LETM1_BOVIN
ID LETM1_BOVIN Reviewed; 732 AA.
AC Q0VCA3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Mitochondrial proton/calcium exchanger protein {ECO:0000305};
DE AltName: Full=Leucine zipper-EF-hand-containing transmembrane protein 1;
DE Flags: Precursor;
GN Name=LETM1;
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=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mitochondrial proton/calcium antiporter that mediates proton-
CC dependent calcium efflux from mitochondrion (By similarity). Crucial
CC for the maintenance of mitochondrial tubular networks and for the
CC assembly of the supercomplexes of the respiratory chain (By
CC similarity). Required for the maintenance of the tubular shape and
CC cristae organization (By similarity). In contrast to SLC8B1/NCLX, does
CC not constitute the major factor for mitochondrial calcium extrusion (By
CC similarity). {ECO:0000250|UniProtKB:O95202,
CC ECO:0000250|UniProtKB:Q9Z2I0}.
CC -!- ACTIVITY REGULATION: Inhibited by ruthenium red or its derivative
CC Ru360. {ECO:0000250|UniProtKB:O95202}.
CC -!- SUBUNIT: Homohexamer (By similarity). Interacts with BCS1L (By
CC similarity). {ECO:0000250|UniProtKB:O95202,
CC ECO:0000250|UniProtKB:Q9Z2I0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9Z2I0}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9Z2I0}.
CC -!- SIMILARITY: Belongs to the LETM1 family. {ECO:0000305}.
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DR EMBL; BC120274; AAI20275.1; -; mRNA.
DR RefSeq; NP_001069082.1; NM_001075614.2.
DR AlphaFoldDB; Q0VCA3; -.
DR SMR; Q0VCA3; -.
DR STRING; 9913.ENSBTAP00000026785; -.
DR PaxDb; Q0VCA3; -.
DR PeptideAtlas; Q0VCA3; -.
DR PRIDE; Q0VCA3; -.
DR GeneID; 513324; -.
DR KEGG; bta:513324; -.
DR CTD; 3954; -.
DR eggNOG; KOG1043; Eukaryota.
DR InParanoid; Q0VCA3; -.
DR OrthoDB; 516860at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0015369; F:calcium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0099093; P:calcium export from the mitochondrion; ISS:UniProtKB.
DR GO; GO:0006875; P:cellular metal ion homeostasis; IBA:GO_Central.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0051562; P:negative regulation of mitochondrial calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0034214; P:protein hexamerization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:1900069; P:regulation of cellular hyperosmotic salinity response; ISS:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011685; LETM1-like.
DR InterPro; IPR044202; LETM1/MDM38-like.
DR InterPro; IPR033122; LETM1_RBD.
DR PANTHER; PTHR14009; PTHR14009; 1.
DR Pfam; PF07766; LETM1; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51758; LETM1_RBD; 1.
PE 2: Evidence at transcript level;
KW Antiport; Calcium; Calcium transport; Coiled coil; Ion transport; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..93
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 94..732
FT /note="Mitochondrial proton/calcium exchanger protein"
FT /id="PRO_0000380701"
FT TOPO_DOM 94..194
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..732
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT DOMAIN 238..529
FT /note="Letm1 RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01094"
FT DOMAIN 656..691
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 711..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 448..478
FT /evidence="ECO:0000255"
FT COILED 528..620
FT /evidence="ECO:0000255"
FT COILED 701..732
FT /evidence="ECO:0000255"
FT BINDING 669
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 671
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 673
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 675
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 680
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 732 AA; 81818 MW; 9AAF671DA1772D90 CRC64;
MASILLRSCR GRGPARLPPP RSAAPRGPAG DLACLSGASA VGLMSYVPLP LGSCAPVRPV
YLSLRADPLG CWTLRPKRAC AVLAGPRLLP VRCWHSSRPL GDDSVVEKSL RSLKDKNKKL
EEGGPVYSPP AQAAVRKPLG QRVLDELRHY YHGFRLLWID TKIAARMLWR ILHGHSLTRR
ERRQFLRICA DLFRLVPFLF FVVVPFMEFL LPVAVKLFPN MLPSTFETQS SKEERLKKEL
RVKLELAKFL QDTIEEMALK NKAAKGSATK DFSVFFQKIR ETGERPSNEE IMRFSKLFED
ELTLDNLTRP QLVALCKLLE LQSIGTNNFL RFQLTMRLRS IKADDKLIAE EGVDSLNVKE
LQAACRARGM RALGVTEDRL RGQLKQWLEL HLHQEIPTSL LILSRAMYLP ETLSPADQLK
STLQTLPEIV AKEAQVKVAE VEGEQVDNKA KLEATLQEEA AIQQEHREKE LQRKSQAAVA
QAAKEVEPEV VAEGAPGRPV AELQPEEPAV TLPSEVLKDS APVLEGLKEE EITQEEIDVL
SNACSKLKEQ KKSLTKEKEE LELLKGDVQD YSQDLQEIKK ELSKTGEEMY VEESKASKRL
TKRVQQMIGQ MDSLLAQLEA DQKAGRLGPA AEAAPAGETV ISVSELINAM KQIKHIPESK
LLSLASALDD NKDGKVDIDD LVKVIELVDK EDVHISTSQV AEIVATLEKE EKVEEKEKAK
EKAEKEAAEV QN
