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PXMP2_MOUSE
ID   PXMP2_MOUSE             Reviewed;         194 AA.
AC   P42925; Q9ERF1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Peroxisomal membrane protein 2;
DE   AltName: Full=22 kDa peroxisomal membrane protein;
GN   Name=Pxmp2; Synonyms=Pmp22;
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 [GENOMIC DNA].
RC   STRAIN=Swiss Webster; TISSUE=Liver;
RX   PubMed=7551822; DOI=10.1006/bmme.1995.1027;
RA   Bryant D.D., Wilson G.N.;
RT   "Differential evolution and expression of murine peroxisomal membrane
RT   protein genes.";
RL   Biochem. Mol. Med. 55:22-30(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RX   PubMed=11470509; DOI=10.1016/s0378-1119(01)00531-5;
RA   Luers G.H., Otte D.M., Subramani S., Franz T.;
RT   "Genomic organization, chromosomal localization and tissue specific
RT   expression of the murine Pxmp2 gene encoding the 22 kDa peroxisomal
RT   membrane protein (Pmp22).";
RL   Gene 272:45-50(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, and 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   -!- FUNCTION: Seems to be involved in pore-forming activity and may
CC       contribute to the unspecific permeability of the peroxisomal membrane.
CC   -!- SUBUNIT: Interacts with PEX19 and SIVA1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family.
CC       {ECO:0000305}.
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DR   EMBL; L28835; AAA39957.1; -; Genomic_DNA.
DR   EMBL; AF309644; AAG25724.1; -; mRNA.
DR   EMBL; AK003118; BAB22578.1; -; mRNA.
DR   RefSeq; NP_033019.2; NM_008993.2.
DR   AlphaFoldDB; P42925; -.
DR   STRING; 10090.ENSMUSP00000031472; -.
DR   iPTMnet; P42925; -.
DR   PhosphoSitePlus; P42925; -.
DR   jPOST; P42925; -.
DR   MaxQB; P42925; -.
DR   PaxDb; P42925; -.
DR   PeptideAtlas; P42925; -.
DR   PRIDE; P42925; -.
DR   ProteomicsDB; 301932; -.
DR   DNASU; 19301; -.
DR   GeneID; 19301; -.
DR   KEGG; mmu:19301; -.
DR   CTD; 5827; -.
DR   MGI; MGI:107487; Pxmp2.
DR   eggNOG; KOG1944; Eukaryota.
DR   InParanoid; P42925; -.
DR   OrthoDB; 1324608at2759; -.
DR   PhylomeDB; P42925; -.
DR   Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR   BioGRID-ORCS; 19301; 1 hit in 71 CRISPR screens.
DR   PRO; PR:P42925; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P42925; protein.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR   GO; GO:0005777; C:peroxisome; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   InterPro; IPR007248; Mpv17_PMP22.
DR   PANTHER; PTHR11266; PTHR11266; 1.
DR   Pfam; PF04117; Mpv17_PMP22; 1.
PE   1: Evidence at protein level;
KW   Membrane; Peroxisome; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..194
FT                   /note="Peroxisomal membrane protein 2"
FT                   /id="PRO_0000218930"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        52..74
FT                   /note="Peroxisomal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..113
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..172
FT                   /note="Peroxisomal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        58..60
FT                   /note="KQR -> RK (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64..65
FT                   /note="RL -> QN (in Ref. 2 and 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   194 AA;  22266 MW;  163AE9BDE638B1FC CRC64;
     MAPAASRLRV ESELGSLPKR ALAQYLLLLK LYPVLTKAVS SGILSALGNL LAQTIEKKQR
     KDSRLLEVSG LLRYLVYGLF VTGPLSHYLY LFMEYSVPPE VPWASVKRLL LDRLFFAPTF
     LLLFFFVMNL LEGKNVSVFV AKMRSGFWPA LQMNWRMWTP LQFININYVP LQFRVLFANM
     AALFWYAYLA SLGK
 
 
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