LETM1_DANRE
ID LETM1_DANRE Reviewed; 757 AA.
AC Q1LY46; B8JIA3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 93.
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; ORFNames=si:ch211-195n12.1, si:rp71-77d7.1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Mitochondrial proton/calcium antiporter that mediates proton-
CC dependent calcium efflux from mitochondrion (By similarity). Required
CC for the maintenance of the tubular shape and cristae organization (By
CC similarity). {ECO:0000250|UniProtKB:O95202,
CC ECO:0000250|UniProtKB:Q9Z2I0}.
CC -!- SUBUNIT: Homohexamer. {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; BX119973; CAK03660.1; -; Genomic_DNA.
DR EMBL; CR556722; CAX14247.1; -; Genomic_DNA.
DR RefSeq; NP_001038673.1; NM_001045208.1.
DR AlphaFoldDB; Q1LY46; -.
DR SMR; Q1LY46; -.
DR STRING; 7955.ENSDARP00000074011; -.
DR PaxDb; Q1LY46; -.
DR Ensembl; ENSDART00000079558; ENSDARP00000074011; ENSDARG00000056978.
DR GeneID; 570745; -.
DR KEGG; dre:570745; -.
DR CTD; 3954; -.
DR ZFIN; ZDB-GENE-050522-154; letm1.
DR eggNOG; KOG1043; Eukaryota.
DR GeneTree; ENSGT00950000183167; -.
DR HOGENOM; CLU_008958_2_1_1; -.
DR InParanoid; Q1LY46; -.
DR OrthoDB; 516860at2759; -.
DR PhylomeDB; Q1LY46; -.
DR TreeFam; TF316321; -.
DR Reactome; R-DRE-9013408; RHOG GTPase cycle.
DR PRO; PR:Q1LY46; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000056978; Expressed in testis and 26 other tissues.
DR ExpressionAtlas; Q1LY46; baseline.
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:0034214; P:protein hexamerization; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; 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 3: Inferred from homology;
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..113
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 114..757
FT /note="Mitochondrial proton/calcium exchanger protein"
FT /id="PRO_0000380703"
FT TOPO_DOM 114..215
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..757
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT DOMAIN 259..552
FT /note="Letm1 RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01094"
FT DOMAIN 680..715
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT COILED 476..521
FT /evidence="ECO:0000255"
FT COILED 554..618
FT /evidence="ECO:0000255"
FT COILED 722..755
FT /evidence="ECO:0000255"
FT BINDING 693
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 695
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 697
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 699
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 704
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CONFLICT 72
FT /note="R -> L (in Ref. 1; CAK03660)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 86847 MW; 0B56E039E49589AE CRC64;
MASILLTRSR TPLLKTSRSL KNEFRKGKLS EGACFNCTAL RLATNSPGVL GGIVWPHASS
VQYLDNSSVL QRRLSRSPRL YCAILVPDPA LPVHSRSTYH RTLAWPQNAP VRWVHTTGRL
LDDSKVERSL RTLKDRNKKL EEGGPVYSPT VDAEPVRRTI RQRVIDEVKH YYHGFRLLWI
DTTIAVRMLW RVLNGHILSR RERRQFLRTC ADVFRLLPFL VFIIVPFMEF LLPVALKLFP
NMLPSTFETQ SKKEERLKKE LRVKLEMAKF LQDTIEEIAL RNKASKGNVT EEFSTFFQKI
RDSGEIPSNE QIIRFSKLFE DELTLDNLTR PQLVALCKLL ELQSIGTNNF LRFQLIMKLR
AIRADDKLIA EEGVDSLTAN ELQAACRVRG MRALGVTEER LREQLKQWLE LHLNQHIPTS
LLLLSRAMFL PDTLSPADQL KTTLQNLPEI MAKEAQVKVA ELDFSKVDNK TKLETTLQEE
AAIRQENRER ELERLADAAE KAKEQTQSQE AEVLEVEGER RVDAEHALSS VDVAIHSETL
RDTAPVLEGI KGEEITKEEI DMLSDACTKL KEQKNLLTKE KEELEDLKDD VQEYSEDLEE
IKRELSKTGQ EKAVEESKAS QRLSKRVNRM IGRMDKIITE LEKDKMVLDG QMDSETTPPI
GENLISINEL ITVMKQIQNI PEHKLLSIAD ALDENKDGKI DIDDVIKVVE LIDKEDIDIS
TNQVAEIMVM LQKEEKLMEK EKAKEKVEKE QAAKIQN
