MAS_HUMAN
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 03-AUG-2022, entry version 184.
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}.
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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.ENSP00000252660; -.
DR BindingDB; P04201; -.
DR ChEMBL; CHEMBL3559701; -.
DR GuidetoPHARMACOLOGY; 150; -.
DR GlyGen; P04201; 3 sites.
DR iPTMnet; P04201; -.
DR PhosphoSitePlus; P04201; -.
DR BioMuta; MAS1; -.
DR DMDM; 135920; -.
DR PaxDb; P04201; -.
DR PeptideAtlas; P04201; -.
DR PRIDE; P04201; -.
DR ProteomicsDB; 51677; -.
DR Antibodypedia; 2936; 366 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 CTD; 4142; -.
DR DisGeNET; 4142; -.
DR GeneCards; MAS1; -.
DR HGNC; HGNC:6899; MAS1.
DR HPA; ENSG00000130368; Tissue enriched (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; 1136752at2759; -.
DR PhylomeDB; P04201; -.
DR TreeFam; TF336336; -.
DR PathwayCommons; P04201; -.
DR SignaLink; P04201; -.
DR SIGNOR; P04201; -.
DR BioGRID-ORCS; 4142; 11 hits in 1066 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 prefrontal cortex and 23 other tissues.
DR ExpressionAtlas; P04201; baseline and differential.
DR Genevisible; P04201; HS.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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:0007250; P:activation of NF-kappaB-inducing kinase activity; IEA:Ensembl.
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: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 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..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
