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TM204_MOUSE
ID   TM204_MOUSE             Reviewed;         226 AA.
AC   Q7TQI0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Transmembrane protein 204;
DE   AltName: Full=Claudin-like protein 24;
GN   Name=Tmem204; Synonyms=Clp24;
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].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory epithelium;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
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).
CC   -!- FUNCTION: Can influence paracellular permeability. Appears to be
CC       involved in cell-cell interactions through adherens (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Co-
CC       localizes with the beta-catenin adherins. {ECO:0000250}.
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DR   EMBL; BC054438; AAH54438.1; -; mRNA.
DR   CCDS; CCDS28506.1; -.
DR   RefSeq; NP_001001183.1; NM_001001183.1.
DR   RefSeq; XP_006524641.1; XM_006524578.1.
DR   AlphaFoldDB; Q7TQI0; -.
DR   BioGRID; 240475; 2.
DR   STRING; 10090.ENSMUSP00000024984; -.
DR   GlyGen; Q7TQI0; 1 site.
DR   PhosphoSitePlus; Q7TQI0; -.
DR   MaxQB; Q7TQI0; -.
DR   PaxDb; Q7TQI0; -.
DR   PRIDE; Q7TQI0; -.
DR   ProteomicsDB; 259405; -.
DR   Antibodypedia; 2862; 84 antibodies from 22 providers.
DR   Ensembl; ENSMUST00000024984; ENSMUSP00000024984; ENSMUSG00000024168.
DR   GeneID; 407831; -.
DR   KEGG; mmu:407831; -.
DR   UCSC; uc008azp.1; mouse.
DR   CTD; 79652; -.
DR   MGI; MGI:3039635; Tmem204.
DR   VEuPathDB; HostDB:ENSMUSG00000024168; -.
DR   eggNOG; ENOG502QTQQ; Eukaryota.
DR   GeneTree; ENSGT00390000015528; -.
DR   HOGENOM; CLU_107201_0_0_1; -.
DR   InParanoid; Q7TQI0; -.
DR   OMA; EYVESPC; -.
DR   OrthoDB; 1317636at2759; -.
DR   PhylomeDB; Q7TQI0; -.
DR   TreeFam; TF331492; -.
DR   BioGRID-ORCS; 407831; 1 hit in 72 CRISPR screens.
DR   PRO; PR:Q7TQI0; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q7TQI0; protein.
DR   Bgee; ENSMUSG00000024168; Expressed in right lung lobe and 216 other tissues.
DR   ExpressionAtlas; Q7TQI0; baseline and differential.
DR   Genevisible; Q7TQI0; MM.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0001945; P:lymph vessel development; IMP:MGI.
DR   GO; GO:0030947; P:regulation of vascular endothelial growth factor receptor signaling pathway; IGI:MGI.
DR   GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
DR   InterPro; IPR038992; TMEM204.
DR   PANTHER; PTHR14627; PTHR14627; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..226
FT                   /note="Transmembrane protein 204"
FT                   /id="PRO_0000089866"
FT   TOPO_DOM        1..5
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..103
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..170
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        192..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   226 AA;  24785 MW;  F46F79B0F84B0DCA CRC64;
     MTLQKLVATA VLVALVSLIL NNAAAFTPNW VYQTLEDGRK RSVGLWKSCW LVDRGKGVTS
     PGTRTGQVDT HDCEVLGWGS ESAGFQESRG TVKLQFDMMR ACNLVATAAL VVGQITFILG
     LTGLPLMSPE SQCWEEAMAA AFQLASFVLV IGLVTFYRIG PYTNLSWSCY LNIGACLLAT
     LAAAMLIWNI LHRREDCMAP RVIVISRSLT ARFRRGLDND YVESPC
 
 
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