MTUS1_XENLA
ID MTUS1_XENLA Reviewed; 1338 AA.
AC Q7SZL5; Q9PTL6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Microtubule-associated tumor suppressor 1 homolog;
DE AltName: Full=F-box protein 27;
DE AltName: Full=Inner centromere KinI stimulator;
DE AltName: Full=Mitochondrial tumor suppressor 1 homolog;
GN Name=mtus1; Synonyms=fbx27, icis;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBUNIT, INTERACTION WITH KIF2C; AURKB; INCENP AND SKP1,
RP TISSUE SPECIFICITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12919681; DOI=10.1016/s1534-5807(03)00229-6;
RA Ohi R., Coughlin M.L., Lane W.S., Mitchison T.J.;
RT "An inner centromere protein that stimulates the microtubule depolymerizing
RT activity of a KinI kinesin.";
RL Dev. Cell 5:309-321(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 672-1140 (ISOFORM 2), AND POSSIBLE
RP INTERACTION WITH SKP1.
RC TISSUE=Oocyte;
RX PubMed=10531041; DOI=10.1016/s0960-9822(00)80006-8;
RA Regan-Reimann J.D., Duong Q.V., Jackson P.K.;
RT "Identification of novel F-box proteins in Xenopus laevis.";
RL Curr. Biol. 9:R762-R763(1999).
CC -!- FUNCTION: Regulates microtubule dynamics during mitosis by stimulating
CC kif2c. Probably recognizes and binds to some phosphorylated proteins
CC and promotes their ubiquitination and degradation.
CC {ECO:0000269|PubMed:12919681}.
CC -!- SUBUNIT: Homodimer (Probable). Binds microtubules. Interacts with
CC kif2c, aurkb, incenp and SKP1. Probably part of a SCF (SKP1-CUL1-F-box)
CC protein ligase complex. {ECO:0000269|PubMed:12919681, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12919681}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:12919681}. Chromosome
CC {ECO:0000269|PubMed:12919681}. Midbody {ECO:0000269|PubMed:12919681}.
CC Note=Chromosomal until metaphase. Located at the midbody during
CC telophase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7SZL5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7SZL5-2; Sequence=VSP_028286;
CC -!- TISSUE SPECIFICITY: Present in egg (at protein level).
CC {ECO:0000269|PubMed:12919681}.
CC -!- SIMILARITY: Belongs to the MTUS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF14556.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={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; AY352638; AAQ22723.1; -; mRNA.
DR EMBL; AF176665; AAF14556.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001082742.1; NM_001089273.1. [Q7SZL5-1]
DR AlphaFoldDB; Q7SZL5; -.
DR SMR; Q7SZL5; -.
DR IntAct; Q7SZL5; 1.
DR MaxQB; Q7SZL5; -.
DR PRIDE; Q7SZL5; -.
DR GeneID; 398697; -.
DR KEGG; xla:398697; -.
DR CTD; 398697; -.
DR Xenbase; XB-GENE-979441; mtus1.L.
DR OrthoDB; 91479at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 398697; Expressed in heart and 19 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR InterPro; IPR029786; MTUS1.
DR PANTHER; PTHR24200:SF7; PTHR24200:SF7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..1338
FT /note="Microtubule-associated tumor suppressor 1 homolog"
FT /id="PRO_0000305202"
FT DOMAIN 731..774
FT /note="F-box"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 469..494
FT /evidence="ECO:0000255"
FT COILED 966..1298
FT /evidence="ECO:0000255"
FT COMPBIAS 542..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1319..1338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 798..938
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10531041"
FT /id="VSP_028286"
SQ SEQUENCE 1338 AA; 147067 MW; 628843528301A2EF CRC64;
MSVQTATTEN RFQSTLDDNN GNNSESKNIA RCPKYEWNAN VNDQGPGVID HSILDQQSDN
EINKHYLLQS PNALELDSTL DYIGNAAGHC DTFNLKADKG CKTVNSSLLH ENPGEEDETV
DYINNELCNK MQDTLCPPSI PIQTSASDEI HKGLGAITDR GSAYNKIAEQ SLCVQESTDY
LCKMEPKWTV QAFFGDADKL CRNEANNLVD ISTTDHKYDH NSSFGIFTLS LDFSDEKCMR
EDSLVLSGSE KPLSASILEG SALPNSSIDV FTGSVKKTDN IDGFCQGAEL SLRDLDYLEV
PHQKDSTETP QSKLSLTSEH SVFTSETSEV MLEVDARRVM DKTVESHLPN LRLSSNVGKE
DSAPGASLEE FVSGSVPAVA PEELASNLIK DKNTIKNKES HGEAHSLESP ARPDSSSSEL
KDLLSNLSGQ NCEDTFIISS PNSGIGSKAF TSTPLPESKN MTFSVPVLES ITENNELQQN
LDAIKYDLEG LRHSSDSNIV TKPTNKKPAV GSVVGKAKKN EVISFPKPSF KNVKAKVLTR
PSLQAKDSNP YASKTSPRSP PSLSNASSPA QSPRPLSSAV KTVQKRSVIN QDMKTEAAIA
KSQKQPITKQ LFPTHSAHVP THSKHALGKV PRAAALKHTQ NETERASSSN STRSSGSAAA
ALTCTAGSRV TENKSEKAKT SAKPSAPNVR LMGPNKIEQK GIIQPHFDKA QSLKEAKEGT
VSADMDILAN IVPLPTKLAI PSSRNLHKEL ILGIKNVASQ PAKGRVQTTV QRRGSLGKNI
LTIRVSSPPR EKPQVTVEGG LNSPKGRPIS VKASAANGTG SLPRTRLPCR GTTLQRTASV
SSVCSTQSEL SNLSTRSTTT TSSIKTEDIP TAKCIRPNSA SGALTAKSSI PRGRSQSLKV
TQTVTGTKKS PSIIPTLPRS SGPALSLTKK LEARSLQNVE KNKQKTSPRG PVTQAQTPPV
DPKSIELTKC KAACEQQRGV IENLKNLLSS SNQRFEALTV VVQQLINQRE ETLKKRKALS
QELLNLRGDL VCASSTCERL EKEKNELLKA YEGILQKVKE EHHAELSDLE EKLKQFYTGE
CEKLQSIFIE EAEKYKNELQ EKVDDLNTTH EAYRLQAETS QIETIHTLKE DYEKSLTELK
DAKDKENKIL EDSFKEKQAE VEKKILELKD VNESLKEKLK YEEEQRKLTK EKSVQKNPQV
MYLEQELESL KAVLEIKNEK LHQQDKKLMQ VEKLVETNTT LVERLNKCQQ ENEDLKARMV
NHVALSRQLS TEQEVLQRSL EKESKANKRL SMENEELLWK LHNGDLCSPK KLSPSSPGIP
FHPSRNSGSF SSPTVSPR