MAS_MOUSE
ID MAS_MOUSE Reviewed; 324 AA.
AC P30554; O35944; Q8BHI8;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Proto-oncogene Mas;
GN Name=Mas1; Synonyms=Mas, Mas-1;
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 [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8001672; DOI=10.1016/0014-5793(94)01292-9;
RA Metzger R., Bader M., Ludwig T., Berberich C., Bunnemann B., Ganten D.;
RT "Expression of the mouse and rat mas proto-oncogene in the brain and
RT peripheral tissues.";
RL FEBS Lett. 357:27-32(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-25.
RC STRAIN=BCBA; TISSUE=Testis;
RX PubMed=9268631; DOI=10.1006/geno.1997.4816;
RA Schweifer N., Valk P.J., Delwel R., Cox R., Francis F., Meier-Ewert S.,
RA Lehrach H., Barlow D.P.;
RT "Characterization of the C3 YAC contig from proximal mouse chromosome 17
RT and analysis of allelic expression of genes flanking the imprinted Igf2r
RT gene.";
RL Genomics 43:285-297(1997).
RN [4]
RP FUNCTION AS RECEPTOR FOR ANGIOTENSIN 1-7.
RX PubMed=12829792; DOI=10.1073/pnas.1432869100;
RA Santos R.A.S., Simoes e Silva A.C., Maric C., Silva D.M.R., Machado R.P.,
RA de Buhr I., Heringer-Walther S., Pinheiro S.V.B., Lopes M.T., Bader M.,
RA Mendes E.P., Lemos V.S., Campagnole-Santos M.J., Schultheiss H.-P.,
RA Speth R., Walther T.;
RT "Angiotensin-(1-7) is an endogenous ligand for the G protein-coupled
RT receptor Mas.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8258-8263(2003).
CC -!- FUNCTION: Acts specifically as a functional antagonist of AGTR1
CC (angiotensin-2 type 1 receptor), although it up-regulates AGTR1
CC receptor levels. Positive regulation of AGTR1 levels occurs through
CC activation of the G-proteins GNA11 and GNAQ, and stimulation of the
CC protein kinase C signaling cascade. The antagonist effect on AGTR1
CC function is probably due to AGTR1 being physically altered by MAS1 (By
CC similarity). Receptor for angiotensin 1-7. {ECO:0000250,
CC ECO:0000269|PubMed:12829792}.
CC -!- SUBUNIT: Interacts with AGTR1. Interacts with FLNA (via filamin repeat
CC 21); increases PKA-mediated phosphorylation of FLNA.
CC {ECO:0000250|UniProtKB:P04201}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X67735; CAA47964.1; -; Genomic_DNA.
DR EMBL; AK030261; BAC26865.1; -; mRNA.
DR EMBL; AK030265; BAC26868.1; -; mRNA.
DR EMBL; U96273; AAB69120.1; -; mRNA.
DR CCDS; CCDS28394.1; -.
DR PIR; S51001; S51001.
DR RefSeq; NP_032578.2; NM_008552.5.
DR RefSeq; XP_006523356.1; XM_006523293.3.
DR RefSeq; XP_006523357.1; XM_006523294.3.
DR RefSeq; XP_006523359.1; XM_006523296.3.
DR RefSeq; XP_006523360.1; XM_006523297.3.
DR RefSeq; XP_006523362.1; XM_006523299.3.
DR RefSeq; XP_011244492.1; XM_011246190.2.
DR RefSeq; XP_011244493.1; XM_011246191.2.
DR RefSeq; XP_011244494.1; XM_011246192.2.
DR RefSeq; XP_011244495.1; XM_011246193.2.
DR RefSeq; XP_017172759.1; XM_017317270.1.
DR RefSeq; XP_017172760.1; XM_017317271.1.
DR RefSeq; XP_017172761.1; XM_017317272.1.
DR RefSeq; XP_017172762.1; XM_017317273.1.
DR RefSeq; XP_017172763.1; XM_017317274.1.
DR AlphaFoldDB; P30554; -.
DR SMR; P30554; -.
DR STRING; 10090.ENSMUSP00000086409; -.
DR GuidetoPHARMACOLOGY; 150; -.
DR GlyGen; P30554; 3 sites.
DR iPTMnet; P30554; -.
DR PhosphoSitePlus; P30554; -.
DR PaxDb; P30554; -.
DR PRIDE; P30554; -.
DR ProteomicsDB; 295834; -.
DR Antibodypedia; 2936; 366 antibodies from 30 providers.
DR DNASU; 17171; -.
DR Ensembl; ENSMUST00000089015; ENSMUSP00000086409; ENSMUSG00000068037.
DR Ensembl; ENSMUST00000161747; ENSMUSP00000123902; ENSMUSG00000068037.
DR Ensembl; ENSMUST00000162333; ENSMUSP00000125108; ENSMUSG00000068037.
DR Ensembl; ENSMUST00000165020; ENSMUSP00000132300; ENSMUSG00000068037.
DR Ensembl; ENSMUST00000167152; ENSMUSP00000131341; ENSMUSG00000068037.
DR Ensembl; ENSMUST00000233607; ENSMUSP00000156871; ENSMUSG00000068037.
DR GeneID; 17171; -.
DR KEGG; mmu:17171; -.
DR UCSC; uc008ald.2; mouse.
DR CTD; 4142; -.
DR MGI; MGI:96918; Mas1.
DR VEuPathDB; HostDB:ENSMUSG00000068037; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234639; -.
DR HOGENOM; CLU_009579_4_1_1; -.
DR InParanoid; P30554; -.
DR OMA; DGNHCQA; -.
DR OrthoDB; 1136752at2759; -.
DR PhylomeDB; P30554; -.
DR TreeFam; TF336336; -.
DR BioGRID-ORCS; 17171; 2 hits in 71 CRISPR screens.
DR PRO; PR:P30554; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P30554; protein.
DR Bgee; ENSMUSG00000068037; Expressed in dentate gyrus of hippocampal formation granule cell and 78 other tissues.
DR ExpressionAtlas; P30554; baseline and differential.
DR Genevisible; P30554; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001595; F:angiotensin receptor activity; IMP:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; IMP:UniProtKB.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISO:MGI.
DR GO; GO:0070528; P:protein kinase C signaling; ISO:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0034698; P:response to gonadotropin; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; ISO:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR026234; MRGPCRFAMILY.
DR InterPro; IPR000820; Proto-oncogene_Mas.
DR PANTHER; PTHR11334; PTHR11334; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00533; MASONCOGENE.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Proto-oncogene; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..324
FT /note="Proto-oncogene Mas"
FT /id="PRO_0000069715"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..103
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..171
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 19
FT /note="S -> I (in Ref. 2; AAB69120)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="I -> M (in Ref. 1; CAA47964)"
FT /evidence="ECO:0000305"
FT CONFLICT 140..141
FT /note="RC -> TS (in Ref. 1; CAA47964)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="W -> C (in Ref. 1; CAA47964)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="T -> S (in Ref. 1; CAA47964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 37055 MW; 1708FCECAF4656A4 CRC64;
MDQSNMTSLA EEKAMNTSSR NASLGSSHPP IPIVHWVIMS ISPLGFVENG ILLWFLCFRM
RRNPFTVYIT HLSIADISLL FCIFILSIDY ALDYELSSGH HYTIVTLSVT FLFGYNTGLY
LLTAISVERC LSVLYPIWYR CHRPKHQSAF VCALLWALSC LVTTMEYVMC IDSGEESHSR
SDCRAVIIFI AILSFLVFTP LMLVSSTILV VKIRKNTWAS HSSKLYIVIM VTIIIFLIFA
MPMRVLYLLY YEYWSAFGNL HNISLLFSTI NSSANPFIYF FVGSSKKKRF RESLKVVLTR
AFKDEMQPRR QEGNGNTVSI ETVV
