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IST1_MOUSE
ID   IST1_MOUSE              Reviewed;         362 AA.
AC   Q9CX00; Q80U68;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 138.
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; Synonyms=Kiaa0174;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-256.
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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; AK010262; BAB26804.1; -; mRNA.
DR   EMBL; AK088192; BAC40200.1; -; mRNA.
DR   EMBL; AK152830; BAE31530.1; -; mRNA.
DR   EMBL; BC017605; AAH17605.1; -; mRNA.
DR   EMBL; AK122215; BAC65497.1; -; mRNA.
DR   CCDS; CCDS22655.1; -.
DR   RefSeq; NP_082294.1; NM_028018.2.
DR   AlphaFoldDB; Q9CX00; -.
DR   SMR; Q9CX00; -.
DR   BioGRID; 215054; 9.
DR   STRING; 10090.ENSMUSP00000034164; -.
DR   iPTMnet; Q9CX00; -.
DR   PhosphoSitePlus; Q9CX00; -.
DR   EPD; Q9CX00; -.
DR   jPOST; Q9CX00; -.
DR   MaxQB; Q9CX00; -.
DR   PaxDb; Q9CX00; -.
DR   PeptideAtlas; Q9CX00; -.
DR   PRIDE; Q9CX00; -.
DR   ProteomicsDB; 301680; -.
DR   Antibodypedia; 44614; 143 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000034164; ENSMUSP00000034164; ENSMUSG00000031729.
DR   GeneID; 71955; -.
DR   KEGG; mmu:71955; -.
DR   UCSC; uc009niy.2; mouse.
DR   CTD; 9798; -.
DR   MGI; MGI:1919205; Ist1.
DR   VEuPathDB; HostDB:ENSMUSG00000031729; -.
DR   eggNOG; KOG2027; Eukaryota.
DR   GeneTree; ENSGT00390000007453; -.
DR   HOGENOM; CLU_037652_0_0_1; -.
DR   InParanoid; Q9CX00; -.
DR   OMA; TEACREE; -.
DR   OrthoDB; 1302348at2759; -.
DR   PhylomeDB; Q9CX00; -.
DR   TreeFam; TF314258; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   BioGRID-ORCS; 71955; 20 hits in 70 CRISPR screens.
DR   ChiTaRS; Ist1; mouse.
DR   PRO; PR:Q9CX00; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9CX00; protein.
DR   Bgee; ENSMUSG00000031729; Expressed in urinary bladder urothelium and 265 other tissues.
DR   Genevisible; Q9CX00; MM.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0000785; C:chromatin; ISO:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:MGI.
DR   GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR   GO; GO:0090543; C:Flemming body; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0030496; C:midbody; ISO:MGI.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0090541; F:MIT domain binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0009838; P:abscission; ISO:MGI.
DR   GO; GO:0051301; P:cell division; ISO:MGI.
DR   GO; GO:0048668; P:collateral sprouting; IGI:MGI.
DR   GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; ISO:MGI.
DR   GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR   GO; GO:0048672; P:positive regulation of collateral sprouting; IGI:MGI.
DR   GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
DR   GO; GO:0008104; P:protein localization; ISO:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0046745; P:viral capsid secondary envelopment; ISO:MGI.
DR   GO; GO:0019076; P:viral release from host cell; ISO:MGI.
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   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..362
FT                   /note="IST1 homolog"
FT                   /id="PRO_0000050728"
FT   REGION          292..350
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"
FT   CONFLICT        252..256
FT                   /note="SDFSG -> VSMCV (in Ref. 3; BAC65497)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   362 AA;  39468 MW;  F3FB378DDBCD8BE7 CRC64;
     MLGSGFKAER LRVNLRLVIN RLKLLEKKKT ELAQKARKEI ADYLAAGKDE RARIRVEHII
     REDYLVEAME ILELYCDLLL ARFGLIQSMK ELDSGLAESV STLIWAAPRL QSEVAELKIV
     ADQLCAKYSK EYGKLCRTNQ IGTVNDRLMH KLSVEAPPKI LVERYLIEIA KNYNVPYEPD
     SVVMAEAPVG VETDLIDVGF TDDVKKGGPG RGGGGGFTAP VGGPDGIVPM PMPMPMPSPN
     APFAYPLPKG PSDFSGLPVG TYQAFPNIHP PQIPATPPSY ESVDDINGDK TVSSAQIVGP
     KPEAPAKPPS RPVDNYNTFV LPELPSVPDT LPTASAGAST SASEDIDFDD LSRRFEELKK
     KT
 
 
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