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MB12A_MOUSE
ID   MB12A_MOUSE             Reviewed;         271 AA.
AC   Q78HU3;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Multivesicular body subunit 12A;
DE   AltName: Full=ESCRT-I complex subunit MVB12A;
DE   AltName: Full=Protein FAM125A;
GN   Name=Mvb12a; Synonyms=Fam125a;
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=Czech II, and FVB/N; TISSUE=Liver, and 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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND TYR-202, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC   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 the
CC       ligand-mediated internalization and down-regulation of EGF receptor (By
CC       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 CD2AP and CIN85/SH3KBP1. Interacts with CD2AP (via one
CC       of the SH3 domains). Interacts with TSG101; the association appears to
CC       be mediated by the TSG101-VPS37 binary subcomplex. Interacts with
CC       VPS28. Interacts with VPS37B; the association appears to be mediated by
CC       the TSG101-VPS37 binary subcomplex. Interacts with VPS37C; the
CC       association appears to be mediated by the TSG101-VPS37 binary
CC       subcomplex. Interacts with VPS37D; the association appears to be
CC       mediated by the TSG101-VPS37 binary subcomplex. Interacts with CEP55
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Endosome. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome. Late endosome membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with F-
CC       actin. Some fraction may be nuclear (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated on Tyr-202 upon EGF stimulation. Phosphorylation is
CC       required for interaction with CD2AP and CIN85/SH3KBP1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MVB12 family. {ECO:0000305}.
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DR   EMBL; BC020119; AAH20119.1; -; mRNA.
DR   EMBL; BC027419; AAH27419.1; -; mRNA.
DR   EMBL; BC087734; AAH87734.1; -; mRNA.
DR   CCDS; CCDS22398.1; -.
DR   RefSeq; NP_082893.1; NM_028617.2.
DR   AlphaFoldDB; Q78HU3; -.
DR   SMR; Q78HU3; -.
DR   BioGRID; 216204; 1.
DR   STRING; 10090.ENSMUSP00000034272; -.
DR   iPTMnet; Q78HU3; -.
DR   PhosphoSitePlus; Q78HU3; -.
DR   EPD; Q78HU3; -.
DR   jPOST; Q78HU3; -.
DR   MaxQB; Q78HU3; -.
DR   PaxDb; Q78HU3; -.
DR   PeptideAtlas; Q78HU3; -.
DR   PRIDE; Q78HU3; -.
DR   ProteomicsDB; 252738; -.
DR   Antibodypedia; 51512; 35 antibodies from 11 providers.
DR   Ensembl; ENSMUST00000034272; ENSMUSP00000034272; ENSMUSG00000031813.
DR   GeneID; 73711; -.
DR   KEGG; mmu:73711; -.
DR   UCSC; uc009mdt.1; mouse.
DR   CTD; 93343; -.
DR   MGI; MGI:1920961; Mvb12a.
DR   VEuPathDB; HostDB:ENSMUSG00000031813; -.
DR   eggNOG; KOG4000; Eukaryota.
DR   GeneTree; ENSGT00940000160542; -.
DR   HOGENOM; CLU_064823_2_0_1; -.
DR   InParanoid; Q78HU3; -.
DR   OMA; EYNYTFA; -.
DR   OrthoDB; 1021387at2759; -.
DR   PhylomeDB; Q78HU3; -.
DR   TreeFam; TF314477; -.
DR   Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   BioGRID-ORCS; 73711; 2 hits in 71 CRISPR screens.
DR   ChiTaRS; Mvb12a; mouse.
DR   PRO; PR:Q78HU3; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q78HU3; protein.
DR   Bgee; ENSMUSG00000031813; Expressed in right kidney and 243 other tissues.
DR   ExpressionAtlas; Q78HU3; baseline and differential.
DR   Genevisible; Q78HU3; MM.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0000813; C:ESCRT I complex; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031982; C:vesicle; ISO:MGI.
DR   GO; GO:0008289; F:lipid binding; ISO:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR   GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0032801; P:receptor catabolic process; IBA:GO_Central.
DR   GO; GO:0042058; P:regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR   GO; GO:0046755; P:viral budding; ISO:MGI.
DR   GO; GO:0019075; P:virus maturation; ISO:MGI.
DR   InterPro; IPR023341; MABP.
DR   InterPro; IPR040335; MVB12A.
DR   InterPro; IPR018798; MVB12A/B.
DR   InterPro; IPR023340; UMA.
DR   PANTHER; PTHR31612; PTHR31612; 1.
DR   Pfam; PF10240; DUF2464; 1.
DR   PROSITE; PS51498; MABP; 1.
DR   PROSITE; PS51497; UMA; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Endosome; Membrane; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; SH3-binding; Transport.
FT   CHAIN           1..271
FT                   /note="Multivesicular body subunit 12A"
FT                   /id="PRO_0000249070"
FT   DOMAIN          7..149
FT                   /note="MABP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00831"
FT   DOMAIN          213..263
FT                   /note="UMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00830"
FT   REGION          149..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..271
FT                   /note="Interaction with TSG101, VPS37B and VPS28"
FT                   /evidence="ECO:0000250"
FT   MOTIF           153..158
FT                   /note="SH3-binding"
FT   MOD_RES         128
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY5"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY5"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY5"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY5"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         202
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96EY5"
SQ   SEQUENCE   271 AA;  28705 MW;  92749C457B4BB95D CRC64;
     MDPGTDSAPL AGLVWSSASA PPPPGFSAIT CTVEGGTASF GRGFAQKAGY FLCLSTLGIP
     ENPQDNVVVD MQIVMDKGPL PSGFSAVNDP QDIKASVSKK KRMCVKLMPL GTADVVVSDV
     KLSGKTKTVP GYLRVGDIGG FAIWCKKSKA PRPVPKPRTL SQDMRGLSLD PPKEPSKGSH
     PERTLSRLGS RASTLRRTDS IYEASSLYGI SAMDGVPFTL HPRFEGKSCG PLNLSAFGDL
     TIKSLADIEK EYNYGFVVEK TAAARLPPSV S
 
 
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