ID   CHMP7_CHICK             Reviewed;         448 AA.
AC   Q5ZJB7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Charged multivesicular body protein 7;
DE   AltName: Full=Chromatin-modifying protein 7;
GN   Name=CHMP7; ORFNames=RCJMB04_19g23;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: ESCRT-III-like protein required to recruit the ESCRT-III
CC       complex to the nuclear envelope (NE) during late anaphase (By
CC       similarity). Together with SPAST, the ESCRT-III complex promotes NE
CC       sealing and mitotic spindle disassembly during late anaphase (By
CC       similarity). Recruited to the reforming NE during anaphase by LEMD2 (By
CC       similarity). Plays a role in the endosomal sorting pathway (By
CC       similarity). {ECO:0000250|UniProtKB:Q8WUX9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus
CC       envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization,
CC       with some punctate distribution, especially in the perinuclear area.
CC       Localizes to the reforming nuclear envelope on chromatin disks during
CC       late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; AJ720517; CAG32176.1; -; mRNA.
DR   RefSeq; NP_001006306.1; NM_001006306.2.
DR   AlphaFoldDB; Q5ZJB7; -.
DR   SMR; Q5ZJB7; -.
DR   STRING; 9031.ENSGALP00000000556; -.
DR   PaxDb; Q5ZJB7; -.
DR   Ensembl; ENSGALT00000000557; ENSGALP00000000556; ENSGALG00000000409.
DR   GeneID; 419535; -.
DR   KEGG; gga:419535; -.
DR   CTD; 91782; -.
DR   VEuPathDB; HostDB:geneid_419535; -.
DR   eggNOG; KOG2911; Eukaryota.
DR   GeneTree; ENSGT00720000108860; -.
DR   HOGENOM; CLU_044768_0_0_1; -.
DR   InParanoid; Q5ZJB7; -.
DR   OMA; NFMFSDF; -.
DR   OrthoDB; 832779at2759; -.
DR   PhylomeDB; Q5ZJB7; -.
DR   Reactome; R-GGA-1632852; Macroautophagy.
DR   Reactome; R-GGA-5620971; Pyroptosis.
DR   Reactome; R-GGA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-GGA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   PRO; PR:Q5ZJB7; -.
DR   Proteomes; UP000000539; Chromosome 22.
DR   Bgee; ENSGALG00000000409; Expressed in skeletal muscle tissue and 13 other tissues.
DR   GO; GO:0000815; C:ESCRT III complex; ISS:UniProtKB.
DR   GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR   GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR   GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR   GO; GO:0045324; P:late endosome to vacuole transport; ISS:UniProtKB.
DR   GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0031468; P:nuclear membrane reassembly; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR   InterPro; IPR005024; Snf7_fam.
DR   PANTHER; PTHR22761; PTHR22761; 1.
DR   Pfam; PF03357; Snf7; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Nucleus; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..448
FT                   /note="Charged multivesicular body protein 7"
FT                   /id="PRO_0000211519"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          241..392
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  49780 MW;  2783CAE40268E6D8 CRC64;
     MCSPGRAPPG PAPAGDLPPE WETDDERMAF LFSAFKQSRE VNSTEWDSKM AFWVGLVLAR
     GRRRGVVRTC LRELQNGFER RGSVPLGLGT VLRELLRRGK MQRESDFMAS VDSSWISWGV
     GVFILKPLKW TLSSVLGDSK VPEEEEVLIY VELLQEKAEE VYRLYQNSVL SSHPVVALSE
     LRSLCAGVCP DERTFYLLLL QLQKEKKVTI LEQNGEKIVK FARGLHAKVS PMNDVDIGVY
     QLMQSEQLLS QKVESLSQEA EKCKDDARSA CRAGKKQLAL RCLKSKRRTE RRIEELHSKL
     DAVQGILDRI YASQTDQMVF NAYQAGVGAL KLSMKDVTVE KAENLVDQIQ ELCDTQDEVA
     QTLAGAGVNG LEMDSEELEK ELDSLLQDSA KEPVHLHPVP QKDSGFAGAI SDAELEAELE
     KLSVCDGDLA QKTPSASSEP QTALGLNL