MP17L_MOUSE
ID MP17L_MOUSE Reviewed; 194 AA.
AC Q99MS3; Q3UWD2; Q8CI14;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Mpv17-like protein;
DE Short=M-LP;
GN Name=Mpv17l;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11327696; DOI=10.1006/bbrc.2001.4769;
RA Iida R., Yasuda T., Tsubota E., Matsuki T., Kishi K.;
RT "Cloning, mapping, genomic organization, and expression of mouse M-LP, a
RT new member of the peroxisomal membrane protein Mpv17 domain family.";
RL Biochem. Biophys. Res. Commun. 283:292-296(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TOPOLOGY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=15541722; DOI=10.1016/j.yexcr.2004.08.027;
RA Iida R., Yasuda T., Tsubota E., Takatsuka H., Masuyama M., Matsuki T.,
RA Kishi K.;
RT "A novel alternative spliced Mpv17-like protein isoform localizes in
RT cytosol and is expressed in a kidney- and adult-specific manner.";
RL Exp. Cell Res. 302:22-30(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Colon;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12471025; DOI=10.1074/jbc.m210886200;
RA Iida R., Yasuda T., Tsubota E., Takatsuka H., Masuyama M., Matsuki T.,
RA Kishi K.;
RT "M-LP, Mpv17-like protein, has a peroxisomal membrane targeting signal
RT comprising a transmembrane domain and a positively charged loop and up-
RT regulates expression of the manganese superoxide dismutase gene.";
RL J. Biol. Chem. 278:6301-6306(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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: Isoform 1 and isoform 3 participate in reactive oxygen
CC species metabolism by up- or down-regulation of the genes of
CC antioxidant enzymes. {ECO:0000269|PubMed:12471025,
CC ECO:0000269|PubMed:15541722}.
CC -!- INTERACTION:
CC Q99MS3; Q9JIY5: Htra2; NbExp=2; IntAct=EBI-15727135, EBI-2365838;
CC Q99MS3-1; Q9JIY5: Htra2; NbExp=3; IntAct=EBI-15727082, EBI-2365838;
CC Q99MS3-3; Q9JIY5: Htra2; NbExp=2; IntAct=EBI-15727109, EBI-2365838;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Peroxisome membrane
CC {ECO:0000269|PubMed:12471025}; Multi-pass membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:15541722}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=M-LP long;
CC IsoId=Q99MS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99MS3-2; Sequence=VSP_033464, VSP_033466;
CC Name=3; Synonyms=M-LP short;
CC IsoId=Q99MS3-3; Sequence=VSP_033465;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in the kidney
CC (at protein level). Isoform 1 is expressed in the kidney, spleen,
CC heart, brain, lung and liver. Isoform 3 is expressed in the kidney.
CC Isoform 1 and isoform 3 expression increase during development, reache
CC their highest level in adulthood and decrease with aging.
CC {ECO:0000269|PubMed:11327696, ECO:0000269|PubMed:12471025,
CC ECO:0000269|PubMed:15541722}.
CC -!- SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family.
CC {ECO:0000305}.
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DR EMBL; AF305634; AAK32113.2; -; mRNA.
DR EMBL; AY513273; AAS82777.1; -; mRNA.
DR EMBL; AK136449; BAE22983.1; -; mRNA.
DR EMBL; AK144372; BAE25854.1; -; mRNA.
DR EMBL; BC094450; AAH94450.1; -; mRNA.
DR EMBL; BC037713; AAH37713.1; -; mRNA.
DR CCDS; CCDS27970.1; -. [Q99MS3-1]
DR CCDS; CCDS79423.1; -. [Q99MS3-2]
DR CCDS; CCDS79426.1; -. [Q99MS3-3]
DR PIR; JC7685; JC7685.
DR RefSeq; NP_001276491.1; NM_001289562.1. [Q99MS3-2]
DR RefSeq; NP_001276492.1; NM_001289563.1. [Q99MS3-3]
DR RefSeq; NP_001276494.1; NM_001289565.1. [Q99MS3-3]
DR RefSeq; NP_001276496.1; NM_001289567.1. [Q99MS3-3]
DR RefSeq; NP_291042.2; NM_033564.3. [Q99MS3-1]
DR RefSeq; XP_011244354.1; XM_011246052.2.
DR AlphaFoldDB; Q99MS3; -.
DR SMR; Q99MS3; -.
DR DIP; DIP-46298N; -.
DR IntAct; Q99MS3; 1.
DR STRING; 10090.ENSMUSP00000023360; -.
DR PhosphoSitePlus; Q99MS3; -.
DR SwissPalm; Q99MS3; -.
DR jPOST; Q99MS3; -.
DR MaxQB; Q99MS3; -.
DR PaxDb; Q99MS3; -.
DR PRIDE; Q99MS3; -.
DR ProteomicsDB; 291390; -. [Q99MS3-1]
DR ProteomicsDB; 291391; -. [Q99MS3-2]
DR ProteomicsDB; 291392; -. [Q99MS3-3]
DR DNASU; 93734; -.
DR Ensembl; ENSMUST00000023360; ENSMUSP00000023360; ENSMUSG00000022679. [Q99MS3-1]
DR Ensembl; ENSMUST00000124947; ENSMUSP00000117826; ENSMUSG00000022679. [Q99MS3-3]
DR Ensembl; ENSMUST00000128757; ENSMUSP00000120169; ENSMUSG00000022679. [Q99MS3-2]
DR GeneID; 93734; -.
DR KEGG; mmu:93734; -.
DR UCSC; uc007ygo.2; mouse. [Q99MS3-2]
DR UCSC; uc007ygp.2; mouse. [Q99MS3-3]
DR UCSC; uc007ygr.2; mouse. [Q99MS3-1]
DR CTD; 255027; -.
DR MGI; MGI:2135951; Mpv17l.
DR VEuPathDB; HostDB:ENSMUSG00000022679; -.
DR eggNOG; KOG1944; Eukaryota.
DR GeneTree; ENSGT00730000111088; -.
DR HOGENOM; CLU_164445_0_0_1; -.
DR InParanoid; Q99MS3; -.
DR OMA; LVHQWFS; -.
DR OrthoDB; 1301408at2759; -.
DR PhylomeDB; Q99MS3; -.
DR TreeFam; TF324392; -.
DR BioGRID-ORCS; 93734; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q99MS3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q99MS3; protein.
DR Bgee; ENSMUSG00000022679; Expressed in right kidney and 245 other tissues.
DR ExpressionAtlas; Q99MS3; baseline and differential.
DR Genevisible; Q99MS3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; ISO:MGI.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR InterPro; IPR007248; Mpv17_PMP22.
DR PANTHER; PTHR11266; PTHR11266; 1.
DR Pfam; PF04117; Mpv17_PMP22; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Membrane; Peroxisome; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..194
FT /note="Mpv17-like protein"
FT /id="PRO_0000333179"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15541722"
FT TRANSMEM 15..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..50
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:15541722"
FT TRANSMEM 51..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15541722"
FT TRANSMEM 92..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..150
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:15541722"
FT TRANSMEM 151..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15541722"
FT REGION 16..55
FT /note="Targeting to peroxisomes"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15541722, ECO:0000303|PubMed:16141072"
FT /id="VSP_033465"
FT VAR_SEQ 1..98
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033464"
FT VAR_SEQ 99..103
FT /note="SAFYV -> MRYPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033466"
SQ SEQUENCE 194 AA; 22180 MW; A0F43AC6F80F6B86 CRC64;
MASWWRAFPQ AARRYPWPTN VLLYAGLFSA GDALQQRLRG GPADWRQTRR VATLAVTFHG
NFNYVWLRLL ERALPGRAPR TVLAKVLCDQ TVGGPIALSA FYVGMSVLQG KDDIFLDLKQ
KFWNTYKSGL MYWPFVQLTN FSLVPVHWRT AYTGLCAFLW ATFLCFSQQS GDGTLQSIFI
FLRRKEASDK SPEK
