LETM1_RAT
ID LETM1_RAT Reviewed; 739 AA.
AC Q5XIN6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 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=Testis;
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 451-462 AND 492-513, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Hippocampus;
RA Lubec G., Diao W., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=18628306; DOI=10.1242/jcs.026625;
RA Tamai S., Iida H., Yokota S., Sayano T., Kiguchiya S., Ishihara N.,
RA Hayashi J., Mihara K., Oka T.;
RT "Characterization of the mitochondrial protein LETM1, which maintains the
RT mitochondrial tubular shapes and interacts with the AAA-ATPase BCS1L.";
RL J. Cell Sci. 121:2588-2600(2008).
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 -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18628306}.
CC -!- SIMILARITY: Belongs to the LETM1 family. {ECO:0000305}.
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DR EMBL; BC083642; AAH83642.1; -; mRNA.
DR RefSeq; NP_001005884.1; NM_001005884.1.
DR AlphaFoldDB; Q5XIN6; -.
DR SMR; Q5XIN6; -.
DR BioGRID; 258178; 2.
DR IntAct; Q5XIN6; 1.
DR MINT; Q5XIN6; -.
DR STRING; 10116.ENSRNOP00000022540; -.
DR CarbonylDB; Q5XIN6; -.
DR iPTMnet; Q5XIN6; -.
DR PhosphoSitePlus; Q5XIN6; -.
DR jPOST; Q5XIN6; -.
DR PaxDb; Q5XIN6; -.
DR PRIDE; Q5XIN6; -.
DR Ensembl; ENSRNOT00000022540; ENSRNOP00000022540; ENSRNOG00000016427.
DR GeneID; 305457; -.
DR KEGG; rno:305457; -.
DR CTD; 3954; -.
DR RGD; 1359678; Letm1.
DR eggNOG; KOG1043; Eukaryota.
DR GeneTree; ENSGT00950000183167; -.
DR HOGENOM; CLU_008958_2_1_1; -.
DR InParanoid; Q5XIN6; -.
DR OMA; EILHYYH; -.
DR OrthoDB; 516860at2759; -.
DR PhylomeDB; Q5XIN6; -.
DR TreeFam; TF316321; -.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR PRO; PR:Q5XIN6; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000016427; Expressed in adult mammalian kidney and 19 other tissues.
DR Genevisible; Q5XIN6; RN.
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:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0015369; F:calcium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0042407; P:cristae formation; ISO:RGD.
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; 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; PS51758; LETM1_RBD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antiport; Calcium; Calcium transport; Coiled coil;
KW Direct protein sequencing; Ion transport; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..114
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 115..739
FT /note="Mitochondrial proton/calcium exchanger protein"
FT /id="PRO_0000017696"
FT TOPO_DOM 115..207
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..739
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT DOMAIN 251..536
FT /note="Letm1 RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01094"
FT DOMAIN 663..698
FT /note="EF-hand"
FT REGION 717..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 115..135
FT /evidence="ECO:0000255"
FT COILED 445..492
FT /evidence="ECO:0000255"
FT COILED 537..626
FT /evidence="ECO:0000255"
FT COILED 707..738
FT /evidence="ECO:0000255"
FT BINDING 676
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 678
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 680
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 682
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 687
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT MOD_RES 596
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95202"
SQ SEQUENCE 739 AA; 83060 MW; 726DE7D0EAB54331 CRC64;
MASILLRSCR GRGPARLASP RAASPRGSLR DRACLSCTRT VGLTSHESVL SRCCTPANPV
YLYFKSEPLS CWTQRPECQG TVARAAWTPA SARLVVTGPQ YLPVRGWHSS SPLGEDSMIE
KSLKSLKDKN KKLEEGGPVY SPPAQVVVKK SLGQKILDEL KHYYHGFRLL WIDTKIAARM
LWRILNGHTL TRRERRQFLR ICADLFRLVP FLVFVVVPFM EFLLPVVVKL FPNMLPSTFE
TQSIKEERLK KELRVKLELA KFLQDTIEEM ALKNKAAKGN ATKDFSAFFQ KIRETGERPS
NEEIMRFSKL FEDELTLDNL TRPQLVALCK LLELQSIGTN NFLRFQLTMR LRSIKADDKL
ISEEGVDSLT VKELQAACRA RGMRALGVTE DRLKGQLKQW LDLHLYHEIP TSLLILSRAM
YLPDTLSPAD QLKSTLQTLP EIVAKEAQVK AAEVEGEQVD NKAKLEATLQ EEAAIQQEHL
EELKRAAETA KDIQPEVAEA TVPGRPGAEL QPKMVDVIPP SEILKDTAPV LEGLKGEEIT
KEEIDILSDA CSKLKEQKKS LTKEKEELEL LKEDVQDYSE DLQEIKKELS KTGDEKYIEE
STASKRLSKR VQQMIGQIDG LITQLETTQQ NGKLDPAAAS SPTGESVISV DELISAMKQI
KHIPEHKLIS LTSALDENKD GNINIDDLVK VIDLVNKEDV QISTTQVAEI VATLEKEEKV
EEKEKAKEKA EKEAAEVKN
