STMP1_MOUSE
ID STMP1_MOUSE Reviewed; 47 AA.
AC P0DP99; A0A5F8MPG2; Q3TAI1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Short transmembrane mitochondrial protein 1 {ECO:0000305};
DE AltName: Full=Mitochondrial micropeptide-47 {ECO:0000303|PubMed:31836654};
DE Short=Mm47 {ECO:0000303|PubMed:31836654};
DE AltName: Full=Protein mitolamban {ECO:0000303|PubMed:31836654};
GN Name=Stmp1 {ECO:0000250|UniProtKB:E0CX11};
GN Synonyms=Mtlbn {ECO:0000303|PubMed:31836654};
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=NOD; TISSUE=Spleen;
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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY TLR
RP LIGANDS.
RX PubMed=31836654; DOI=10.4049/jimmunol.1900791;
RA Bhatta A., Atianand M., Jiang Z., Crabtree J., Blin J., Fitzgerald K.A.;
RT "A Mitochondrial Micropeptide Is Required for Activation of the Nlrp3
RT Inflammasome.";
RL J. Immunol. 204:428-437(2020).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH UQCRC1;
RP UQCRC2 AND UQCR10/QCR9.
RX PubMed=35101990; DOI=10.1073/pnas.2120476119;
RA Makarewich C.A., Munir A.Z., Bezprozvannaya S., Gibson A.M., Young Kim S.,
RA Martin-Sandoval M.S., Mathews T.P., Szweda L.I., Bassel-Duby R.,
RA Olson E.N.;
RT "The cardiac-enriched microprotein mitolamban regulates mitochondrial
RT respiratory complex assembly and function in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
CC -!- FUNCTION: Microprotein involved in mitochondrial respiratory chain
CC complex III (ubiquinol-cytochrome c oxidoreductase) and complex IV
CC (mitochondrial cytochrome c oxidase complex) assembly
CC (PubMed:35101990). Required for the formation of mitochondrial
CC supercomplexes (SCs) (PubMed:35101990). Also required for the
CC activation of the NLRP3 inflammasome (PubMed:31836654).
CC {ECO:0000269|PubMed:31836654, ECO:0000269|PubMed:35101990}.
CC -!- SUBUNIT: Interacts with components of the ubiquinol-cytochrome c
CC oxidoreductase (cytochrome b-c1 complex, complex III, CIII), such as
CC UQCRC1/QCR1, UQCRC2/QCR2 and UQCR10/QCR9 (PubMed:35101990). Interacts
CC with components of the cytochrome c oxidase (mitochondrial respiratory
CC chain complex IV) complex, such as MT-CO2 (By similarity).
CC {ECO:0000250|UniProtKB:E0CX11, ECO:0000269|PubMed:35101990}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:35101990}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:31836654}; Single-pass membrane protein
CC {ECO:0000255}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:31836654}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in lung,
CC skeletal muscle and heart (PubMed:31836654, PubMed:35101990). Expressed
CC in bone marrow-derived macrophages (at protein level)
CC (PubMed:31836654). {ECO:0000269|PubMed:31836654,
CC ECO:0000269|PubMed:35101990}.
CC -!- INDUCTION: Down-regulated by TLR ligands, including bacterial
CC lipopolysaccharide (LPS), in bone marrow-derived macrophages.
CC {ECO:0000269|PubMed:31836654}.
CC -!- DISRUPTION PHENOTYPE: Mice were born at expected Mendelian ratios and
CC do not show any visible phenotype, displaying normal heart function and
CC cardiac dimensions (PubMed:35101990). Cells however display defects in
CC complex III activity and metabolic perturbations in the heart, as well
CC as altered complex III assembly into respiratory supercomplexes
CC (PubMed:35101990). {ECO:0000269|PubMed:35101990}.
CC -!- SIMILARITY: Belongs to the STMP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE42687.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AK171831; BAE42687.1; ALT_SEQ; mRNA.
DR EMBL; AC158681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL456132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DP99; -.
DR SMR; P0DP99; -.
DR PhosphoSitePlus; P0DP99; -.
DR PRIDE; P0DP99; -.
DR ProteomicsDB; 257457; -.
DR Antibodypedia; 77172; 4 antibodies from 4 providers.
DR Ensembl; ENSMUST00000152147; ENSMUSP00000158958; ENSMUSG00000073155.
DR MGI; MGI:1914955; 1810058I24Rik.
DR VEuPathDB; HostDB:ENSMUSG00000073155; -.
DR GeneTree; ENSGT00550000076278; -.
DR ChiTaRS; 1810058I24Rik; mouse.
DR PRO; PR:P0DP99; -.
DR Proteomes; UP000000589; Chromosome 6.
DR Bgee; ENSMUSG00000073155; Expressed in blood and 234 other tissues.
DR ExpressionAtlas; P0DP99; baseline and differential.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005746; C:mitochondrial respirasome; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0097250; P:mitochondrial respirasome assembly; IMP:UniProtKB.
DR GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IMP:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:UniProtKB.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IMP:UniProtKB.
DR InterPro; IPR027854; STMP1.
DR PANTHER; PTHR47709; PTHR47709; 1.
DR Pfam; PF15054; DUF4535; 1.
PE 1: Evidence at protein level;
KW Immunity; Innate immunity; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion outer membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..47
FT /note="Short transmembrane mitochondrial protein 1"
FT /id="PRO_0000441870"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 47 AA; 5327 MW; EAC5A137CBED5398 CRC64;
MLQFLLGFTL GNVVGMYLAQ NYEMPNLAKK LEEIKKDLEA KKKPPSS
