LETM1_DROME
ID LETM1_DROME Reviewed; 1013 AA.
AC P91927; A4UZV1; Q0E8W7; Q9W160;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Mitochondrial proton/calcium exchanger protein {ECO:0000305};
DE AltName: Full=Leucine zipper-EF-hand-containing transmembrane protein 1;
DE Short=dLetm1 {ECO:0000303|PubMed:19797662};
DE Flags: Precursor;
GN Name=Letm1; Synonyms=anon-60Da; ORFNames=CG4589;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 626-944.
RC TISSUE=Ovary;
RX PubMed=10071211; DOI=10.1007/s004380050942;
RA Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R.,
RA Barsanti P.;
RT "Identification of nuclear genes encoding mitochondrial proteins: isolation
RT of a collection of D. melanogaster cDNAs homologous to sequences in the
RT Human Gene Index database.";
RL Mol. Gen. Genet. 261:64-70(1999).
RN [5]
RP FUNCTION.
RX PubMed=19797662; DOI=10.1126/science.1175145;
RA Jiang D., Zhao L., Clapham D.E.;
RT "Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+
RT antiporter.";
RL Science 326:144-147(2009).
CC -!- FUNCTION: Mitochondrial proton/calcium antiporter that mediates proton-
CC dependent calcium efflux from mitochondrion.
CC {ECO:0000305|PubMed:19797662}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O95202}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the LETM1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA71853.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAM68316.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68317.1; -; Genomic_DNA.
DR EMBL; AY047527; AAK77259.1; -; mRNA.
DR EMBL; Y10912; CAA71853.1; ALT_FRAME; mRNA.
DR RefSeq; NP_611922.1; NM_138078.3.
DR RefSeq; NP_726453.1; NM_166674.2.
DR RefSeq; NP_726454.1; NM_166675.2.
DR AlphaFoldDB; P91927; -.
DR SMR; P91927; -.
DR BioGRID; 63485; 6.
DR DIP; DIP-23753N; -.
DR IntAct; P91927; 7.
DR STRING; 7227.FBpp0072255; -.
DR TCDB; 2.A.97.1.3; the mitochondrial inner membrane k(+)/h(+) and ca(2+)/h(+) exchanger (letm1) family.
DR PaxDb; P91927; -.
DR PRIDE; P91927; -.
DR EnsemblMetazoa; FBtr0072347; FBpp0072254; FBgn0284252.
DR EnsemblMetazoa; FBtr0072348; FBpp0072255; FBgn0284252.
DR EnsemblMetazoa; FBtr0072349; FBpp0072256; FBgn0284252.
DR GeneID; 37912; -.
DR KEGG; dme:Dmel_CG4589; -.
DR UCSC; CG4589-RA; d. melanogaster.
DR CTD; 3954; -.
DR FlyBase; FBgn0284252; Letm1.
DR VEuPathDB; VectorBase:FBgn0284252; -.
DR eggNOG; KOG1043; Eukaryota.
DR GeneTree; ENSGT00950000183167; -.
DR HOGENOM; CLU_008958_1_0_1; -.
DR InParanoid; P91927; -.
DR OMA; PVQHKEH; -.
DR OrthoDB; 516860at2759; -.
DR PhylomeDB; P91927; -.
DR SignaLink; P91927; -.
DR GenomeRNAi; 37912; -.
DR PRO; PR:P91927; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0284252; Expressed in adult hindgut (Drosophila) and 34 other tissues.
DR Genevisible; P91927; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005432; F:calcium:sodium antiporter activity; IDA:FlyBase.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IMP:FlyBase.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0006875; P:cellular metal ion homeostasis; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IMP:FlyBase.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IMP:FlyBase.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:FlyBase.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:FlyBase.
DR GO; GO:1902600; P:proton transmembrane transport; IMP:FlyBase.
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; PF13202; EF-hand_5; 2.
DR Pfam; PF07766; LETM1; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
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; Repeat; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..60
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 61..1013
FT /note="Mitochondrial proton/calcium exchanger protein"
FT /id="PRO_0000073861"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 280..554
FT /note="Letm1 RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01094"
FT DOMAIN 687..722
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 770..805
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 877..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..131
FT /evidence="ECO:0000255"
FT COILED 488..525
FT /evidence="ECO:0000255"
FT COILED 573..653
FT /evidence="ECO:0000255"
FT COILED 823..919
FT /evidence="ECO:0000255"
FT COMPBIAS 877..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 700
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 702
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 704
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 711
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 783
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 785
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 787
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 794
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CONFLICT 687
FT /note="E -> Q (in Ref. 4; CAA71853)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="K -> G (in Ref. 4; CAA71853)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="Q -> H (in Ref. 4; CAA71853)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="E -> D (in Ref. 4; CAA71853)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="K -> R (in Ref. 4; CAA71853)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="K -> E (in Ref. 4; CAA71853)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="G -> S (in Ref. 4; CAA71853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1013 AA; 113580 MW; 8C710380263F262E CRC64;
MNALLRHKGR NLRTSHLAQN VYKRFLKSNC CACSSVNVTD EPAKEDELPR RSASTSVLEL
SRSLGTYRRF QPHANYGYDY SGYGFRHLHT SRTLLETSSS KIDATVKKLK NQQKEKVEEI
MKEVANGQAA AVRASSAATA TASSEKGQNA SATAGSTSAT ASTTSLAKTA DKSVAKPKKP
LRTRIWDELV HYYHGFRLLF IDVAICSKLL WRVLNGKTLT RRENKQLQRT TSDLFRLIPF
SVFIIVPFME LLLPLFIKFF PGMLPSTFQT STDRQEKLRQ SLSVRLEVAK FLQQTLDQMP
VQHKEHSSEE AKQFEAFFTK IRNPTEPVSN DEIIKFAKRF DDEITLDSLS REQLAALCRV
LELNTIGTTT LLRFQLRLKL RSLATDDRVI AREGVDSLDL LELQQACKAR GMRAYGLTEE
RLRFQLKEWI DLSLNEQVPP TLLLLSRTML ISDDSITTDK LKETIRVLPD AVGAHTRHAI
GESEGKVDNK TKIEIIKEEE RKIREEREEE REETIAKRSA IKEEIPAPYV FAEKLSGSQD
LLDHKEQSSV SETDKGISST DVQLLSEALK TLSSDKQLVV EKETIKELKE ELADYKEDVE
ELREVRQVVK EPVRESRAAK LLYNRVNKMI SQLDNVLNDL EARQHQIKQA ESSDYAASSP
TVEPQQMVHI DELVATIRRM KEASDEERFK VVGDLLVKLD ADKDGVISVN EITKAVQSID
REATNIDKKQ LEEFTELLSK LASRRRHEEI VHIDDLMNNI KVLKETSDEA RLKHIEAVLE
KFDADKDGVV TVNDIRKVLE SIGRDNIKLS DKAIEELISL LDKEQVLQAE QKIEKAIAKS
MKEAEKLKSE VDKADKDLSK LVNDIHDSAK EIQDIANEMR DKEETVPDKA KELKAEPAFK
DTAKTLKDNA KDLDDLAKDP KSDPKSPTKA STGSGPAGLS GGGPSSGSSG IATGSTTESA
LREAAERQME KILPSTDIGL PPTIQTPSQP PTSKKATATA STLSTTITAK KLL
