IST1_RAT
ID IST1_RAT Reviewed; 366 AA.
AC Q568Z6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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 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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
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; BC092631; AAH92631.1; -; mRNA.
DR RefSeq; NP_001017454.1; NM_001017454.2.
DR AlphaFoldDB; Q568Z6; -.
DR SMR; Q568Z6; -.
DR STRING; 10116.ENSRNOP00000020365; -.
DR iPTMnet; Q568Z6; -.
DR PhosphoSitePlus; Q568Z6; -.
DR jPOST; Q568Z6; -.
DR PaxDb; Q568Z6; -.
DR PRIDE; Q568Z6; -.
DR GeneID; 307833; -.
DR KEGG; rno:307833; -.
DR UCSC; RGD:1307799; rat.
DR CTD; 9798; -.
DR RGD; 1307799; Ist1.
DR VEuPathDB; HostDB:ENSRNOG00000015144; -.
DR eggNOG; KOG2027; Eukaryota.
DR HOGENOM; CLU_037652_0_0_1; -.
DR InParanoid; Q568Z6; -.
DR OMA; TEACREE; -.
DR OrthoDB; 1302348at2759; -.
DR PhylomeDB; Q568Z6; -.
DR TreeFam; TF314258; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:Q568Z6; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000015144; Expressed in thymus and 20 other tissues.
DR Genevisible; Q568Z6; RN.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR GO; GO:0090543; C:Flemming body; ISO:RGD.
DR GO; GO:0030496; C:midbody; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0090541; F:MIT domain binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0009838; P:abscission; ISO:RGD.
DR GO; GO:0051301; P:cell division; ISO:RGD.
DR GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; ISO:RGD.
DR GO; GO:0045184; P:establishment of protein localization; ISO:RGD.
DR GO; GO:0048672; P:positive regulation of collateral sprouting; ISO:RGD.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0046745; P:viral capsid secondary envelopment; ISO:RGD.
DR GO; GO:0019076; P:viral release from host cell; ISO:RGD.
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..366
FT /note="IST1 homolog"
FT /id="PRO_0000327595"
FT REGION 297..354
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 366 AA; 39942 MW; DDFC8E43B0C6DFEF CRC64;
MLGSGFKAER LRVNLRLVIN RLKLLEKKKT ELAQKARKEI ADYLAAGKDE RARIRVEHII
REDYLVEAME ILELYCDLLL ARFGLIQSMK ELDSGLAESV STLIWAAPRL QSEVAELKIV
ADQLCAKYSK EYGKLCRTNQ IGTVNDRLMH KLSVEAPPKI LVERYLIEIA KNYNVPYEPD
SVVMAEAPVG VETDLIDVGF TDDVKKGGPG RGGGGGFTAP VGAPDGTMPM PMPMPMPMPS
PSPNAPFAYP LPKGPSDFSG LPVGTYQAFP NIHPPQIPAT PPSYESVDDI NADKNVSSAQ
IVGPKPEAPA KPPSRPVDNY NTFVLPELPS VPDTLPTASA GASTSASEDI DFDDLSRRFE
ELKKKT
