STML2_BOVIN
ID STML2_BOVIN Reviewed; 356 AA.
AC Q32LL2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Stomatin-like protein 2, mitochondrial;
DE Short=SLP-2;
DE Flags: Precursor;
GN Name=STOML2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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 with this mediator of mitochondrial fusion. Interacts
CC with PHB1 and PHB2; stabilizes and recruits them to cardiolipin-
CC enriched mitochondrial membranes. Interacts with CACNA2D2 (By
CC 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; BC109523; AAI09524.1; -; mRNA.
DR RefSeq; NP_001033157.1; NM_001038068.1.
DR AlphaFoldDB; Q32LL2; -.
DR SMR; Q32LL2; -.
DR STRING; 9913.ENSBTAP00000015136; -.
DR PaxDb; Q32LL2; -.
DR PeptideAtlas; Q32LL2; -.
DR PRIDE; Q32LL2; -.
DR GeneID; 510324; -.
DR KEGG; bta:510324; -.
DR CTD; 30968; -.
DR eggNOG; KOG2620; Eukaryota.
DR InParanoid; Q32LL2; -.
DR OrthoDB; 1237942at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB.
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:1901612; F:cardiolipin binding; ISS:UniProtKB.
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 2: Evidence at transcript 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..356
FT /note="Stomatin-like protein 2, mitochondrial"
FT /id="PRO_0000262587"
FT REGION 326..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 215..252
FT /evidence="ECO:0000255"
FT COMPBIAS 340..356
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 356 AA; 38733 MW; 3810D5B43996982F CRC64;
MLARAARGTG ALLLKGSVQA SARAPRRASS GLPRNTVVLF VPQQEAWVVE RMGRFHRILE
PGLNILIPVL DRIRYVQSLK EIVINVPEQS AVTLDNVTLQ IDGVLYLRIM DPYKASYGVE
DPEYAVTQLA QTTMRSELGK LSLDKVFRER ESLNASIVDA INQAADCWGI RCLRYEIKDI
HVPPRVKESM KMQVEAERRK RATVLESEGT RESAINVAEG KKQAQILASE AEKAEQINQA
AGEASAVLAK AKAKAEAIRI LAAALTQHNG DAAASLTVAE QYVSAFSKLA KDSNTILLPS
NPGDVTSMVA QAMGVYGALT KAPIPEAQDS VSSRSSRDVR STDASLDEEL DRVKLS
