PhosphoSitePlus; Q9CXA2; -.
DR   jPOST; Q9CXA2; -.
DR   MaxQB; Q9CXA2; -.
DR   PaxDb; Q9CXA2; -.
DR   PeptideAtlas; Q9CXA2; -.
DR   PRIDE; Q9CXA2; -.
DR   ProteomicsDB; 254639; -.
DR   Antibodypedia; 68443; 52 antibodies from 14 providers.
DR   DNASU; 67217; -.
DR   Ensembl; ENSMUST00000019862; ENSMUSP00000019862; ENSMUSG00000019718.
DR   GeneID; 67217; -.
DR   KEGG; mmu:67217; -.
DR   UCSC; uc007nvd.1; mouse.
DR   CTD; 112849; -.
DR   MGI; MGI:1914467; L3hypdh.
DR   VEuPathDB; HostDB:ENSMUSG00000019718; -.
DR   eggNOG; ENOG502QRPF; Eukaryota.
DR   GeneTree; ENSGT00390000002032; -.
DR   HOGENOM; CLU_036729_0_1_1; -.
DR   InParanoid; Q9CXA2; -.
DR   OMA; SHVLWTG; -.
DR   OrthoDB; 894373at2759; -.
DR   PhylomeDB; Q9CXA2; -.
DR   TreeFam; TF329167; -.
DR   BioGRID-ORCS; 67217; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; L3hypdh; mouse.
DR   PRO; PR:Q9CXA2; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q9CXA2; protein.
DR   Bgee; ENSMUSG00000019718; Expressed in metanephric proximal tubule and 178 other tissues.
DR   Genevisible; Q9CXA2; MM.
DR   GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR   GO; GO:0050346; F:trans-L-3-hydroxyproline dehydratase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR008794; Pro_racemase_fam.
DR   PANTHER; PTHR33442; PTHR33442; 1.
DR   Pfam; PF05544; Pro_racemase; 1.
DR   PIRSF; PIRSF029792; Pro_racemase; 1.
DR   SFLD; SFLDS00028; Proline_Racemase; 1.
PE   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..354
FT                   /note="Trans-L-3-hydroxyproline dehydratase"
FT                   /id="PRO_0000288950"
FT   ACT_SITE        104
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         105..106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        13
FT                   /note="N -> H (in Ref. 3; AAH04753)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="P -> S (in Ref. 3; AAH04753)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="V -> M (in Ref. 3; AAH04753)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="K -> E (in Ref. 3; AAH04753)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  37804 MW;  B993BF8E7BFA3505 CRC64;
     MEAALAVTRL PPNDPRTPAL SVVDMHTGGE PLRIVHAGCP EVAGPTLLAK RRYMRQHLDY
     IRRRLVFEPR GHRDMYGAIL VPSELPDAHL GVLFLHNEGY SSMCGHAVLA LGRFALDFGL
     VPAPPKGARE AQVNIHCPCG LVTAFVECEG GRSCGPVRFH SVPAFVLASD LTVDVPGHGK
     VLVDIAYGGA FYAFVSAEKL GLDVCSAKTR DLVDAASALT GAVKAQFKIN HPESEDLGFL
     YGSILTDGKD AYSEEATTNI CVFADEQVDR SPTGSGVTAR IALQYHKGLL QLNQTRAFKS
     SATGSVFTGC AVREAKCGDF KAVIVEVAGQ AHYTGTANLT VEDGDPLRDG FLLK
 
 
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