VP37C_MOUSE
ID VP37C_MOUSE Reviewed; 352 AA.
AC Q8R105; Q3TY76;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Vacuolar protein sorting-associated protein 37C;
DE AltName: Full=ESCRT-I complex subunit VPS37C;
GN Name=Vps37c;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Visual cortex;
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] (ISOFORM 1).
RC TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, 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 HGS and STAM2.
CC Interacts with CEP55 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Probably associates with
CC membranes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R105-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R105-2; Sequence=VSP_029730;
CC -!- PTM: Phosphorylated by TBK1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the VPS37 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK158833; BAE34687.1; -; mRNA.
DR EMBL; AK159309; BAE34977.1; -; mRNA.
DR EMBL; BC025865; AAH25865.1; -; mRNA.
DR CCDS; CCDS29585.1; -. [Q8R105-1]
DR RefSeq; NP_852068.1; NM_181403.2. [Q8R105-1]
DR RefSeq; XP_006526635.1; XM_006526572.3.
DR RefSeq; XP_006526636.1; XM_006526573.3.
DR RefSeq; XP_006526637.1; XM_006526574.3. [Q8R105-1]
DR RefSeq; XP_006526638.1; XM_006526575.1.
DR RefSeq; XP_011245412.1; XM_011247110.2.
DR AlphaFoldDB; Q8R105; -.
DR SMR; Q8R105; -.
DR BioGRID; 223239; 12.
DR IntAct; Q8R105; 1.
DR STRING; 10090.ENSMUSP00000085264; -.
DR iPTMnet; Q8R105; -.
DR PhosphoSitePlus; Q8R105; -.
DR EPD; Q8R105; -.
DR MaxQB; Q8R105; -.
DR PaxDb; Q8R105; -.
DR PeptideAtlas; Q8R105; -.
DR PRIDE; Q8R105; -.
DR ProteomicsDB; 297579; -. [Q8R105-1]
DR ProteomicsDB; 297580; -. [Q8R105-2]
DR Antibodypedia; 28060; 153 antibodies from 28 providers.
DR DNASU; 107305; -.
DR Ensembl; ENSMUST00000087951; ENSMUSP00000085264; ENSMUSG00000048832. [Q8R105-1]
DR Ensembl; ENSMUST00000235927; ENSMUSP00000158500; ENSMUSG00000048832. [Q8R105-1]
DR GeneID; 107305; -.
DR KEGG; mmu:107305; -.
DR UCSC; uc008gqr.1; mouse. [Q8R105-1]
DR CTD; 55048; -.
DR MGI; MGI:2147661; Vps37c.
DR VEuPathDB; HostDB:ENSMUSG00000048832; -.
DR eggNOG; KOG3270; Eukaryota.
DR GeneTree; ENSGT00950000183012; -.
DR HOGENOM; CLU_067118_0_0_1; -.
DR InParanoid; Q8R105; -.
DR OMA; PMYRAGY; -.
DR OrthoDB; 1197293at2759; -.
DR PhylomeDB; Q8R105; -.
DR TreeFam; TF321840; -.
DR Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 107305; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Vps37c; mouse.
DR PRO; PR:Q8R105; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8R105; protein.
DR Bgee; ENSMUSG00000048832; Expressed in paneth cell and 258 other tissues.
DR ExpressionAtlas; Q8R105; baseline and differential.
DR Genevisible; Q8R105; MM.
DR GO; GO:0000813; C:ESCRT I complex; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048306; F:calcium-dependent protein binding; 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 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 Alternative splicing; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..352
FT /note="Vacuolar protein sorting-associated protein 37C"
FT /id="PRO_0000312199"
FT DOMAIN 78..167
FT /note="VPS37 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00646"
FT REGION 162..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..212
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..352
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029730"
SQ SEQUENCE 352 AA; 38453 MW; CA3F793154A6BB95 CRC64;
MEGLKDKTLQ ELEEMQNDPE AIARLALESP EVQDLQLERE MALATNRSLA EQNLEFQGPL
EISRSNLSDK YQELRKLVER CQEQKAKLEK FSSALQPGTL LDLLQIEGMK IEEESEAMAE
KFLEGEVPLE TFLESFSSMR TLLHLRRVRV EKLQDVVRRP RALPELAGDV PPKRPPPPRP
VPQATPPETE EQPPQPSVVT PYPLPYSPSP GLPVGPTAQG ALQPAPFPVV AQPSSYGGPL
GPYPSPHPGP RAMVGYSWSP QRSGPPQPGY PTAPTSTSGP GYPLVGGRTP GPGYPQQSPY
LPSGNKPPYP TQPQLPGFPG QPQPPVPPQP PYPPGTTPSY GFHPPGPAWP RY
