TM182_MOUSE
ID TM182_MOUSE Reviewed; 229 AA.
AC B2RVY9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Transmembrane protein 182;
DE Flags: Precursor;
GN Name=Tmem182;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18803820; DOI=10.1186/1756-0500-1-85;
RA Wu Y., Smas C.M.;
RT "Expression and regulation of transcript for the novel transmembrane
RT protein Tmem182 in the adipocyte and muscle lineage.";
RL BMC Res. Notes 1:85-85(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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 FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=34427057; DOI=10.1002/jcsm.12767;
RA Luo W., Lin Z., Chen J., Chen G., Zhang S., Liu M., Li H., He D., Liang S.,
RA Luo Q., Zhang D., Nie Q., Zhang X.;
RT "TMEM182 interacts with integrin beta 1 and regulates myoblast
RT differentiation and muscle regeneration.";
RL J. Cachexia Sarcopenia Muscle 12:1704-1723(2021).
CC -!- FUNCTION: Negatively regulates myogenesis and skeletal muscle
CC regeneration via its association with ITGB1 (PubMed:34427057).
CC Modulates ITGB1 activation by decreasing ITGB1-LAMB1 interaction and
CC inhibiting ITGB1-mediated intracellular signaling during myogenesis
CC (PubMed:34427057). {ECO:0000269|PubMed:34427057}.
CC -!- SUBUNIT: Interacts with ITGB1. {ECO:0000250|UniProtKB:A0A1D5NY17}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A0A1D5NY17};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in white adipose tissues (WAT),
CC with 10-fold to 20-fold higher levels than in brown adipose tissue
CC (BAT). Also expressed in skeletal muscle, heart and lung. Lower
CC relative levels of expression in kidney, spleen, testis, brain and
CC liver. {ECO:0000269|PubMed:18803820, ECO:0000269|PubMed:34427057}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in adipogenesis and also markedly up-
CC regulated during in vitro myogenesis of C2C12 myoblasts to myocytes.
CC {ECO:0000269|PubMed:18803820}.
CC -!- INDUCTION: Up-regulated during myoblast differentiation.
CC {ECO:0000269|PubMed:34427057}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit significant increases in body
CC weight, muscle mass, muscle fiber number, muscle fiber diameter and
CC myotube formation and an acceleration of skeletal muscle regeneration.
CC {ECO:0000269|PubMed:34427057}.
CC -!- SIMILARITY: Belongs to the TMEM182 family. {ECO:0000305}.
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DR EMBL; CH466536; EDL14585.1; -; Genomic_DNA.
DR EMBL; BC147440; AAI47441.1; -; mRNA.
DR EMBL; BC147458; AAI47459.1; -; mRNA.
DR EMBL; BC147740; AAI47741.1; -; mRNA.
DR EMBL; BC147743; AAI47744.1; -; mRNA.
DR CCDS; CCDS35550.1; -.
DR RefSeq; NP_001074667.1; NM_001081198.1.
DR AlphaFoldDB; B2RVY9; -.
DR STRING; 10090.ENSMUSP00000110413; -.
DR GlyGen; B2RVY9; 4 sites.
DR PhosphoSitePlus; B2RVY9; -.
DR MaxQB; B2RVY9; -.
DR PaxDb; B2RVY9; -.
DR PRIDE; B2RVY9; -.
DR ProteomicsDB; 259466; -.
DR Antibodypedia; 66643; 20 antibodies from 14 providers.
DR Ensembl; ENSMUST00000114765; ENSMUSP00000110413; ENSMUSG00000079588.
DR GeneID; 381339; -.
DR KEGG; mmu:381339; -.
DR UCSC; uc007auq.1; mouse.
DR CTD; 130827; -.
DR MGI; MGI:1923725; Tmem182.
DR VEuPathDB; HostDB:ENSMUSG00000079588; -.
DR eggNOG; ENOG502QVS4; Eukaryota.
DR GeneTree; ENSGT00390000017581; -.
DR HOGENOM; CLU_105472_0_0_1; -.
DR InParanoid; B2RVY9; -.
DR OMA; WLLVTEV; -.
DR OrthoDB; 1246131at2759; -.
DR PhylomeDB; B2RVY9; -.
DR TreeFam; TF331344; -.
DR BioGRID-ORCS; 381339; 2 hits in 73 CRISPR screens.
DR PRO; PR:B2RVY9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; B2RVY9; protein.
DR Bgee; ENSMUSG00000079588; Expressed in interventricular septum and 87 other tissues.
DR Genevisible; B2RVY9; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0014906; P:myotube cell development involved in skeletal muscle regeneration; IMP:UniProtKB.
DR GO; GO:0014908; P:myotube differentiation involved in skeletal muscle regeneration; IMP:UniProtKB.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IMP:UniProtKB.
DR GO; GO:1901740; P:negative regulation of myoblast fusion; IMP:UniProtKB.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR InterPro; IPR026763; TMEM182.
DR PANTHER; PTHR32012; PTHR32012; 1.
DR Pfam; PF13903; Claudin_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Myogenesis; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..229
FT /note="Transmembrane protein 182"
FT /id="PRO_0000369257"
FT TOPO_DOM 27..114
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 49..59
FT /note="Interaction with ITGB1"
FT /evidence="ECO:0000250|UniProtKB:A0A1D5NY17"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 229 AA; 25845 MW; 35617F40902545A4 CRC64;
MRLNVAVFFG ALFGALGVLL FLVAFGSDYW LLATEVGRCS GEQNIENITF HHEGFFWRCW
FSGVVEENNS NIWKFWYTNQ PPSKNCTHAY LSPYPFMRGE HNSTSYDSAI IYRGFWAVLL
LLGVVAALTA SFLIICAAPF SSHFLYKAGG GSYIASGVLF SLVVILYVIW VQAVADMESY
RALRMRDCWE FTPSILYGWS FFLAPAGVFF SLLAGLLFLV VGRHIQIHH
