VP37B_MOUSE
ID VP37B_MOUSE Reviewed; 285 AA.
AC Q8R0J7; Q3TLR2; Q3UDW1;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Vacuolar protein sorting-associated protein 37B;
DE Short=Vps37B;
DE AltName: Full=ESCRT-I complex subunit VPS37B;
GN Name=Vps37b;
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; TISSUE=Bone marrow, and Mammary gland;
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 STRAIN=FVB/N; TISSUE=Liver;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and 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: Component of the ESCRT-I complex, a regulator of vesicular
CC trafficking process. Required for the sorting of endocytic
CC ubiquitinated cargos into multivesicular bodies. May be involved in
CC cell growth and differentiation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of TSG101, VPS28, a VPS37
CC protein (VPS37A to -D) and MVB12A or MVB12B in a 1:1:1:1 stoichiometry.
CC Interacts with TSG101, VPS28, MVB12A and MVB12B. Component of the
CC ESCRT-I complex (endosomal sorting complex required for transport I)
CC which consists of TSG101, VPS28, a VPS37 protein (VPS37A to -D) and
CC UBAP1 in a 1:1:1:1 stoichiometry. Interacts with CEP55. Interacts with
CC IST1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Recruited to the endosomal
CC membrane in a VPS4A-dependent fashion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS37 family. {ECO:0000305}.
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DR EMBL; AK149893; BAE29150.1; -; mRNA.
DR EMBL; AK166359; BAE38730.1; -; mRNA.
DR EMBL; BC026744; AAH26744.1; -; mRNA.
DR CCDS; CCDS19670.1; -.
DR RefSeq; NP_808544.1; NM_177876.4.
DR AlphaFoldDB; Q8R0J7; -.
DR SMR; Q8R0J7; -.
DR BioGRID; 236921; 5.
DR STRING; 10090.ENSMUSP00000047980; -.
DR iPTMnet; Q8R0J7; -.
DR PhosphoSitePlus; Q8R0J7; -.
DR EPD; Q8R0J7; -.
DR MaxQB; Q8R0J7; -.
DR PaxDb; Q8R0J7; -.
DR PeptideAtlas; Q8R0J7; -.
DR PRIDE; Q8R0J7; -.
DR ProteomicsDB; 300177; -.
DR Antibodypedia; 52311; 75 antibodies from 17 providers.
DR Ensembl; ENSMUST00000040967; ENSMUSP00000047980; ENSMUSG00000066278.
DR GeneID; 330192; -.
DR KEGG; mmu:330192; -.
DR UCSC; uc008zot.1; mouse.
DR CTD; 79720; -.
DR MGI; MGI:1916724; Vps37b.
DR VEuPathDB; HostDB:ENSMUSG00000066278; -.
DR eggNOG; KOG3270; Eukaryota.
DR GeneTree; ENSGT00950000183012; -.
DR HOGENOM; CLU_067118_1_0_1; -.
DR InParanoid; Q8R0J7; -.
DR OMA; QRAPPRM; -.
DR OrthoDB; 1197293at2759; -.
DR PhylomeDB; Q8R0J7; -.
DR TreeFam; TF321840; -.
DR Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 330192; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Vps37b; mouse.
DR PRO; PR:Q8R0J7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8R0J7; protein.
DR Bgee; ENSMUSG00000066278; Expressed in embryonic brain and 247 other tissues.
DR Genevisible; Q8R0J7; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0000813; C:ESCRT I complex; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:1903774; P:positive regulation of viral budding via host ESCRT complex; ISO:MGI.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0019076; P:viral release from host cell; ISO:MGI.
DR Gene3D; 1.10.287.660; -; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR029012; Helix_hairpin_bin_sf.
DR InterPro; IPR009851; Mod_r.
DR Pfam; PF07200; Mod_r; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR PROSITE; PS51314; VPS37_C; 1.
PE 1: Evidence at protein level;
KW Endosome; Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..285
FT /note="Vacuolar protein sorting-associated protein 37B"
FT /id="PRO_0000287201"
FT DOMAIN 84..173
FT /note="VPS37 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00646"
FT REGION 50..170
FT /note="Interaction with IST1"
FT /evidence="ECO:0000250"
FT REGION 167..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..188
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..278
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 40
FT /note="T -> N (in Ref. 1; BAE38730)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="I -> V (in Ref. 1; BAE29150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 31056 MW; D3B8241F206A9425 CRC64;
MAGAVSEARF AGLSLMQLHE LLEDDAQLGD MVRGMEEAQT VQLNKEMTLA SNRSLAEGNL
LYQPQLDAQK ARLTQKYQEL QVLFEAYQIK KTKLDKQSNN ASLETLLALL QAEGAKIEED
TENMAEKFLD GELPLDSFID VYQSKRKLAH MRRVKVEKLQ ELVLKGQRHP QAGAPPPPRV
PEPSPATALP YPSLEATGLP SVVPRRIPPP PPPVPAGHVA TPFAAAMGSG QVSAYPGLQC
PPLPPRVGLP SQQGFSAQLV SPYPPALPQR PPPRMAPHQP GFILQ
