TMM25_MOUSE
ID TMM25_MOUSE Reviewed; 365 AA.
AC Q9DCF1; Q3TMP3; Q6PAK7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Transmembrane protein 25 {ECO:0000305};
DE Flags: Precursor;
GN Name=Tmem25 {ECO:0000312|MGI:MGI:1918937};
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Medulla oblongata;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP GRIN2B.
RX PubMed=31424425; DOI=10.1172/jci122599;
RA Zhang H., Tian X., Lu X., Xu D., Guo Y., Dong Z., Li Y., Ma Y., Chen C.,
RA Yang Y., Yang M., Yang Y., Liu F., Zhou R., He M., Xiao F., Wang X.;
RT "TMEM25 modulates neuronal excitability and NMDA receptor subunit NR2B
RT degradation.";
RL J. Clin. Invest. 129:3864-3876(2019).
CC -!- FUNCTION: In neurons, modulates the degradation of NMDA receptor GRIN2B
CC subunit. Plays a role in the regulation of neuronal excitability.
CC {ECO:0000269|PubMed:31424425}.
CC -!- SUBUNIT: Interacts with GRIN2B. {ECO:0000269|PubMed:31424425}.
CC -!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:31424425}.
CC Lysosome {ECO:0000269|PubMed:31424425}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DCF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DCF1-2; Sequence=VSP_012942;
CC -!- TISSUE SPECIFICITY: Expressed throughout the brain with higher levels
CC within the hippocampus. {ECO:0000269|PubMed:31424425}.
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DR EMBL; AK002841; BAB22398.1; -; mRNA.
DR EMBL; AK165199; BAE38074.1; -; mRNA.
DR EMBL; AK165827; BAE38398.1; -; mRNA.
DR EMBL; BC060057; AAH60057.1; -; mRNA.
DR EMBL; BC060243; AAH60243.1; -; mRNA.
DR CCDS; CCDS23120.1; -. [Q9DCF1-1]
DR RefSeq; NP_082141.1; NM_027865.2. [Q9DCF1-1]
DR RefSeq; XP_006510672.1; XM_006510609.3.
DR RefSeq; XP_006510673.1; XM_006510610.3. [Q9DCF1-1]
DR AlphaFoldDB; Q9DCF1; -.
DR STRING; 10090.ENSMUSP00000002100; -.
DR GlyConnect; 2795; 2 N-Linked glycans (1 site).
DR GlyGen; Q9DCF1; 4 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q9DCF1; -.
DR PhosphoSitePlus; Q9DCF1; -.
DR PaxDb; Q9DCF1; -.
DR PRIDE; Q9DCF1; -.
DR ProteomicsDB; 259582; -. [Q9DCF1-1]
DR ProteomicsDB; 259583; -. [Q9DCF1-2]
DR Antibodypedia; 2512; 93 antibodies from 19 providers.
DR DNASU; 71687; -.
DR Ensembl; ENSMUST00000002100; ENSMUSP00000002100; ENSMUSG00000002032. [Q9DCF1-1]
DR GeneID; 71687; -.
DR KEGG; mmu:71687; -.
DR UCSC; uc009pem.1; mouse. [Q9DCF1-1]
DR CTD; 84866; -.
DR MGI; MGI:1918937; Tmem25.
DR VEuPathDB; HostDB:ENSMUSG00000002032; -.
DR eggNOG; KOG4555; Eukaryota.
DR GeneTree; ENSGT01040000240433; -.
DR HOGENOM; CLU_048525_0_0_1; -.
DR InParanoid; Q9DCF1; -.
DR OMA; CVCLGRW; -.
DR OrthoDB; 914115at2759; -.
DR PhylomeDB; Q9DCF1; -.
DR TreeFam; TF333068; -.
DR BioGRID-ORCS; 71687; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q9DCF1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DCF1; protein.
DR Bgee; ENSMUSG00000002032; Expressed in metanephric proximal tubule and 157 other tissues.
DR ExpressionAtlas; Q9DCF1; baseline and differential.
DR Genevisible; Q9DCF1; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IMP:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR042864; TMEM25.
DR PANTHER; PTHR47224; PTHR47224; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Endosome;
KW Glycoprotein; Immunoglobulin domain; Lysosome; Membrane;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..365
FT /note="Transmembrane protein 25"
FT /id="PRO_0000014985"
FT TOPO_DOM 27..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..123
FT /note="Ig-like"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 280..365
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012942"
FT CONFLICT 279
FT /note="S -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 39170 MW; 9BE03C7945A24757 CRC64;
MELPLSQATL RHTLLLLPAL LSSGQGELAP QIDGQTWAER ALRENEHHAF TCRVAGGSAT
PRLAWYLDGQ LQEATTSRLL SVGGDAFSGG TSTFTVTAQR SQHELNCSLQ DPGSGRPANA
SVILNVQFKP EIAQVGAKYQ EAQGPGLLVV LFALVRANPP ANVTWIDQDG PVTVNASDFL
VLDAQNYPWL TNHTVQLQLR SLAHNLSVVA TNDVGVTSAS LPAPGLLATR IEVPLLGIVV
AGGLALGTLV GFSTLVACLV CRKEKKTKGP SRRPSLISSD SNNLKLNNVR LPRENMSLPS
NLQLNDLTPD LRGKATERPM AQHSSRPELL EAEPGGLLTS RGFIRLPMLG YIYRVSSVSS
DEIWL
