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Protein

Stomatin-like protein 2, mitochondrial

Gene

Stoml2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation.2 Publications

GO - Molecular functioni

GO - Biological processi

  • CD4-positive, alpha-beta T cell activation Source: UniProtKB
  • cellular calcium ion homeostasis Source: UniProtKB
  • interleukin-2 production Source: UniProtKB
  • lipid localization Source: UniProtKB
  • mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  • mitochondrial calcium ion transport Source: UniProtKB
  • mitochondrial protein processing Source: UniProtKB
  • mitochondrion organization Source: UniProtKB
  • positive regulation of cardiolipin metabolic process Source: UniProtKB
  • positive regulation of mitochondrial DNA replication Source: UniProtKB
  • positive regulation of mitochondrial membrane potential Source: UniProtKB
  • protein oligomerization Source: UniProtKB
  • stress-induced mitochondrial fusion Source: UniProtKB
  • T cell receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Stomatin-like protein 2, mitochondrial
Short name:
SLP-2
Short name:
mslp2
Gene namesi
Name:Stoml2
Synonyms:Slp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1913842. Stoml2.

Subcellular locationi

  • Cell membrane 1 Publication; Peripheral membrane protein By similarity
  • Mitochondrion 1 Publication
  • Mitochondrion inner membrane By similarity; Lipid-anchor By similarity
  • Mitochondrion intermembrane space By similarity
  • Membrane raft By similarity
  • Cytoplasmcytoskeleton By similarity

  • Note: Behaves as an integral membrane protein of the mitochondrion despite the absence of a detectable transmembrane domain. Also associates with the actin cytoskeleton and membrane rafts in activated T-cells. A minor pool is associated with the plasma membrane and is enriched at the immunological synapse in activated T-cells.By similarity

GO - Cellular componenti

  • actin cytoskeleton Source: Ensembl
  • COP9 signalosome Source: Ensembl
  • extrinsic component of plasma membrane Source: UniProtKB
  • immunological synapse Source: Ensembl
  • membrane raft Source: UniProtKB
  • mitochondrial inner membrane Source: MGI
  • mitochondrial intermembrane space Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • T cell receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Disruption phenotypei

Embryonic lethal at the preimplantation stage. T-cell-specific conditional knockout does not alter the normal development of those cells but decreases their responses to stimulation through the T-cell receptor.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionSequence analysisAdd
BLAST
Chaini29 – 353325Stomatin-like protein 2, mitochondrialPRO_0000094032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphoserine; by PKC/PRKCZBy similarity
Modified residuei124 – 1241PhosphotyrosineBy similarity
Modified residuei145 – 1451N6-acetyllysine; alternateCombined sources
Modified residuei145 – 1451N6-succinyllysine; alternateCombined sources
Modified residuei233 – 2331N6-acetyllysineCombined sources
Modified residuei330 – 3301PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein

Proteomic databases

EPDiQ99JB2.
MaxQBiQ99JB2.
PaxDbiQ99JB2.
PRIDEiQ99JB2.

2D gel databases

REPRODUCTION-2DPAGEQ99JB2.

PTM databases

iPTMnetiQ99JB2.
PhosphoSiteiQ99JB2.

Expressioni

Gene expression databases

BgeeiQ99JB2.
CleanExiMM_STOML2.
ExpressionAtlasiQ99JB2. baseline and differential.
GenevisibleiQ99JB2. MM.

Interactioni

Subunit structurei

Forms homooligomers (By similarity). Interacts with MFN2; may form heterooligomers (By similarity). Interacts with PHB and PHB2; recruits them to cardiolipin-enriched mitochondrial membranes and stabilizes them (By similarity). Interacts with CACNA2D2.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211578. 1 interaction.
IntActiQ99JB2. 2 interactions.
STRINGi10090.ENSMUSP00000030169.

Structurei

3D structure databases

ProteinModelPortaliQ99JB2.
SMRiQ99JB2. Positions 76-222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili215 – 25238Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the band 7/mec-2 family.Curated

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

eggNOGiKOG2620. Eukaryota.
COG0330. LUCA.
GeneTreeiENSGT00550000074454.
HOGENOMiHOG000217038.
HOVERGENiHBG061488.
InParanoidiQ99JB2.
OMAiGVTDYRY.
OrthoDBiEOG77M8NR.
PhylomeDBiQ99JB2.
TreeFamiTF105750.

Family and domain databases

InterProiIPR001107. Band_7.
IPR032435. Band_7_C.
IPR001972. Stomatin_fam.
[Graphical view]
PANTHERiPTHR10264. PTHR10264. 1 hit.
PfamiPF01145. Band_7. 1 hit.
PF16200. Band_7_C. 1 hit.
[Graphical view]
PRINTSiPR00721. STOMATIN.
SMARTiSM00244. PHB. 1 hit.
[Graphical view]
SUPFAMiSSF117892. SSF117892. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99JB2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLARAARGTG ALLLRGSVQA SGRVPRRASS GLPRNTVILF VPQQEAWVVE
60 70 80 90 100
RMGRFHRILE PGLNVLIPVL DRIRYVQSLK EIVINVPEQS AVTLDNVTLQ
110 120 130 140 150
IDGVLYLRIM DPYKASYGVE DPEYAVTQLA QTTMRSELGK LSLDKVFRER
160 170 180 190 200
ESLNANIVDA INQAADCWGI RCLRYEIKDI HVPPRVKESM QMQVEAERRK
210 220 230 240 250
RATVLESEGT RESAINVAEG KKQAQILASE AEKAEQINQA AGEASAVLAK
260 270 280 290 300
AKAKAEAIRI LAGALTQHNG DAAASLTVAE QYVSAFSKLA KDSNTVLLPS
310 320 330 340 350
NPSDVTSMVA QAMGVYGALT KAPVPGAQNS SQSRRDVQAT DTSIEELGRV

KLS
Length:353
Mass (Da):38,385
Last modified:June 1, 2001 - v1
Checksum:i391D269576F6E6BB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → R in BAB22363 (PubMed:16141072).Curated
Sequence conflicti152 – 1521S → F in BAB22363 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323178 mRNA. Translation: AAG53404.1.
AK002793 mRNA. Translation: BAB22363.1.
BC003425 mRNA. Translation: AAH03425.1.
BC069941 mRNA. Translation: AAH69941.1.
CCDSiCCDS18089.1.
RefSeqiNP_075720.1. NM_023231.2.
UniGeneiMm.331565.

Genome annotation databases

EnsembliENSMUST00000030169; ENSMUSP00000030169; ENSMUSG00000028455.
GeneIDi66592.
KEGGimmu:66592.
UCSCiuc008soy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323178 mRNA. Translation: AAG53404.1.
AK002793 mRNA. Translation: BAB22363.1.
BC003425 mRNA. Translation: AAH03425.1.
BC069941 mRNA. Translation: AAH69941.1.
CCDSiCCDS18089.1.
RefSeqiNP_075720.1. NM_023231.2.
UniGeneiMm.331565.

3D structure databases

ProteinModelPortaliQ99JB2.
SMRiQ99JB2. Positions 76-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211578. 1 interaction.
IntActiQ99JB2. 2 interactions.
STRINGi10090.ENSMUSP00000030169.

PTM databases

iPTMnetiQ99JB2.
PhosphoSiteiQ99JB2.

2D gel databases

REPRODUCTION-2DPAGEQ99JB2.

Proteomic databases

EPDiQ99JB2.
MaxQBiQ99JB2.
PaxDbiQ99JB2.
PRIDEiQ99JB2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030169; ENSMUSP00000030169; ENSMUSG00000028455.
GeneIDi66592.
KEGGimmu:66592.
UCSCiuc008soy.1. mouse.

Organism-specific databases

CTDi30968.
MGIiMGI:1913842. Stoml2.

Phylogenomic databases

eggNOGiKOG2620. Eukaryota.
COG0330. LUCA.
GeneTreeiENSGT00550000074454.
HOGENOMiHOG000217038.
HOVERGENiHBG061488.
InParanoidiQ99JB2.
OMAiGVTDYRY.
OrthoDBiEOG77M8NR.
PhylomeDBiQ99JB2.
TreeFamiTF105750.

Miscellaneous databases

NextBioi322100.
PROiQ99JB2.
SOURCEiSearch...

Gene expression databases

BgeeiQ99JB2.
CleanExiMM_STOML2.
ExpressionAtlasiQ99JB2. baseline and differential.
GenevisibleiQ99JB2. MM.

Family and domain databases

InterProiIPR001107. Band_7.
IPR032435. Band_7_C.
IPR001972. Stomatin_fam.
[Graphical view]
PANTHERiPTHR10264. PTHR10264. 1 hit.
PfamiPF01145. Band_7. 1 hit.
PF16200. Band_7_C. 1 hit.
[Graphical view]
PRINTSiPR00721. STOMATIN.
SMARTiSM00244. PHB. 1 hit.
[Graphical view]
SUPFAMiSSF117892. SSF117892. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of mouse mslp2 gene from EST databases by repeated searching, comparison, and assembling."
    Chan W.L., Chang J.G., Chen Y.F., Chan Y.K., Chu Y.P.
    Comput. Biol. Med. 36:101-108(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FVB/NJ.
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N and FVB/N-3.
    Tissue: Mammary tumor.
  4. "The calcium channel alpha2delta-2 subunit partitions with CaV2.1 into lipid rafts in cerebellum: implications for localization and function."
    Davies A., Douglas L., Hendrich J., Wratten J., Tran Van Minh A., Foucault I., Koch D., Pratt W.S., Saibil H.R., Dolphin A.C.
    J. Neurosci. 26:8748-8757(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CACNA2D2.
  5. Cited for: FUNCTION IN MITOCHONDRIAL FUSION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "Stomatin-like protein 2 deficiency in T cells is associated with altered mitochondrial respiration and defective CD4+ T cell responses."
    Christie D.A., Mitsopoulos P., Blagih J., Dunn S.D., St-Pierre J., Jones R.G., Hatch G.M., Madrenas J.
    J. Immunol. 189:4349-4360(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Mitochondrial and plasma membrane pools of stomatin-like protein 2 coalesce at the immunological synapse during T cell activation."
    Christie D.A., Kirchhof M.G., Vardhana S., Dustin M.L., Madrenas J.
    PLoS ONE 7:E37144-E37144(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145 AND LYS-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSTML2_MOUSE
AccessioniPrimary (citable) accession number: Q99JB2
Secondary accession number(s): Q9DCG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.