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 24-JAN-2024, entry version 147.
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 BioGRID; 230732; 1.
DR STRING; 10090.ENSMUSP00000028593; -.
DR iPTMnet; Q8BGN6; -.
DR PhosphoSitePlus; Q8BGN6; -.
DR EPD; Q8BGN6; -.
DR PaxDb; 10090-ENSMUSP00000028593; -.
DR ProteomicsDB; 259129; -.
DR Antibodypedia; 2457; 53 antibodies from 13 providers.
DR DNASU; 228413; -.
DR Ensembl; ENSMUST00000028593.11; ENSMUSP00000028593.5; ENSMUSG00000027171.11.
DR GeneID; 228413; -.
DR KEGG; mmu:228413; -.
DR UCSC; uc008lkh.1; mouse.
DR AGR; MGI:2442211; -.
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; WKDVFTS; -.
DR OrthoDB; 5357248at2759; -.
DR PhylomeDB; Q8BGN6; -.
DR TreeFam; TF332123; -.
DR BioGRID-ORCS; 228413; 4 hits in 77 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 93 other cell types or 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:0005615; C:extracellular space; IBA:GO_Central.
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; Coagulation Factor IX; 1.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR PANTHER; PTHR24278:SF38; TRANSMEMBRANE GAMMA-CARBOXYGLUTAMIC ACID PROTEIN 4; 1.
DR Pfam; PF00594; Gla; 1.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00069; GLA; 1.
DR SUPFAM; SSF57630; GLA-domain; 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
//
