MTUS1_RAT
ID MTUS1_RAT Reviewed; 440 AA.
AC Q6IMY1; Q6XUU5; Q80Z99;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Microtubule-associated tumor suppressor 1 homolog;
DE AltName: Full=Angiotensin-II type 2 receptor-interacting protein;
DE AltName: Full=Mitochondrial tumor suppressor 1 homolog;
GN Name=Mtus1; Synonyms=Atip, Mtsg1;
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 [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Wistar;
RA Seibold S., Wanner C., Galle J.;
RT "Cloning and characterization of rat MTSG1.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
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=17068200; DOI=10.1210/me.2006-0005;
RA Li J.-M., Mogi M., Tsukuda K., Tomochika H., Iwanami J., Min L.-J.,
RA Nahmias C., Iwai M., Horiuchi M.;
RT "Angiotensin II-induced neural differentiation via angiotensin II type 2
RT (AT2) receptor-MMS2 cascade involving interaction between AT2 receptor-
RT interacting protein and Src homology 2 domain-containing protein-tyrosine
RT phosphatase 1.";
RL Mol. Endocrinol. 21:499-511(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-394; SER-429;
RP SER-431; SER-434 AND SER-438, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Cooperates with AGTR2 to inhibit ERK2 activation and cell
CC proliferation. May be required for AGTR2 cell surface expression.
CC Together with PTPN6, induces UBE2V2 expression upon angiotensin-II
CC stimulation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with AGTR2. Interacts with PTPN6 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Golgi apparatus
CC {ECO:0000250}. Cell membrane {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=In neurons, translocates into the nucleus after treatment with
CC angiotensin-II. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6IMY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IMY1-2; Sequence=VSP_028284, VSP_028285;
CC -!- TISSUE SPECIFICITY: Present in neurons (at protein level).
CC {ECO:0000269|PubMed:17068200}.
CC -!- SIMILARITY: Belongs to the MTUS1 family. {ECO:0000305}.
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; AY208916; AAO60218.1; -; mRNA.
DR EMBL; AY208915; AAO60217.1; -; mRNA.
DR EMBL; BC072537; AAH72537.1; -; mRNA.
DR RefSeq; NP_835194.2; NM_178093.2. [Q6IMY1-1]
DR AlphaFoldDB; Q6IMY1; -.
DR SMR; Q6IMY1; -.
DR STRING; 10116.ENSRNOP00000030995; -.
DR iPTMnet; Q6IMY1; -.
DR PhosphoSitePlus; Q6IMY1; -.
DR PaxDb; Q6IMY1; -.
DR Ensembl; ENSRNOT00000037685; ENSRNOP00000030995; ENSRNOG00000010748. [Q6IMY1-1]
DR GeneID; 306487; -.
DR KEGG; rno:306487; -.
DR CTD; 57509; -.
DR RGD; 631381; Mtus1.
DR eggNOG; ENOG502QPVG; Eukaryota.
DR GeneTree; ENSGT00950000183026; -.
DR HOGENOM; CLU_029786_1_0_1; -.
DR InParanoid; Q6IMY1; -.
DR PhylomeDB; Q6IMY1; -.
DR PRO; PR:Q6IMY1; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000010748; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; Q6IMY1; baseline and differential.
DR Genevisible; Q6IMY1; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1904385; P:cellular response to angiotensin; IEP:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0010758; P:regulation of macrophage chemotaxis; ISO:RGD.
DR InterPro; IPR029786; MTUS1.
DR PANTHER; PTHR24200:SF7; PTHR24200:SF7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell membrane; Coiled coil;
KW Golgi apparatus; Membrane; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..440
FT /note="Microtubule-associated tumor suppressor 1 homolog"
FT /id="PRO_0000305200"
FT REGION 407..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 106..401
FT /evidence="ECO:0000255"
FT COMPBIAS 411..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULD2"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5HZI1"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5HZI1"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028284"
FT VAR_SEQ 95..112
FT /note="GNTKFEALTVVIQHLLSE -> MGCPSSKMCLSPPQAAAR (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028285"
FT CONFLICT 73
FT /note="D -> Q (in Ref. 1; AAO60217)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="T -> A (in Ref. 1; AAO60218/AAO60217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 50745 MW; A20F08D74ECCE902 CRC64;
MLLSPKFSLS TIHVRLTAKG LLRNLRLPSG LRKNTVIFHT VEKGRQKNPR SLCIQTQTAP
DVLSTERTLE LADYKTKCEN QSGFILHLKQ LLSCGNTKFE ALTVVIQHLL SEREEALKQH
KTLSQELVSL RGELVAASST CEKLEKARND LQTAYEGFVQ KLNQQHQTDQ TELENRLKEF
YTAECEKLQS IYIEEAEKYK TQLQEQFDNL NAAHETTKLE IEASHSEKVE LLKKTYETSL
SEIKKSHEME KKLLENLLNE KQESLEKQIN DLKSENDALN ERLKSEEQKQ LSREKANSKN
PQVMYLEQEL ESLKAVLEIK NEKLHQQDLK LMKMEKLVDN NTTLVDKLTR FQQENEELKA
RMDRHMAISR QLSTEQAALQ ESLEKESKVN KRLSMENEEL LWKLHNGDLC SPKRSPTSSA
IPFQSPRNSG SFSSPSISPR
