TRI18_MUSCR
ID TRI18_MUSCR Reviewed; 108 AA.
AC P82456;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=E3 ubiquitin-protein ligase Midline-1;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein Midline-1;
DE AltName: Full=RING-type E3 ubiquitin transferase Midline-1 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 18;
DE Flags: Fragment;
GN Name=Mid1; Synonyms=Fxy, Trim18;
OS Mus caroli (Ryukyu mouse) (Ricefield mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10089;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10508587; DOI=10.1016/s0960-9822(99)80430-8;
RA Perry J., Ashworth A.;
RT "Evolutionary rate of a gene affected by chromosomal position.";
RL Curr. Biol. 9:987-989(1999).
CC -!- FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1, promoting its
CC monoubiquitination, which results in deprotection of the catalytic
CC subunit of protein phosphatase PP2A, and its subsequent degradation by
CC polyubiquitination. {ECO:0000250|UniProtKB:O15344}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- SUBUNIT: Homodimer or heterodimer with MID2. Interacts with IGBP1.
CC {ECO:0000250|UniProtKB:O15344}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15344}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15344}.
CC Note=Microtubule-associated. {ECO:0000250|UniProtKB:O15344}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF186462; AAF01246.1; -; Genomic_DNA.
DR AlphaFoldDB; P82456; -.
DR SMR; P82456; -.
DR MGI; MGI:1100537; Mid1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IBA:GO_Central.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR027727; MID1.
DR InterPro; IPR003877; SPRY_dom.
DR PANTHER; PTHR24099:SF23; PTHR24099:SF23; 1.
DR Pfam; PF00622; SPRY; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Metal-binding; Microtubule; Transferase;
KW Ubl conjugation pathway.
FT CHAIN <1..108
FT /note="E3 ubiquitin-protein ligase Midline-1"
FT /id="PRO_0000056229"
FT DOMAIN <1..100
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT NON_TER 1
SQ SEQUENCE 108 AA; 12195 MW; 8BDD3F2D9A8D61B5 CRC64;
KSAPKHEWIG KNSASWALCR CNNNWVVRHN SKEIPIEPAP HLRRVGILLD YDNGSIAFYD
ALNSIHLYTF DVALAQPVCP TFTVWNKCLT IITGLPIPDH LDCTEQLP
