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 02-SEP-2026, entry version 202. 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 FUNCTION. RX PubMed=17984366; DOI=10.1161/hypertensionaha.106.084848; RA Sampaio W.O., Henrique de Castro C., Santos R.A., Schiffrin E.L., RA Touyz R.M.; RT "Angiotensin-(1-7) counterregulates angiotensin II signaling in human RT endothelial cells."; RL Hypertension 50:1093-1098(2007). RN [10] 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). RN [11] RP FUNCTION. RX PubMed=25967876; DOI=10.1159/000374047; RA Liang B., Wang X., Zhang N., Yang H., Bai R., Liu M., Bian Y., Xiao C., RA Yang Z.; RT "Angiotensin-(1-7) Attenuates Angiotensin II-Induced ICAM-1, VCAM-1, and RT MCP-1 Expression via the MAS Receptor Through Suppression of P38 and NF- RT kappaB Pathways in HUVECs."; RL Cell. Physiol. Biochem. 35:2472-2482(2015). RN [12] RP FUNCTION. RX PubMed=41167449; DOI=10.1016/j.abb.2025.110666; RA Hu W.F., Wang J.J., Yu J., Liu Y.L., Xu Z.G., Guo Z.Y.; RT "CXCL17 activates three MAS-related G protein-coupled receptors RT independently of its conserved C-terminal fragment."; RL Arch. Biochem. Biophys. 775:110666-110666(2025). CC -!- FUNCTION: G protein-coupled receptor that plays key roles in the renin- CC angiotensin system (RAS) specifically in the protective, counter- CC regulatory arm of the RAS (PubMed:25967876). Receptor mainly stimulated CC by angiotensin 1-7, which is a bioactive metabolite of the angiotensin CC produced by ACE2 (PubMed:17984366). Activation promotes nitric oxide CC via PI3K/Akt-eNOS pathway (PubMed:17984366). Modulates also the MAPK, CC ERK1/2, and NF-kappa-B signaling (PubMed:25967876). Positive regulation CC of AGTR1 levels occurs through activation of the G proteins GNA11 and CC GNAQ, and stimulation of the protein kinase C signaling cascade CC (PubMed:15809376, PubMed:16611642). The antagonist effect on AGTR1 CC function is probably due to AGTR1 being physically altered by MAS1 CC (PubMed:15809376, PubMed:16611642). Acts as functional receptor for CC CXCL17 and induces chemotactic movement (PubMed:41167449). CC {ECO:0000250|UniProtKB:P30554, ECO:0000269|PubMed:15809376, CC ECO:0000269|PubMed:16611642, ECO:0000269|PubMed:17984366, CC ECO:0000269|PubMed:41167449}. 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 -!- INTERACTION: CC P04201; Q02410: APBA1; NbExp=2; IntAct=EBI-21274133, EBI-368690; CC P04201; Q99767: APBA2; NbExp=2; IntAct=EBI-21274133, EBI-81711; CC P04201; O14936: CASK; NbExp=2; IntAct=EBI-21274133, EBI-1215506; CC P04201; Q12959: DLG1; NbExp=4; IntAct=EBI-21274133, EBI-357481; CC P04201; Q15700: DLG2; NbExp=2; IntAct=EBI-21274133, EBI-80426; CC P04201; Q92796: DLG3; NbExp=2; IntAct=EBI-21274133, EBI-80440; CC P04201; P78352: DLG4; NbExp=3; IntAct=EBI-21274133, EBI-80389; CC P04201; Q68DX3: FRMPD2; NbExp=2; IntAct=EBI-21274133, EBI-53993476; CC P04201; A4D2P6: GRID2IP; NbExp=2; IntAct=EBI-21274133, EBI-15893226; CC P04201; Q9Y3R0: GRIP1; NbExp=3; IntAct=EBI-21274133, EBI-5349621; CC P04201; Q9C0E4: GRIP2; NbExp=4; IntAct=EBI-21274133, EBI-949557; CC P04201; Q14005: IL16; NbExp=2; IntAct=EBI-21274133, EBI-2831580; CC P04201; Q8TBB1: LNX1; NbExp=2; IntAct=EBI-21274133, EBI-739832; CC P04201; Q8N448: LNX2; NbExp=2; IntAct=EBI-21274133, EBI-2340947; CC P04201; Q96QZ7: MAGI1; NbExp=2; IntAct=EBI-21274133, EBI-924464; CC P04201; Q86UL8: MAGI2; NbExp=3; IntAct=EBI-21274133, EBI-311035; CC P04201; Q86UT5: NHERF4; NbExp=2; IntAct=EBI-21274133, EBI-8744528; CC P04201; Q8NI35: PATJ; NbExp=8; IntAct=EBI-21274133, EBI-724390; CC P04201; O60894: RAMP1; NbExp=2; IntAct=EBI-21274133, EBI-962893; CC P04201; O60895: RAMP2; NbExp=2; IntAct=EBI-21274133, EBI-9009040; CC P04201; O60896: RAMP3; NbExp=2; IntAct=EBI-21274133, EBI-720447; CC P04201; Q14160: SCRIB; NbExp=2; IntAct=EBI-21274133, EBI-357345; CC P04201; Q07157: TJP1; NbExp=2; IntAct=EBI-21274133, EBI-79553; CC P04201; Q9P202: WHRN; NbExp=3; IntAct=EBI-21274133, EBI-310886; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16611642}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- MISCELLANEOUS: 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_001353633.1; NM_001366704.2. DR RefSeq; NP_002368.1; NM_002377.4. DR RefSeq; XP_047274732.1; XM_047418776.1. DR RefSeq; XP_054211418.1; XM_054355443.1. DR PDB; 9JLC; EM; 2.98 A; R=31-283. DR PDB; 9X3Y; EM; 2.77 A; R=1-325. DR PDB; 9X3Z; EM; 2.54 A; R=1-325. DR AlphaFoldDB; P04201; -. DR EMDB; EMD-61583; -. DR EMDB; EMD-66514; -. DR EMDB; EMD-66515; -. DR SMR; P04201; -. DR BioGRID; 110312; 84. DR CORUM; P04201; -. DR FunCoup; P04201; 793. DR IntAct; P04201; 155. DR NDEx; IQUERY-CP-MAS1; 11 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000501180; -. DR BindingDB; P04201; -. DR ChEMBL; CHEMBL3559701; -. DR DrugBank; DB12631; Aclerastide. DR DrugBank; DB11720; Angiotensin 1-7. 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-ENSP00000501180; -. DR PeptideAtlas; P04201; -. DR ProteomicsDB; 51677; -. DR Antibodypedia; 2936; 359 antibodies from 31 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 ClinPGx; PA30643; -. DR CTD; 4142; -. DR DisGeNET; 4142; -. DR GeneCards; MAS1; -. DR HGNC; HGNC:6899; MAS1. DR HPA; ENSG00000130368; Tissue enriched (brain). DR MIM; 165180; gene. DR OpenTargets; ENSG00000130368; -. 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; 6091802at2759; -. DR PAN-GO; P04201; 3 GO annotations based on evolutionary models. DR PhylomeDB; P04201; -. DR PathwayCommons; P04201; -. DR Reactome; R-HSA-375276; Peptide ligand-binding receptors. DR SignaLink; P04201; -. DR SIGNOR; P04201; -. DR Agora; ENSG00000130368; -. 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: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:0016493; F:C-C chemokine receptor activity; IDA:UniProtKB. DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB. DR GO; GO:0042277; F:peptide binding; ISS:UniProtKB. DR GO; GO:0016477; P:cell migration; IDA:UniProtKB. DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0086097; P:phospholipase C-activating angiotensin-activated signaling pathway; IMP:UniProtKB. DR CDD; cd15110; 7tmA_MrgprH; 1. DR FunFam; 1.20.1070.10:FF:000134; proto-oncogene Mas; 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 PDBsum; 9JLC; -. DR PDBsum; 9X3Y; -. DR PDBsum; 9X3Z; -. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Disulfide bond; G protein-coupled receptor; KW Glycoprotein; Membrane; Proteomics identification; Proto-oncogene; KW 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 DISULFID 171..184 FT /evidence="ECO:0000250|UniProtKB:Q8TDS7" 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 //