MAS_RAT
ID MAS_RAT Reviewed; 324 AA.
AC P12526;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Proto-oncogene Mas;
GN Name=Mas1; Synonyms=Mas, Mas-1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2455902; DOI=10.1073/pnas.85.14.5339;
RA Young D., O'Neill K., Jessell T., Wigler M.;
RT "Characterization of the rat mas oncogene and its high-level expression in
RT the hippocampus and cerebral cortex of rat brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5339-5342(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=18026570; DOI=10.2119/2007-00073.fraga-silva;
RA Fraga-Silva R.A., Pinheiro S.V.B., Goncalves A.C., Alenina N., Bader M.,
RA Santos R.A.S.;
RT "The antithrombotic effect of angiotensin-(1-7) involves mas-mediated NO
RT release from platelets.";
RL Mol. Med. 14:28-35(2008).
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 (By similarity). {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Expressed in platelets.
CC {ECO:0000269|PubMed:18026570}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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; J03823; AAA41573.1; -; Genomic_DNA.
DR EMBL; BC078884; AAH78884.1; -; mRNA.
DR PIR; A31816; TVRTAS.
DR RefSeq; NP_036889.1; NM_012757.2.
DR RefSeq; XP_006227922.1; XM_006227860.3.
DR RefSeq; XP_017444296.1; XM_017588807.1.
DR RefSeq; XP_017444297.1; XM_017588808.1.
DR AlphaFoldDB; P12526; -.
DR SMR; P12526; -.
DR STRING; 10116.ENSRNOP00000020100; -.
DR GuidetoPHARMACOLOGY; 150; -.
DR GlyGen; P12526; 3 sites.
DR PhosphoSitePlus; P12526; -.
DR PaxDb; P12526; -.
DR Ensembl; ENSRNOT00000020100; ENSRNOP00000020100; ENSRNOG00000014971.
DR Ensembl; ENSRNOT00000104217; ENSRNOP00000097396; ENSRNOG00000014971.
DR GeneID; 25153; -.
DR KEGG; rno:25153; -.
DR CTD; 4142; -.
DR RGD; 3049; Mas1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234639; -.
DR HOGENOM; CLU_009579_4_1_1; -.
DR InParanoid; P12526; -.
DR OMA; DGNHCQA; -.
DR OrthoDB; 1136752at2759; -.
DR PhylomeDB; P12526; -.
DR TreeFam; TF336336; -.
DR PRO; PR:P12526; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000014971; Expressed in Ammon's horn and 9 other tissues.
DR ExpressionAtlas; P12526; baseline and differential.
DR Genevisible; P12526; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0001595; F:angiotensin receptor activity; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:RGD.
DR GO; GO:0042277; F:peptide binding; ISO:RGD.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISO:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:RGD.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IDA:RGD.
DR GO; GO:0070528; P:protein kinase C signaling; ISO:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; IMP:RGD.
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 2: Evidence at transcript 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_0000069716"
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"
SQ SEQUENCE 324 AA; 37131 MW; AD810229BF1E7D36 CRC64;
MDQSNMTSFA EEKAMNTSSR NASLGTSHPP IPIVHWVIMS ISPLGFVENG ILLWFLCFRM
RRNPFTVYIT HLSIADISLL FCIFILSIDY ALDYELSSGH YYTIVTLSVT FLFGYNTGLY
LLTAISVERC LSVLYPIWYR CHRPKHQSAF VCALLWALSC LVTTMEYVMC IDSGEESHSQ
SDCRAVIIFI AILSFLVFTP LMLVSSTILV VKIRKNTWAS HSSKLYIVIM VTIIIFLIFA
MPMRVLYLLY YEYWSTFGNL HNISLLFSTI NSSANPFIYF FVGSSKKKRF RESLKVVLTR
AFKDEMQPRR QEGNGNTVSI ETVV
