ID   F1M8B7_RAT              Unreviewed;       213 AA.
AC   F1M8B7;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 2.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Charged multivesicular body protein 2B {ECO:0000313|Ensembl:ENSRNOP00000000904.6};
GN   Name=Chmp2b {ECO:0000313|Ensembl:ENSRNOP00000000904.6,
GN   ECO:0000313|RGD:1306781};
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 {ECO:0000313|Ensembl:ENSRNOP00000000904.6, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000000904.6, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000904.6,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000000904.6}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000904.6};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004481}. Late endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004633}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004633}.
CC   -!- SIMILARITY: Belongs to the SNF7 family.
CC       {ECO:0000256|ARBA:ARBA00006190}.
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DR   RefSeq; XP_001063932.2; XM_001063932.6.
DR   RefSeq; XP_343996.5; XM_343995.8.
DR   AlphaFoldDB; F1M8B7; -.
DR   SMR; F1M8B7; -.
DR   IntAct; F1M8B7; 1.
DR   STRING; 10116.ENSRNOP00000000904; -.
DR   PhosphoSitePlus; F1M8B7; -.
DR   PaxDb; 10116-ENSRNOP00000000904; -.
DR   Ensembl; ENSRNOT00000000904.8; ENSRNOP00000000904.6; ENSRNOG00000040257.5.
DR   KEGG; rno:363720; -.
DR   AGR; RGD:1306781; -.
DR   CTD; 25978; -.
DR   RGD; 1306781; Chmp2b.
DR   eggNOG; KOG3231; Eukaryota.
DR   GeneTree; ENSGT00950000182832; -.
DR   HOGENOM; CLU_069208_1_2_1; -.
DR   OrthoDB; 2876801at2759; -.
DR   TreeFam; TF314163; -.
DR   Reactome; R-RNO-1632852; Macroautophagy.
DR   Reactome; R-RNO-5620971; Pyroptosis.
DR   Reactome; R-RNO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-RNO-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000040257; Expressed in jejunum and 20 other cell types or tissues.
DR   GO; GO:1904930; C:amphisome membrane; ISO:RGD.
DR   GO; GO:0000421; C:autophagosome membrane; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0000815; C:ESCRT III complex; ISO:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0000776; C:kinetochore; ISO:RGD.
DR   GO; GO:0005828; C:kinetochore microtubule; ISO:RGD.
DR   GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
DR   GO; GO:0030496; C:midbody; ISO:RGD.
DR   GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR   GO; GO:0032585; C:multivesicular body membrane; ISO:RGD.
DR   GO; GO:0005643; C:nuclear pore; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR   GO; GO:0097352; P:autophagosome maturation; ISO:RGD.
DR   GO; GO:0006914; P:autophagy; ISO:RGD.
DR   GO; GO:0050890; P:cognition; ISO:RGD.
DR   GO; GO:0007032; P:endosome organization; ISO:RGD.
DR   GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:1902774; P:late endosome to lysosome transport; ISO:RGD.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR   GO; GO:0061952; P:midbody abscission; ISO:RGD.
DR   GO; GO:0007080; P:mitotic metaphase chromosome alignment; ISO:RGD.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0071985; P:multivesicular body sorting pathway; ISO:RGD.
DR   GO; GO:0070050; P:neuron cellular homeostasis; ISO:RGD.
DR   GO; GO:0031468; P:nuclear membrane reassembly; ISO:RGD.
DR   GO; GO:0006997; P:nucleus organization; ISO:RGD.
DR   GO; GO:0001778; P:plasma membrane repair; ISO:RGD.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   GO; GO:0010824; P:regulation of centrosome duplication; ISO:RGD.
DR   GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:RGD.
DR   GO; GO:0099159; P:regulation of modification of postsynaptic structure; IDA:SynGO.
DR   GO; GO:0099175; P:regulation of postsynapse organization; IDA:SynGO.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISO:RGD.
DR   GO; GO:0046761; P:viral budding from plasma membrane; ISO:RGD.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; ISO:RGD.
DR   Gene3D; 6.10.140.1230; -; 1.
DR   InterPro; IPR005024; Snf7_fam.
DR   PANTHER; PTHR10476; CHARGED MULTIVESICULAR BODY PROTEIN; 1.
DR   PANTHER; PTHR10476:SF56; CHARGED MULTIVESICULAR BODY PROTEIN 2B; 1.
DR   Pfam; PF03357; Snf7; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
SQ   SEQUENCE   213 AA;  23935 MW;  AC5B40ED59E4489B CRC64;
     MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA KIGNKEACRV
     LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG AMSTTAKTMQ AVNKKMDPQK
     TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DGSDDEEESQ DIVNQVLDEI GIEISGKMAK
     APSAARSLPS ASTSKATISD EEIERQLKAL GVD
//