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TMG4_MOUSE
ID   TMG4_MOUSE              Reviewed;         226 AA.
AC   Q8BGN6; Q8BM25;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Transmembrane gamma-carboxyglutamic acid protein 4;
DE   AltName: Full=Proline-rich gamma-carboxyglutamic acid protein 4;
DE            Short=Proline-rich Gla protein 4;
DE   Flags: Precursor;
GN   Name=Prrg4; Synonyms=Prgp4, Tmg4;
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=Hypothalamus, Urinary bladder, and Vagina;
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).
CC   -!- FUNCTION: May control axon guidance across the CNS (By similarity).
CC       Prevents the delivery of ROBO1 at the cell surface and down-regulates
CC       its expression (By similarity). {ECO:0000250|UniProtKB:Q9BZD6}.
CC   -!- SUBUNIT: Interacts (via cytoplasmic domain) with WW domain-containing
CC       proteins MAGI1, MAGI3, NEDD4, NEDD4L, WWTR1/TAZ and YAP1.
CC       {ECO:0000250|UniProtKB:Q9BZD6}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC       compartment membrane {ECO:0000250|UniProtKB:Q9BZD6}; Single-pass type I
CC       membrane protein {ECO:0000255}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9BZD6}; Single-pass type I membrane protein
CC       {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}.
CC   -!- SIMILARITY: Belongs to the commissureless family. {ECO:0000305}.
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DR   EMBL; AK035530; BAC29092.1; -; mRNA.
DR   EMBL; AK037087; BAC29697.1; -; mRNA.
DR   EMBL; AK038703; BAC30106.1; -; mRNA.
DR   CCDS; CCDS16493.1; -.
DR   RefSeq; NP_848810.3; NM_178695.5.
DR   AlphaFoldDB; Q8BGN6; -.
DR   SMR; Q8BGN6; -.
DR   STRING; 10090.ENSMUSP00000028593; -.
DR   iPTMnet; Q8BGN6; -.
DR   PhosphoSitePlus; Q8BGN6; -.
DR   EPD; Q8BGN6; -.
DR   PaxDb; Q8BGN6; -.
DR   PRIDE; Q8BGN6; -.
DR   ProteomicsDB; 259129; -.
DR   Antibodypedia; 2457; 42 antibodies from 13 providers.
DR   DNASU; 228413; -.
DR   Ensembl; ENSMUST00000028593; ENSMUSP00000028593; ENSMUSG00000027171.
DR   GeneID; 228413; -.
DR   KEGG; mmu:228413; -.
DR   UCSC; uc008lkh.1; mouse.
DR   CTD; 79056; -.
DR   MGI; MGI:2442211; Prrg4.
DR   VEuPathDB; HostDB:ENSMUSG00000027171; -.
DR   eggNOG; ENOG502S0JP; Eukaryota.
DR   GeneTree; ENSGT00940000158268; -.
DR   HOGENOM; CLU_084796_0_0_1; -.
DR   InParanoid; Q8BGN6; -.
DR   OMA; FWKDYST; -.
DR   OrthoDB; 1354567at2759; -.
DR   PhylomeDB; Q8BGN6; -.
DR   TreeFam; TF332123; -.
DR   BioGRID-ORCS; 228413; 4 hits in 72 CRISPR screens.
DR   ChiTaRS; Prrg4; mouse.
DR   PRO; PR:Q8BGN6; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8BGN6; protein.
DR   Bgee; ENSMUSG00000027171; Expressed in ectoplacental cone and 90 other tissues.
DR   ExpressionAtlas; Q8BGN6; baseline and differential.
DR   Genevisible; Q8BGN6; MM.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0050699; F:WW domain binding; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cell membrane; Cleavage on pair of basic residues; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Membrane; Phosphoprotein; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..49
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000022553"
FT   CHAIN           50..226
FT                   /note="Transmembrane gamma-carboxyglutamic acid protein 4"
FT                   /id="PRO_0000022554"
FT   TOPO_DOM        50..113
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          52..98
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOTIF           186..189
FT                   /note="LPXY motif; mediates binding to WW domain-containing
FT                   proteins"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZD6"
FT   MOTIF           204..207
FT                   /note="PPXY motif; mediates binding to WW domain-containing
FT                   proteins"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZD6"
FT   MOD_RES         72
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZD6"
FT   DISULFID        69..74
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   CONFLICT        21
FT                   /note="C -> Y (in Ref. 1; BAC29092)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   226 AA;  25401 MW;  824441E4217CF3A9 CRC64;
     MFPLLIVLSQ LPRLTLAVPH CIRSLKDSEH APEEVFASKE AANIFMHRRL LNNRFDLELF
     TPGDLERECY EEFCSYEEAR EILGDDENTI KFWQTYSIKG PTTGSDVNKE KIDVMSLLTG
     LIVAGVFLVI FGLVGYYVCL TKCKRRPYPS SSANYTRTAR YTPSIVFRSP EEAVLSPSTS
     SEDAGLPSYE QAVALTRKHS VSPPPPYPGP ARGFRVFKKS MSLPSH
 
 
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