MB12A_RAT
ID MB12A_RAT Reviewed; 271 AA.
AC Q6P777;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
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).
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; BC061799; AAH61799.1; -; mRNA.
DR RefSeq; NP_955407.1; NM_199375.1.
DR AlphaFoldDB; Q6P777; -.
DR SMR; Q6P777; -.
DR IntAct; Q6P777; 1.
DR STRING; 10116.ENSRNOP00000024413; -.
DR iPTMnet; Q6P777; -.
DR PhosphoSitePlus; Q6P777; -.
DR jPOST; Q6P777; -.
DR PaxDb; Q6P777; -.
DR PRIDE; Q6P777; -.
DR GeneID; 290635; -.
DR KEGG; rno:290635; -.
DR UCSC; RGD:735220; rat.
DR CTD; 93343; -.
DR RGD; 735220; Mvb12a.
DR VEuPathDB; HostDB:ENSRNOG00000017949; -.
DR eggNOG; KOG4000; Eukaryota.
DR HOGENOM; CLU_064823_2_0_1; -.
DR InParanoid; Q6P777; -.
DR OMA; EYNYTFA; -.
DR OrthoDB; 1021387at2759; -.
DR PhylomeDB; Q6P777; -.
DR TreeFam; TF314477; -.
DR Reactome; R-RNO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR PRO; PR:Q6P777; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000017949; Expressed in ovary and 20 other tissues.
DR Genevisible; Q6P777; RN.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0000813; C:ESCRT I complex; ISO:RGD.
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:RGD.
DR GO; GO:0008289; F:lipid binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
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:RGD.
DR GO; GO:0046755; P:viral budding; ISO:RGD.
DR GO; GO:0019075; P:virus maturation; ISO:RGD.
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_0000249071"
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 155..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:0007744|PubMed:22673903"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EY5"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EY5"
FT MOD_RES 202
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96EY5"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96EY5"
SQ SEQUENCE 271 AA; 28752 MW; E367D22ED6FEA809 CRC64;
MDPGTDSTPL AALVWSSASA PPPPGFSAIT CTVEGATASF GRGFAQKAGY FLCLSTLGIP
ENPQDNVVVD MQIVMDKGPL PPGFSTVNDP QDARTSVSKK KRMCVKLMPL GTADVVVSDV
KLSGKTKTVP GYLRVGDIGG FAIWCKKSKA PKLVPKPGTL SQDMRGLSLD QPKEPSKGSH
PERTLSRLGS RASTLRRNDS IYEASSLYGI SAMDGVPFTL HPRFEGKSCG PLNLSAFGDL
TIKSLADIEK EYNYGFVVEK TAAARLPPSV S
