TMG2_MOUSE
ID TMG2_MOUSE Reviewed; 198 AA.
AC Q8R182; Q9EQI2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Transmembrane gamma-carboxyglutamic acid protein 2;
DE AltName: Full=NEDD4 WW domain-binding protein 1;
DE AltName: Full=Proline-rich gamma-carboxyglutamic acid protein 2;
DE Short=Proline-rich Gla protein 2;
DE Flags: Precursor;
GN Name=Prrg2; Synonyms=N4wbp1;
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 TISSUE=Liver;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 114-198, MUTAGENESIS OF TYR-191, AND
RP INTERACTION WITH NEDD4.
RX PubMed=11042109; DOI=10.1042/bj3510557;
RA Jolliffe C.N., Harvey K.F., Haines B.P., Parasivam G., Kumar S.;
RT "Identification of multiple proteins expressed in murine embryos as binding
RT partners for the WW domains of the ubiquitin-protein ligase Nedd4.";
RL Biochem. J. 351:557-565(2000).
CC -!- SUBUNIT: Interacts with NEDD4 (PubMed:11042109). Interacts with
CC transcriptional coactivator YAP1 (By similarity).
CC {ECO:0000250|UniProtKB:O14669, ECO:0000269|PubMed:11042109}.
CC -!- INTERACTION:
CC Q8R182; P46935: Nedd4; NbExp=5; IntAct=EBI-6304055, EBI-773516;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14669};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent
CC carboxylation. These residues are essential for the binding of calcium.
CC {ECO:0000255|PROSITE-ProRule:PRU00463}.
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DR EMBL; BC025098; AAH25098.1; -; mRNA.
DR EMBL; AF220205; AAG44244.1; -; mRNA.
DR CCDS; CCDS21227.1; -.
DR RefSeq; NP_075375.1; NM_022999.1.
DR RefSeq; XP_006541125.1; XM_006541062.2.
DR RefSeq; XP_006541126.1; XM_006541063.2.
DR RefSeq; XP_011249190.1; XM_011250888.1.
DR AlphaFoldDB; Q8R182; -.
DR SMR; Q8R182; -.
DR BioGRID; 211139; 1.
DR IntAct; Q8R182; 1.
DR STRING; 10090.ENSMUSP00000103464; -.
DR iPTMnet; Q8R182; -.
DR PhosphoSitePlus; Q8R182; -.
DR PaxDb; Q8R182; -.
DR PRIDE; Q8R182; -.
DR ProteomicsDB; 259577; -.
DR Antibodypedia; 2418; 73 antibodies from 25 providers.
DR DNASU; 65116; -.
DR Ensembl; ENSMUST00000007981; ENSMUSP00000007981; ENSMUSG00000007837.
DR Ensembl; ENSMUST00000210690; ENSMUSP00000148014; ENSMUSG00000007837.
DR GeneID; 65116; -.
DR KEGG; mmu:65116; -.
DR UCSC; uc009gsv.1; mouse.
DR CTD; 5639; -.
DR MGI; MGI:1929596; Prrg2.
DR VEuPathDB; HostDB:ENSMUSG00000007837; -.
DR eggNOG; ENOG502RZZF; Eukaryota.
DR GeneTree; ENSGT00950000183084; -.
DR InParanoid; Q8R182; -.
DR OMA; NRSGQHD; -.
DR OrthoDB; 1420559at2759; -.
DR PhylomeDB; Q8R182; -.
DR TreeFam; TF332123; -.
DR BioGRID-ORCS; 65116; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8R182; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R182; protein.
DR Bgee; ENSMUSG00000007837; Expressed in lip and 180 other tissues.
DR ExpressionAtlas; Q8R182; baseline and differential.
DR Genevisible; Q8R182; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR Gene3D; 4.10.740.10; -; 1.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR Pfam; PF00594; Gla; 1.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00069; GLA; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Gamma-carboxyglutamic acid; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..51
FT /evidence="ECO:0000250"
FT /id="PRO_0000022545"
FT CHAIN 52..198
FT /note="Transmembrane gamma-carboxyglutamic acid protein 2"
FT /id="PRO_0000022546"
FT TOPO_DOM 52..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 52..98
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT REGION 156..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 171..174
FT /note="LPXY motif; mediates binding to WW domain-containing
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:O14669"
FT MOTIF 188..191
FT /note="PPXY motif; mediates binding to WW domain-containing
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:O14669"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 69..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MUTAGEN 191
FT /note="Y->A: No effect on interaction with NEDD4."
FT /evidence="ECO:0000269|PubMed:11042109"
SQ SEQUENCE 198 AA; 22369 MW; 1C6482C8445450FC CRC64;
MRGRPSLLLV YMGLATCLDT SPHREQNQVL DIFLDAPEAQ SFLVGRRRFP RANHWDLELL
TPGNLERECL EERCSWEEAR EYFEDNTLTE RFWESYTYNG KGGRGRVDVA GLAVGLTSGI
LLIVLAGLGA FWYLHYRRRR LRGQESCLQE TGLIIPLSPQ TPQSPPLPPG LPTYEQALAA
SGVHDAPPPP YSSLRRPH
