ID   IST1_BOVIN              Reviewed;         364 AA.
AC   Q3ZBV1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=IST1 homolog;
DE   AltName: Full=Charged multivesicular body protein 8 {ECO:0000250|UniProtKB:P53990};
DE            Short=CHMP8 {ECO:0000250|UniProtKB:P53990};
GN   Name=IST1;
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=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ESCRT-III-like protein involved in cytokinesis, nuclear
CC       envelope reassembly and endosomal tubulation (By similarity). Is
CC       required for efficient abscission during cytokinesis (By similarity).
CC       Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing
CC       cells (By similarity). During late anaphase, involved in nuclear
CC       envelope reassembly and mitotic spindle disassembly together with the
CC       ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to
CC       the nuclear membrane, leading to microtubule severing (By similarity).
CC       Recruited to the reforming nuclear envelope (NE) during anaphase by
CC       LEMD2 (By similarity). Regulates early endosomal tubulation together
CC       with the ESCRT-III complex by mediating the recruitment of SPAST (By
CC       similarity). {ECO:0000250|UniProtKB:P53990}.
CC   -!- SUBUNIT: Interacts with CHMP1A, CHMP1B, VPS4A and VTA1. Interacts with
CC       SPAST, STAMBP, and USP8. May interact with VPS37B. May associate with
CC       the ESCRT-I complex. Interacts with MITD1, in competition with VSP4.
CC       Interacts with SPART (via MIT domain); leading to the recruitment of
CC       SPART to midbodies. Interacts with SPAST.
CC       {ECO:0000250|UniProtKB:P53990}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:P53990}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:P53990}. Midbody
CC       {ECO:0000250|UniProtKB:P53990}. Nucleus envelope
CC       {ECO:0000250|UniProtKB:P53990}. Note=Localizes to centrosome and
CC       midbody of dividing cells. Colocalized with SPART to the ends of
CC       Flemming bodies during cytokinesis. Localizes to the reforming nuclear
CC       envelope on chromatin disks during late anaphase.
CC       {ECO:0000250|UniProtKB:P53990}.
CC   -!- SIMILARITY: Belongs to the IST1 family. {ECO:0000305}.
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DR   EMBL; BC103094; AAI03095.1; -; mRNA.
DR   RefSeq; NP_001029507.1; NM_001034335.2.
DR   AlphaFoldDB; Q3ZBV1; -.
DR   SMR; Q3ZBV1; -.
DR   STRING; 9913.ENSBTAP00000032246; -.
DR   PaxDb; Q3ZBV1; -.
DR   PRIDE; Q3ZBV1; -.
DR   GeneID; 508900; -.
DR   KEGG; bta:508900; -.
DR   CTD; 9798; -.
DR   eggNOG; KOG2027; Eukaryota.
DR   InParanoid; Q3ZBV1; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   Gene3D; 1.20.1260.60; -; 1.
DR   InterPro; IPR005061; Ist1.
DR   InterPro; IPR042277; IST1-like.
DR   PANTHER; PTHR12161; PTHR12161; 1.
DR   Pfam; PF03398; Ist1; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..364
FT                   /note="IST1 homolog"
FT                   /id="PRO_0000274478"
FT   REGION          292..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P53990"
FT   MOD_RES         43
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P53990"
SQ   SEQUENCE   364 AA;  39791 MW;  E0BA7181F38AD5E1 CRC64;
     MLGSGIKAER LRVNLRLVIN RLKLLEKKKT ELAQKARKEI ADYLAAGKDE RARIRVEHII
     REDYLVEAME ILELYCDLLL ARFGLIQSMK ELDSGLAESV STLIWAAPRL QSEVAELKIV
     ADQLCAKYSK EYGKLCRTNQ IGTVNDRLMH KLSVEAPPKI LVERYLIEIA KNYNVPYEPD
     SVVMAEAPPG VETDLIDVGF TDDVKKGGPG RGGGGGFTAP VGGPDGTVPM PMPMPMPSPN
     TPFSYPLPKG PSDFNGLPVG TYQAFPNIHP PQIPATPPSY ESVDDINADK NVSSTQIVGP
     GPKPEPPAKP ASRLTETYDN FVLPELPSVP DTLPTASPGA NTSASEDIDF DDLSRRFEEL
     KKKT