MP17L_HUMAN
ID MP17L_HUMAN Reviewed; 196 AA.
AC Q2QL34; B4DDY1; Q6P7T6; Q8N8E9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Mpv17-like protein;
DE AltName: Full=M-LP homolog;
DE Short=M-LPH;
GN Name=MPV17L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16631601; DOI=10.1016/j.bbrc.2006.04.008;
RA Iida R., Yasuda T., Tsubota E., Takatsuka H., Matsuki T., Kishi K.;
RT "Human Mpv17-like protein is localized in peroxisomes and regulates
RT expression of antioxidant enzymes.";
RL Biochem. Biophys. Res. Commun. 344:948-954(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2).
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterus;
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).
CC -!- FUNCTION: Isoform 1 participates in reactive oxygen species metabolism
CC by up- or down-regulation of the genes of antioxidant enzymes.
CC {ECO:0000269|PubMed:16631601}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Peroxisome membrane
CC {ECO:0000269|PubMed:16631601}; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=M-LPH1;
CC IsoId=Q2QL34-1; Sequence=Displayed;
CC Name=2; Synonyms=M-LPH2;
CC IsoId=Q2QL34-2; Sequence=VSP_033462, VSP_033463;
CC -!- TISSUE SPECIFICITY: Isoform 1 is detected in the kidney (at protein
CC level). Isoform 1 and isoform 2 are expressed in the kidney, heart,
CC liver, lung, pancreas and skeletal muscle.
CC {ECO:0000269|PubMed:16631601}.
CC -!- SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ004255; AAY58892.1; -; mRNA.
DR EMBL; DQ004256; AAY58893.1; -; mRNA.
DR EMBL; AK096918; BAC04895.1; -; mRNA.
DR EMBL; AK293380; BAG56892.1; -; mRNA.
DR EMBL; CH471226; EAW53915.1; -; Genomic_DNA.
DR EMBL; BC061514; AAH61514.1; -; mRNA.
DR CCDS; CCDS10560.1; -. [Q2QL34-2]
DR CCDS; CCDS45421.1; -. [Q2QL34-1]
DR RefSeq; NP_001121895.1; NM_001128423.1. [Q2QL34-1]
DR RefSeq; NP_776164.2; NM_173803.3. [Q2QL34-2]
DR AlphaFoldDB; Q2QL34; -.
DR BioGRID; 129068; 2.
DR STRING; 9606.ENSP00000379669; -.
DR iPTMnet; Q2QL34; -.
DR PhosphoSitePlus; Q2QL34; -.
DR BioMuta; MPV17L; -.
DR DMDM; 121941708; -.
DR MassIVE; Q2QL34; -.
DR MaxQB; Q2QL34; -.
DR PaxDb; Q2QL34; -.
DR PeptideAtlas; Q2QL34; -.
DR PRIDE; Q2QL34; -.
DR ProteomicsDB; 61440; -. [Q2QL34-1]
DR ProteomicsDB; 61441; -. [Q2QL34-2]
DR Antibodypedia; 42860; 36 antibodies from 14 providers.
DR DNASU; 255027; -.
DR Ensembl; ENST00000287594.7; ENSP00000287594.6; ENSG00000156968.9. [Q2QL34-2]
DR Ensembl; ENST00000396385.4; ENSP00000379669.3; ENSG00000156968.9. [Q2QL34-1]
DR Ensembl; ENST00000612041.2; ENSP00000483043.1; ENSG00000275543.4. [Q2QL34-2]
DR Ensembl; ENST00000617552.4; ENSP00000484675.1; ENSG00000275543.4. [Q2QL34-1]
DR GeneID; 255027; -.
DR KEGG; hsa:255027; -.
DR MANE-Select; ENST00000396385.4; ENSP00000379669.3; NM_001128423.2; NP_001121895.1.
DR UCSC; uc002ddm.3; human. [Q2QL34-1]
DR CTD; 255027; -.
DR DisGeNET; 255027; -.
DR GeneCards; MPV17L; -.
DR HGNC; HGNC:26827; MPV17L.
DR HPA; ENSG00000156968; Tissue enhanced (pancreas).
DR MIM; 618100; gene.
DR neXtProt; NX_Q2QL34; -.
DR OpenTargets; ENSG00000156968; -.
DR PharmGKB; PA145007960; -.
DR VEuPathDB; HostDB:ENSG00000156968; -.
DR eggNOG; KOG1944; Eukaryota.
DR GeneTree; ENSGT00730000111088; -.
DR HOGENOM; CLU_049109_11_0_1; -.
DR InParanoid; Q2QL34; -.
DR OMA; LVHQWFS; -.
DR OrthoDB; 1301408at2759; -.
DR PhylomeDB; Q2QL34; -.
DR TreeFam; TF324392; -.
DR PathwayCommons; Q2QL34; -.
DR BioGRID-ORCS; 255027; 13 hits in 1052 CRISPR screens.
DR ChiTaRS; MPV17L; human.
DR GenomeRNAi; 255027; -.
DR Pharos; Q2QL34; Tbio.
DR PRO; PR:Q2QL34; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q2QL34; protein.
DR Bgee; ENSG00000156968; Expressed in body of pancreas and 103 other tissues.
DR ExpressionAtlas; Q2QL34; baseline and differential.
DR Genevisible; Q2QL34; HS.
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; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; IDA:BHF-UCL.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IDA: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; Membrane; Peroxisome; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..196
FT /note="Mpv17-like protein"
FT /id="PRO_0000333178"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT TRANSMEM 17..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..50
FT /note="Lumenal"
FT TRANSMEM 51..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..90
FT /note="Cytoplasmic"
FT TRANSMEM 91..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..150
FT /note="Lumenal"
FT TRANSMEM 151..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..196
FT /note="Cytoplasmic"
FT REGION 16..55
FT /note="Targeting to peroxisomes"
FT /evidence="ECO:0000250"
FT VAR_SEQ 104..147
FT /note="GMSILQGKDDIFLDLKQKFWNTYLSGLMYWPFVQLTNFSLVPVQ -> EWTD
FT VLALCTADQLQPCSCSMENSLRWSLWFSLGHLHLFFPAEW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16631601"
FT /id="VSP_033462"
FT VAR_SEQ 148..196
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16631601"
FT /id="VSP_033463"
FT CONFLICT Q2QL34-2:106
FT /note="T -> I (in Ref. 2; BAC04895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 22116 MW; 0932E5228CB50AF8 CRC64;
MAGWWPALSR AARRHPWPTN VLLYGSLVSA GDALQQRLQG REANWRQTRR VATLVVTFHA
NFNYVWLRLL ERALPGRAPH ALLAKLLCDQ VVGAPIAVSA FYVGMSILQG KDDIFLDLKQ
KFWNTYLSGL MYWPFVQLTN FSLVPVQWRT AYAGVCGFLW ATFICFSQQS GDGTFKSAFT
ILYTKGTSAT EGYPKK
