SELM_MOUSE
ID SELM_MOUSE Reviewed; 145 AA.
AC Q8VHC3; B2RVS9; Q3V374; Q8CBT7; Q8VCJ0;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Selenoprotein M {ECO:0000303|PubMed:11839807};
DE Short=SelM {ECO:0000303|PubMed:11839807};
DE Flags: Precursor;
GN Name=Selenom {ECO:0000312|MGI:MGI:2149786};
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11839807; DOI=10.1128/mcb.22.5.1402-1411.2002;
RA Korotkov K.V., Novoselov S.V., Hatfield D.L., Gladyshev V.N.;
RT "Mammalian selenoprotein in which selenocysteine (Sec) incorporation is
RT supported by a new form of Sec insertion sequence element.";
RL Mol. Cell. Biol. 22:1402-1411(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Corpora quadrigemina, and Urinary bladder;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Pancreas, and Testis;
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 [5]
RP STRUCTURE BY NMR OF 25-145.
RX PubMed=16319061; DOI=10.1074/jbc.m511386200;
RA Ferguson A.D., Labunskyy V.M., Fomenko D.E., Arac D., Chelliah Y.,
RA Amezcua C.A., Rizo J., Gladyshev V.N., Deisenhofer J.;
RT "NMR structures of the selenoproteins Sep15 and SelM reveal redox activity
RT of a new thioredoxin-like family.";
RL J. Biol. Chem. 281:3536-3543(2006).
CC -!- FUNCTION: May function as a thiol-disulfide oxidoreductase that
CC participates in disulfide bond formation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:11839807}. Endoplasmic reticulum
CC {ECO:0000305|PubMed:11839807}. Golgi apparatus
CC {ECO:0000305|PubMed:11839807}. Note=Localized to perinuclear structures
CC corresponding to Golgi and endoplasmic reticulum.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain.
CC {ECO:0000269|PubMed:11839807}.
CC -!- SIMILARITY: Belongs to the selenoprotein M/F family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19742.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY043488; AAK95398.1; -; mRNA.
DR EMBL; AK018791; BAE43252.1; -; mRNA.
DR EMBL; AK035312; BAC29028.2; -; mRNA.
DR EMBL; AK046034; BAE43327.1; -; mRNA.
DR EMBL; BC019742; AAH19742.1; ALT_SEQ; mRNA.
DR EMBL; BC147332; AAI47333.1; -; mRNA.
DR EMBL; BC147333; AAI47334.1; -; mRNA.
DR CCDS; CCDS24365.1; -.
DR RefSeq; NP_444497.1; NM_053267.3.
DR PDB; 2A2P; NMR; -; A=25-145.
DR PDBsum; 2A2P; -.
DR SMR; Q8VHC3; -.
DR STRING; 10090.ENSMUSP00000092041; -.
DR iPTMnet; Q8VHC3; -.
DR PhosphoSitePlus; Q8VHC3; -.
DR MaxQB; Q8VHC3; -.
DR PaxDb; Q8VHC3; -.
DR PeptideAtlas; Q8VHC3; -.
DR PRIDE; Q8VHC3; -.
DR ProteomicsDB; 257116; -.
DR Antibodypedia; 5738; 132 antibodies from 19 providers.
DR DNASU; 114679; -.
DR Ensembl; ENSMUST00000094469; ENSMUSP00000092041; ENSMUSG00000075702.
DR GeneID; 114679; -.
DR KEGG; mmu:114679; -.
DR UCSC; uc007htd.1; mouse.
DR CTD; 140606; -.
DR MGI; MGI:2149786; Selenom.
DR VEuPathDB; HostDB:ENSMUSG00000075702; -.
DR eggNOG; ENOG502S29K; Eukaryota.
DR GeneTree; ENSGT00940000154284; -.
DR HOGENOM; CLU_140417_0_0_1; -.
DR InParanoid; Q8VHC3; -.
DR OMA; TFRPDWN; -.
DR OrthoDB; 1621104at2759; -.
DR PhylomeDB; Q8VHC3; -.
DR TreeFam; TF333248; -.
DR BioGRID-ORCS; 114679; 4 hits in 71 CRISPR screens.
DR EvolutionaryTrace; Q8VHC3; -.
DR PRO; PR:Q8VHC3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VHC3; protein.
DR Bgee; ENSMUSG00000075702; Expressed in cerebellar cortex and 236 other tissues.
DR Genevisible; Q8VHC3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0060612; P:adipose tissue development; IMP:MGI.
DR GO; GO:0035934; P:corticosterone secretion; IMP:MGI.
DR GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0010269; P:response to selenium ion; IMP:MGI.
DR Gene3D; 3.40.30.50; -; 1.
DR InterPro; IPR038219; Sep15/SelM_sf.
DR InterPro; IPR039992; Sep15_SelM.
DR InterPro; IPR014912; Sep15_SelM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR13077; PTHR13077; 1.
DR Pfam; PF08806; Sep15_SelM; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
KW Reference proteome; Selenocysteine; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..145
FT /note="Selenoprotein M"
FT /id="PRO_0000022299"
FT REGION 125..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 45
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 48
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT NON_STD 48
FT /note="Selenocysteine"
FT CROSSLNK 45..48
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000255"
FT CONFLICT 107
FT /note="A -> E (in Ref. 2; BAE43327)"
FT /evidence="ECO:0000305"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:2A2P"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2A2P"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:2A2P"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2A2P"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:2A2P"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:2A2P"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2A2P"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2A2P"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:2A2P"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2A2P"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:2A2P"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2A2P"
SQ SEQUENCE 145 AA; 16378 MW; 29849559CF0445DF CRC64;
MSILLSPPSL LLLLAALVAP ATSTTNYRPD WNRLRGLARG RVETCGGUQL NRLKEVKAFV
TEDIQLYHNL VMKHLPGADP ELVLLSRNYQ ELERIPLSQM TRDEINALVQ ELGFYRKSAP
EAQVPPEYLW APAKPPEEAS EHDDL
