ID   MTUS1_BOVIN             Reviewed;         467 AA.
AC   Q17QT2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Microtubule-associated tumor suppressor 1 homolog;
DE   AltName: Full=Mitochondrial tumor suppressor 1 homolog;
GN   Name=MTUS1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the MTUS1 family. {ECO:0000305}.
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DR   EMBL; BC118198; AAI18199.1; -; mRNA.
DR   RefSeq; NP_001069160.1; NM_001075692.1.
DR   AlphaFoldDB; Q17QT2; -.
DR   SMR; Q17QT2; -.
DR   STRING; 9913.ENSBTAP00000053632; -.
DR   PaxDb; Q17QT2; -.
DR   PRIDE; Q17QT2; -.
DR   Ensembl; ENSBTAT00000002556; ENSBTAP00000002556; ENSBTAG00000039682.
DR   GeneID; 515016; -.
DR   KEGG; bta:515016; -.
DR   CTD; 57509; -.
DR   VEuPathDB; HostDB:ENSBTAG00000039682; -.
DR   VGNC; VGNC:31756; MTUS1.
DR   eggNOG; ENOG502QPVG; Eukaryota.
DR   GeneTree; ENSGT00950000183026; -.
DR   HOGENOM; CLU_029786_1_0_1; -.
DR   InParanoid; Q17QT2; -.
DR   OMA; HQSYQEE; -.
DR   Proteomes; UP000009136; Chromosome 27.
DR   Bgee; ENSBTAG00000039682; Expressed in longissimus thoracis muscle and 100 other tissues.
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; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0010758; P:regulation of macrophage chemotaxis; IBA:GO_Central.
DR   InterPro; IPR029786; MTUS1.
DR   PANTHER; PTHR24200:SF7; PTHR24200:SF7; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell membrane; Coiled coil; Golgi apparatus; Membrane;
KW   Mitochondrion; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..467
FT                   /note="Microtubule-associated tumor suppressor 1 homolog"
FT                   /id="PRO_0000305196"
FT   REGION          411..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          106..401
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        411..456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         373
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6IMY1"
FT   MOD_RES         394
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD2"
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:0000250|UniProtKB:Q6IMY1"
FT   MOD_RES         431
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5HZI1"
FT   MOD_RES         434
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD2"
FT   MOD_RES         438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9ULD2"
SQ   SEQUENCE   467 AA;  53476 MW;  EDD8F01397F9EAAC CRC64;
     MLLSPKFSLS TIHVRLTAKG LLRNLRLPSG FRKSTVIFHT VEKGRQKSPR SLCIQTQTSP
     DVLSSEKALE LAQYKSKCTK QSGIILQLKQ LLSLGNTKFE ALTVVAQHLL SEREEALKQN
     KTLSQELVNL RGELVTVSTT CEKLEKARNE LQIAYEGFVQ KLNQQHQTDL TELENRLKEF
     YTGECEKLQN IYIEEAEKYK TQLQEQFDNL NATHETSKLK IEASHSEKIE LLKKAYENSL
     SEIKKSHEME KKSLEDLLYE KQESLEKQIS DLKSENDTLN EKLKSEEQKR ISREKANLKN
     PQIMYLEQEL ESLKAVLEIK NEKLHQQDVK LMKMEKLVDS NTALVDRLKR FQQENEELKA
     RMDKHMAISR QLSTEQAVLQ ESLEKESKVN KRLSMENEEL LWKLHNGNLC SPKRSPTSPA
     APFQSPRNSG SFPSPSISHP DDLPGNQRQT EGISAGLTLP ATAHHPP