ID MAS_HUMAN Reviewed; 325 AA. AC P04201; E1P5B3; Q2TBC9; Q6FG47; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-1987, sequence version 1. DT 27-MAR-2024, entry version 192. DE RecName: Full=Proto-oncogene Mas; GN Name=MAS1; Synonyms=MAS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3708691; DOI=10.1016/0092-8674(86)90785-3; RA Young D., Waitches G., Birchmeier C., Fasano O., Wigler M.; RT "Isolation and characterization of a new cellular oncogene encoding a RT protein with multiple potential transmembrane domains."; RL Cell 45:711-719(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [6] RP PRELIMINARY FUNCTION. RX PubMed=3419518; DOI=10.1038/335437a0; RA Jackson T.R., Blair L.A.C., Marshall J., Goedert M., Hanley M.R.; RT "The mas oncogene encodes an angiotensin receptor."; RL Nature 335:437-440(1988). RN [7] RP FUNCTION AS AGTR1 ANTAGONIST, AND INTERACTION WITH AGTR1. RX PubMed=15809376; DOI=10.1161/01.cir.0000160867.23556.7d; RA Kostenis E., Milligan G., Christopoulos A., Sanchez-Ferrer C.F., RA Heringer-Walther S., Sexton P.M., Gembardt F., Kellett E., Martini L., RA Vanderheyden P., Schultheiss H.P., Walther T.; RT "G-protein-coupled receptor Mas is a physiological antagonist of the RT angiotensin II type 1 receptor."; RL Circulation 111:1806-1813(2005). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-138. RX PubMed=16611642; DOI=10.1074/jbc.m601121200; RA Canals M., Jenkins L., Kellett E., Milligan G.; RT "Up-regulation of the angiotensin II type 1 receptor by the MAS proto- RT oncogene is due to constitutive activation of Gq/G11 by MAS."; RL J. Biol. Chem. 281:16757-16767(2006). RN [9] RP INTERACTION WITH FLNA. RX PubMed=26460884; DOI=10.1021/acs.biochem.5b00975; RA Tirupula K.C., Ithychanda S.S., Mohan M.L., Naga Prasad S.V., Qin J., RA Karnik S.S.; RT "G Protein-Coupled Receptors Directly Bind Filamin A with High Affinity and RT Promote Filamin Phosphorylation."; RL Biochemistry 54:6673-6683(2015). CC -!- FUNCTION: Receptor for angiotensin 1-7 (By similarity). Acts CC specifically as a functional antagonist of AGTR1 (angiotensin-2 type 1 CC receptor), although it up-regulates AGTR1 receptor levels. Positive CC regulation of AGTR1 levels occurs through activation of the G-proteins CC GNA11 and GNAQ, and stimulation of the protein kinase C signaling CC cascade. The antagonist effect on AGTR1 function is probably due to CC AGTR1 being physically altered by MAS1. {ECO:0000250, CC ECO:0000269|PubMed:15809376, ECO:0000269|PubMed:16611642}. CC -!- SUBUNIT: Interacts with AGTR1. Interacts with FLNA (via filamin repeat CC 21); increases PKA-mediated phosphorylation of FLNA (PubMed:26460884). CC {ECO:0000269|PubMed:26460884, ECO:0000305|PubMed:15809376}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16611642}; CC Multi-pass membrane protein {ECO:0000269|PubMed:16611642}. CC -!- DISEASE: Note=The MAS oncogene has a weak focus-inducing activity in CC transfected NIH 3T3 cells. {ECO:0000269|PubMed:3708691}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC -!- CAUTION: Was originally thought to be a receptor for angiotensin II. CC {ECO:0000305|PubMed:3419518}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M13150; AAA36199.1; -; mRNA. DR EMBL; CR542261; CAG47057.1; -; mRNA. DR EMBL; AL035691; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47610.1; -; Genomic_DNA. DR EMBL; CH471051; EAW47611.1; -; Genomic_DNA. DR EMBL; BC069142; AAH69142.1; -; mRNA. DR EMBL; BC069581; AAH69581.1; -; mRNA. DR EMBL; BC110454; AAI10455.1; -; mRNA. DR CCDS; CCDS5272.1; -. DR PIR; A01375; TVHUAS. DR RefSeq; NP_002368.1; NM_002377.2. DR AlphaFoldDB; P04201; -. DR SMR; P04201; -. DR BioGRID; 110312; 83. DR IntAct; P04201; 68. DR STRING; 9606.ENSP00000501180; -. DR BindingDB; P04201; -. DR ChEMBL; CHEMBL3559701; -. DR GuidetoPHARMACOLOGY; 150; -. DR GlyCosmos; P04201; 3 sites, No reported glycans. DR GlyGen; P04201; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; P04201; -. DR PhosphoSitePlus; P04201; -. DR BioMuta; MAS1; -. DR DMDM; 135920; -. DR PaxDb; 9606-ENSP00000252660; -. DR PeptideAtlas; P04201; -. DR ProteomicsDB; 51677; -. DR Antibodypedia; 2936; 423 antibodies from 30 providers. DR DNASU; 4142; -. DR Ensembl; ENST00000252660.5; ENSP00000252660.4; ENSG00000130368.7. DR Ensembl; ENST00000674077.2; ENSP00000501180.2; ENSG00000130368.7. DR GeneID; 4142; -. DR KEGG; hsa:4142; -. DR MANE-Select; ENST00000674077.2; ENSP00000501180.2; NM_002377.4; NP_002368.1. DR AGR; HGNC:6899; -. DR CTD; 4142; -. DR DisGeNET; 4142; -. DR GeneCards; MAS1; -. DR HGNC; HGNC:6899; MAS1. DR HPA; ENSG00000130368; Tissue enhanced (brain). DR MIM; 165180; gene. DR neXtProt; NX_P04201; -. DR OpenTargets; ENSG00000130368; -. DR PharmGKB; PA30643; -. DR VEuPathDB; HostDB:ENSG00000130368; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01030000234639; -. DR HOGENOM; CLU_009579_4_1_1; -. DR InParanoid; P04201; -. DR OMA; DGNHCQA; -. DR OrthoDB; 5320834at2759; -. DR PhylomeDB; P04201; -. DR TreeFam; TF336336; -. DR PathwayCommons; P04201; -. DR SignaLink; P04201; -. DR SIGNOR; P04201; -. DR BioGRID-ORCS; 4142; 11 hits in 1146 CRISPR screens. DR ChiTaRS; MAS1; human. DR GeneWiki; MAS1; -. DR GenomeRNAi; 4142; -. DR Pharos; P04201; Tchem. DR PRO; PR:P04201; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P04201; Protein. DR Bgee; ENSG00000130368; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 25 other cell types or tissues. DR ExpressionAtlas; P04201; baseline and differential. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0001595; F:angiotensin receptor activity; ISS:UniProtKB. DR GO; GO:0004945; F:angiotensin type II receptor activity; TAS:ProtInc. DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB. DR GO; GO:0042277; F:peptide binding; ISS:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. 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; IEA:Ensembl. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl. DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IEA:Ensembl. DR GO; GO:0070528; P:protein kinase C signaling; IMP:UniProtKB. DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl. 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; IEA:Ensembl. DR CDD; cd15110; 7tmA_MrgprH; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR026234; MRGPCRFAMILY. DR InterPro; IPR000820; Proto-oncogene_Mas. DR PANTHER; PTHR11334; MAS-RELATED G-PROTEIN COUPLED RECEPTOR; 1. DR PANTHER; PTHR11334:SF61; PROTO-ONCOGENE MAS; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00533; MASONCOGENE. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; P04201; HS. 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..325 FT /note="Proto-oncogene Mas" FT /id="PRO_0000069714" FT TOPO_DOM 1..36 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 37..61 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 62..65 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 66..86 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 87..104 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 105..128 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 129..149 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 150..172 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 173..185 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 186..206 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 207..224 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 225..245 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 246..263 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 264..284 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 285..325 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 22 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT MUTAGEN 138 FT /note="I->D: Fails to activate GNA11." FT /evidence="ECO:0000269|PubMed:16611642" SQ SEQUENCE 325 AA; 37465 MW; 3368E7B174744B83 CRC64; MDGSNVTSFV VEEPTNISTG RNASVGNAHR QIPIVHWVIM SISPVGFVEN GILLWFLCFR MRRNPFTVYI THLSIADISL LFCIFILSID YALDYELSSG HYYTIVTLSV TFLFGYNTGL YLLTAISVER CLSVLYPIWY RCHRPKYQSA LVCALLWALS CLVTTMEYVM CIDREEESHS RNDCRAVIIF IAILSFLVFT PLMLVSSTIL VVKIRKNTWA SHSSKLYIVI MVTIIIFLIF AMPMRLLYLL YYEYWSTFGN LHHISLLFST INSSANPFIY FFVGSSKKKR FKESLKVVLT RAFKDEMQPR RQKDNCNTVT VETVV //