LTMD1_MOUSE
ID LTMD1_MOUSE Reviewed; 360 AA.
AC Q924L1; Q3TF05; Q3U3M7; Q8BLG9; Q8K1F7; Q8VDS9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=LETM1 domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Cervical cancer receptor;
DE AltName: Full=MCC-32;
GN Name=Letmd1 {ECO:0000312|MGI:MGI:1915864}; Synonyms=Mccr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C3H/He;
RA Hwang J.H., Kim J.W., Hwang S.Y.;
RT "Mouse cervical cancer receptor.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=FVB/NJ; TISSUE=Kidney;
RA Kim J.W.;
RT "Identification of a mouse cDNA (MCC) homologous to human HCCR-1 and HCCR-2
RT gene.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Embryo, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [5]
RP FUNCTION.
RX PubMed=12879013; DOI=10.1038/sj.onc.1206624;
RA Ko J., Lee Y.H., Hwang S.Y., Lee Y.S., Shin S.M., Hwang J.H., Kim J.,
RA Kim Y.W., Jang S.-W., Ryoo Z.Y., Kim I.-K., Namkoong S.E., Kim J.W.;
RT "Identification and differential expression of novel human cervical cancer
RT oncogene HCCR-2 in human cancers and its involvement in p53
RT stabilization.";
RL Oncogene 22:4679-4689(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=34669999; DOI=10.1096/fj.202100597r;
RA Snyder M.M., Yue F., Zhang L., Shang R., Qiu J., Chen J., Kim K.H.,
RA Peng Y., Oprescu S.N., Donkin S.S., Bi P., Kuang S.;
RT "LETMD1 is required for mitochondrial structure and thermogenic function of
RT brown adipocytes.";
RL FASEB J. 35:e21965-e21965(2021).
CC -!- FUNCTION: Involved in tumorigenesis and may function as a negative
CC regulator of the p53/TP53 (PubMed:12879013). May play an essential role
CC for mitochondrial structure and function, and thermogenesis of brown
CC adipocytes (PubMed:34669999). May regulate phagocytosis and
CC inflammatory responses to lipopolysaccharide in macrophages (By
CC similarity). {ECO:0000250|UniProtKB:Q6P1Q0,
CC ECO:0000269|PubMed:12879013, ECO:0000269|PubMed:34669999}.
CC -!- SUBUNIT: Interacts with BRI3BP. {ECO:0000250|UniProtKB:Q6P1Q0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q6P1Q0}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q6P1Q0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q924L1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924L1-2; Sequence=VSP_029281;
CC Name=3;
CC IsoId=Q924L1-3; Sequence=VSP_029280;
CC -!- TISSUE SPECIFICITY: Highly expressed in brown adipose tissue (BAT).
CC {ECO:0000269|PubMed:34669999}.
CC -!- INDUCTION: Up-regulated in adipose tissues upon cold exposure.
CC {ECO:0000269|PubMed:34669999}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mice for Letmd1 gene are born at
CC normal Mendelian ratios, with normal morphology, bodyweight and body
CC composition at 2-months old (PubMed:34669999). Mice could not tolerate
CC cold exposure without food (PubMed:34669999).
CC {ECO:0000269|PubMed:34669999}.
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DR EMBL; AF287293; AAK83032.1; -; mRNA.
DR EMBL; AF401483; AAM90666.1; -; mRNA.
DR EMBL; AK045256; BAC32283.1; -; mRNA.
DR EMBL; AK080221; BAC37851.1; -; mRNA.
DR EMBL; AK154676; BAE32758.1; -; mRNA.
DR EMBL; AK169341; BAE41093.1; -; mRNA.
DR EMBL; BC021361; AAH21361.1; -; mRNA.
DR CCDS; CCDS27838.1; -. [Q924L1-1]
DR CCDS; CCDS88844.1; -. [Q924L1-2]
DR CCDS; CCDS88845.1; -. [Q924L1-3]
DR RefSeq; NP_598854.1; NM_134093.2. [Q924L1-1]
DR RefSeq; XP_006521384.1; XM_006521321.3.
DR RefSeq; XP_006521385.1; XM_006521322.1. [Q924L1-3]
DR RefSeq; XP_006521386.1; XM_006521323.3.
DR RefSeq; XP_017172228.1; XM_017316739.1. [Q924L1-3]
DR AlphaFoldDB; Q924L1; -.
DR SMR; Q924L1; -.
DR BioGRID; 212953; 3.
DR STRING; 10090.ENSMUSP00000037546; -.
DR iPTMnet; Q924L1; -.
DR PhosphoSitePlus; Q924L1; -.
DR SwissPalm; Q924L1; -.
DR EPD; Q924L1; -.
DR jPOST; Q924L1; -.
DR MaxQB; Q924L1; -.
DR PaxDb; Q924L1; -.
DR PeptideAtlas; Q924L1; -.
DR PRIDE; Q924L1; -.
DR ProteomicsDB; 252683; -. [Q924L1-1]
DR ProteomicsDB; 252684; -. [Q924L1-2]
DR ProteomicsDB; 252685; -. [Q924L1-3]
DR Antibodypedia; 26304; 162 antibodies from 21 providers.
DR DNASU; 68614; -.
DR Ensembl; ENSMUST00000037001; ENSMUSP00000037546; ENSMUSG00000037353. [Q924L1-1]
DR Ensembl; ENSMUST00000229648; ENSMUSP00000155084; ENSMUSG00000037353. [Q924L1-2]
DR Ensembl; ENSMUST00000230294; ENSMUSP00000155807; ENSMUSG00000037353. [Q924L1-3]
DR GeneID; 68614; -.
DR KEGG; mmu:68614; -.
DR UCSC; uc007xrg.2; mouse. [Q924L1-1]
DR CTD; 25875; -.
DR MGI; MGI:1915864; Letmd1.
DR VEuPathDB; HostDB:ENSMUSG00000037353; -.
DR eggNOG; KOG4263; Eukaryota.
DR GeneTree; ENSGT00950000183167; -.
DR HOGENOM; CLU_049801_1_0_1; -.
DR InParanoid; Q924L1; -.
DR OMA; LVFWYPR; -.
DR OrthoDB; 756155at2759; -.
DR PhylomeDB; Q924L1; -.
DR TreeFam; TF314047; -.
DR BioGRID-ORCS; 68614; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Letmd1; mouse.
DR PRO; PR:Q924L1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q924L1; protein.
DR Bgee; ENSMUSG00000037353; Expressed in brown adipose tissue and 250 other tissues.
DR ExpressionAtlas; Q924L1; baseline and differential.
DR Genevisible; Q924L1; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:InterPro.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:MGI.
DR GO; GO:0050764; P:regulation of phagocytosis; ISO:MGI.
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 PROSITE; PS51758; LETM1_RBD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..360
FT /note="LETM1 domain-containing protein 1"
FT /id="PRO_0000310420"
FT TOPO_DOM 1..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..360
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DOMAIN 178..360
FT /note="Letm1 RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01094"
FT REGION 1..110
FT /note="Required and sufficient for mitochondrial import"
FT /evidence="ECO:0000250"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029280"
FT VAR_SEQ 1..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_029281"
FT CONFLICT 20
FT /note="P -> T (in Ref. 3; BAE41093)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="H -> Q (in Ref. 2; AAM90666)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="H -> N (in Ref. 3; BAE32758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 41701 MW; 4689BC4F3D2A0BBD CRC64;
MALSRVCWAR AALWGSTVAP GPFVTRRLQL GRSGPAWRAP RSSKLHLSPK ADVKNLISYV
VTKTRAINGS YHRFLGRHFP RFYALYTTFM KGIQMLWADG KKARRIKADM WKQNLKFHQL
SYREMEHLRQ FRRDITKCLF VGLISIPPFA NYLVFLLMYL FPRQLLVKHF WTPKQQIDFL
DVYHGLRRRS HSEVITHLRR ASTFVSHEKL RRQLTDLCTK VQSGTHPAAQ DVLALRDCFS
TYPLGFSQLQ ASQMRALSQA MLLTPYLPPP LLRQRLKSHT TVIHQLDRAL AKLGIGQLTA
QEVKSACYLR GLNSTHIADD RCRAWLGEWL HISCSLKEPE LSLLLHNVVL LSTNYLETRR
