STML2_RAT
ID STML2_RAT Reviewed; 353 AA.
AC Q4FZT0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Stomatin-like protein 2, mitochondrial;
DE Short=SLP-2;
DE Flags: Precursor;
GN Name=Stoml2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP PROTEIN SEQUENCE OF 58-72; 202-221 AND 322-334, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms homooligomers. Interacts with MFN2; may form
CC heterooligomers. Interacts with PHB1 and PHB2; recruits them to
CC cardiolipin-enriched mitochondrial membranes and stabilizes them.
CC Interacts with CACNA2D2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UJZ1};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9UJZ1}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9UJZ1}. 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 -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
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DR EMBL; BC099164; AAH99164.1; -; mRNA.
DR RefSeq; NP_001026816.1; NM_001031646.1.
DR AlphaFoldDB; Q4FZT0; -.
DR SMR; Q4FZT0; -.
DR BioGRID; 255804; 4.
DR IntAct; Q4FZT0; 2.
DR MINT; Q4FZT0; -.
DR STRING; 10116.ENSRNOP00000013151; -.
DR iPTMnet; Q4FZT0; -.
DR PhosphoSitePlus; Q4FZT0; -.
DR jPOST; Q4FZT0; -.
DR PaxDb; Q4FZT0; -.
DR PRIDE; Q4FZT0; -.
DR Ensembl; ENSRNOT00000013151; ENSRNOP00000013151; ENSRNOG00000009535.
DR GeneID; 298203; -.
DR KEGG; rno:298203; -.
DR UCSC; RGD:1308285; rat.
DR CTD; 30968; -.
DR RGD; 1308285; Stoml2.
DR eggNOG; KOG2620; Eukaryota.
DR GeneTree; ENSGT01030000234614; -.
DR HOGENOM; CLU_024949_1_0_1; -.
DR InParanoid; Q4FZT0; -.
DR OMA; TQIRAEM; -.
DR OrthoDB; 1237942at2759; -.
DR PhylomeDB; Q4FZT0; -.
DR TreeFam; TF105750; -.
DR Reactome; R-RNO-8949664; Processing of SMDT1.
DR PRO; PR:Q4FZT0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009535; Expressed in ovary and 20 other tissues.
DR Genevisible; Q4FZT0; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042101; C:T cell receptor complex; IEA:Ensembl.
DR GO; GO:1901612; F:cardiolipin binding; ISS:UniProtKB.
DR GO; GO:0051020; F:GTPase binding; ISO:RGD.
DR GO; GO:0035710; P:CD4-positive, alpha-beta T cell activation; ISS:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0010876; P:lipid localization; ISS:UniProtKB.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0034982; P:mitochondrial protein processing; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:1990046; P:stress-induced mitochondrial fusion; ISS: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 Direct protein sequencing; Lipid-binding; Lipoprotein; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; 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_0000288494"
FT REGION 324..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 215..252
FT /evidence="ECO:0000255"
FT COMPBIAS 338..353
FT /note="Basic and acidic 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:0000250|UniProtKB:Q9UJZ1"
FT MOD_RES 145
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99JB2"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJZ1"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJZ1"
SQ SEQUENCE 353 AA; 38414 MW; 9E8ED01781B7B08A CRC64;
MLARAARGTG ALLLRGSVQA SGRIPRRASS 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 SEARRDVQTT DTSIEELGRV KLS
