STML2_MOUSE
ID STML2_MOUSE Reviewed; 353 AA.
AC Q99JB2; Q9DCG8;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Stomatin-like protein 2, mitochondrial;
DE Short=SLP-2;
DE Short=mslp2;
DE Flags: Precursor;
GN Name=Stoml2; Synonyms=Slp2;
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].
RC STRAIN=FVB/NJ; TISSUE=Kidney;
RX PubMed=16324911; DOI=10.1016/j.compbiomed.2004.12.001;
RA Chan W.L., Chang J.G., Chen Y.F., Chan Y.K., Chu Y.P.;
RT "Identification of mouse mslp2 gene from EST databases by repeated
RT searching, comparison, and assembling.";
RL Comput. Biol. Med. 36:101-108(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and FVB/N-3; 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 INTERACTION WITH CACNA2D2.
RX PubMed=16928863; DOI=10.1523/jneurosci.2764-06.2006;
RA Davies A., Douglas L., Hendrich J., Wratten J., Tran Van Minh A.,
RA Foucault I., Koch D., Pratt W.S., Saibil H.R., Dolphin A.C.;
RT "The calcium channel alpha2delta-2 subunit partitions with CaV2.1 into
RT lipid rafts in cerebellum: implications for localization and function.";
RL J. Neurosci. 26:8748-8757(2006).
RN [5]
RP FUNCTION IN MITOCHONDRIAL FUSION.
RX PubMed=19360003; DOI=10.1038/emboj.2009.89;
RA Tondera D., Grandemange S., Jourdain A., Karbowski M., Mattenberger Y.,
RA Herzig S., Da Cruz S., Clerc P., Raschke I., Merkwirth C., Ehses S.,
RA Krause F., Chan D.C., Alexander C., Bauer C., Youle R., Langer T.,
RA Martinou J.C.;
RT "SLP-2 is required for stress-induced mitochondrial hyperfusion.";
RL EMBO J. 28:1589-1600(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23028053; DOI=10.4049/jimmunol.1103829;
RA Christie D.A., Mitsopoulos P., Blagih J., Dunn S.D., St-Pierre J.,
RA Jones R.G., Hatch G.M., Madrenas J.;
RT "Stomatin-like protein 2 deficiency in T cells is associated with altered
RT mitochondrial respiration and defective CD4+ T cell responses.";
RL J. Immunol. 189:4349-4360(2012).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22623988; DOI=10.1371/journal.pone.0037144;
RA Christie D.A., Kirchhof M.G., Vardhana S., Dustin M.L., Madrenas J.;
RT "Mitochondrial and plasma membrane pools of stomatin-like protein 2
RT coalesce at the immunological synapse during T cell activation.";
RL PLoS ONE 7:E37144-E37144(2012).
RN [9]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-145, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145 AND LYS-233, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Mitochondrial protein that probably regulates the biogenesis
CC and the activity of mitochondria. Stimulates cardiolipin biosynthesis,
CC binds cardiolipin-enriched membranes where it recruits and stabilizes
CC some proteins including prohibitin and may therefore act in the
CC organization of functional microdomains in mitochondrial membranes.
CC Through regulation of the mitochondrial function may play a role into
CC several biological processes including cell migration, cell
CC proliferation, T-cell activation, calcium homeostasis and cellular
CC response to stress. May play a role in calcium homeostasis through
CC negative regulation of calcium efflux from mitochondria. Required for
CC mitochondrial hyperfusion a pro-survival cellular response to stress
CC which results in increased ATP production by mitochondria. May also
CC regulate the organization of functional domains at the plasma membrane
CC and play a role in T-cell activation through association with the T-
CC cell receptor signaling complex and its regulation.
CC {ECO:0000269|PubMed:19360003, ECO:0000269|PubMed:23028053}.
CC -!- SUBUNIT: Forms homooligomers (By similarity). Interacts with MFN2; may
CC form heterooligomers (By similarity). Interacts with PHB1 and PHB2;
CC recruits them to cardiolipin-enriched mitochondrial membranes and
CC stabilizes them (By similarity). Interacts with CACNA2D2. {ECO:0000250,
CC ECO:0000269|PubMed:16928863}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22623988};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJZ1}.
CC Mitochondrion {ECO:0000269|PubMed:22623988}. Mitochondrion inner
CC membrane {ECO:0000250|UniProtKB:Q9UJZ1}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9UJZ1}. Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:Q9UJZ1}. Membrane raft
CC {ECO:0000250|UniProtKB:Q9UJZ1}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9UJZ1}. Note=Behaves as an integral membrane
CC protein of the mitochondrion despite the absence of a detectable
CC transmembrane domain. Also associates with the actin cytoskeleton and
CC membrane rafts in activated T-cells. A minor pool is associated with
CC the plasma membrane and is enriched at the immunological synapse in
CC activated T-cells. {ECO:0000250|UniProtKB:Q9UJZ1}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal at the preimplantation stage. T-
CC cell-specific conditional knockout does not alter the normal
CC development of those cells but decreases their responses to stimulation
CC through the T-cell receptor. {ECO:0000269|PubMed:23028053}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
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DR EMBL; AF323178; AAG53404.1; -; mRNA.
DR EMBL; AK002793; BAB22363.1; -; mRNA.
DR EMBL; BC003425; AAH03425.1; -; mRNA.
DR EMBL; BC069941; AAH69941.1; -; mRNA.
DR CCDS; CCDS18089.1; -.
DR RefSeq; NP_075720.1; NM_023231.2.
DR AlphaFoldDB; Q99JB2; -.
DR SMR; Q99JB2; -.
DR BioGRID; 211578; 8.
DR IntAct; Q99JB2; 5.
DR MINT; Q99JB2; -.
DR STRING; 10090.ENSMUSP00000030169; -.
DR iPTMnet; Q99JB2; -.
DR PhosphoSitePlus; Q99JB2; -.
DR SwissPalm; Q99JB2; -.
DR REPRODUCTION-2DPAGE; Q99JB2; -.
DR EPD; Q99JB2; -.
DR jPOST; Q99JB2; -.
DR MaxQB; Q99JB2; -.
DR PaxDb; Q99JB2; -.
DR PeptideAtlas; Q99JB2; -.
DR PRIDE; Q99JB2; -.
DR ProteomicsDB; 258640; -.
DR Antibodypedia; 25758; 277 antibodies from 29 providers.
DR DNASU; 66592; -.
DR Ensembl; ENSMUST00000030169; ENSMUSP00000030169; ENSMUSG00000028455.
DR GeneID; 66592; -.
DR KEGG; mmu:66592; -.
DR UCSC; uc008soy.1; mouse.
DR CTD; 30968; -.
DR MGI; MGI:1913842; Stoml2.
DR VEuPathDB; HostDB:ENSMUSG00000028455; -.
DR eggNOG; KOG2620; Eukaryota.
DR GeneTree; ENSGT01030000234614; -.
DR HOGENOM; CLU_024949_1_0_1; -.
DR InParanoid; Q99JB2; -.
DR OMA; TQIRAEM; -.
DR OrthoDB; 1237942at2759; -.
DR PhylomeDB; Q99JB2; -.
DR TreeFam; TF105750; -.
DR Reactome; R-MMU-8949664; Processing of SMDT1.
DR BioGRID-ORCS; 66592; 11 hits in 71 CRISPR screens.
DR ChiTaRS; Stoml2; mouse.
DR PRO; PR:Q99JB2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q99JB2; protein.
DR Bgee; ENSMUSG00000028455; Expressed in epiblast (generic) and 67 other tissues.
DR ExpressionAtlas; Q99JB2; baseline and differential.
DR Genevisible; Q99JB2; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042101; C:T cell receptor complex; ISO:MGI.
DR GO; GO:1901612; F:cardiolipin binding; ISS:UniProtKB.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0035710; P:CD4-positive, alpha-beta T cell activation; IMP:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0010876; P:lipid localization; IMP:UniProtKB.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0034982; P:mitochondrial protein processing; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:1900210; P:positive regulation of cardiolipin metabolic process; ISS:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:UniProtKB.
DR GO; GO:0090297; P:positive regulation of mitochondrial DNA replication; ISS:UniProtKB.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IMP:UniProtKB.
DR GO; GO:1990046; P:stress-induced mitochondrial fusion; IMP:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR032435; Band_7_C.
DR InterPro; IPR001972; Stomatin_HflK_HflKC_fam.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF16200; Band_7_C; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Lipid-binding; Lipoprotein; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..353
FT /note="Stomatin-like protein 2, mitochondrial"
FT /id="PRO_0000094032"
FT REGION 324..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 215..252
FT /evidence="ECO:0000255"
FT COMPBIAS 324..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine; by PKC/PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:Q9UJZ1"
FT MOD_RES 124
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJZ1"
FT MOD_RES 145
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 145
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJZ1"
FT CONFLICT 5
FT /note="A -> R (in Ref. 2; BAB22363)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="S -> F (in Ref. 2; BAB22363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 353 AA; 38385 MW; 391D269576F6E6BB CRC64;
MLARAARGTG ALLLRGSVQA SGRVPRRASS GLPRNTVILF VPQQEAWVVE RMGRFHRILE
PGLNVLIPVL DRIRYVQSLK EIVINVPEQS AVTLDNVTLQ IDGVLYLRIM DPYKASYGVE
DPEYAVTQLA QTTMRSELGK LSLDKVFRER ESLNANIVDA INQAADCWGI RCLRYEIKDI
HVPPRVKESM QMQVEAERRK RATVLESEGT RESAINVAEG KKQAQILASE AEKAEQINQA
AGEASAVLAK AKAKAEAIRI LAGALTQHNG DAAASLTVAE QYVSAFSKLA KDSNTVLLPS
NPSDVTSMVA QAMGVYGALT KAPVPGAQNS SQSRRDVQAT DTSIEELGRV KLS
