GenomeNet

Database: UniProt
Entry: P82457
LinkDB: P82457
Original site: P82457 
ID   TRI18_MUSSP             Reviewed;         667 AA.
AC   P82457;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2000, sequence version 1.
DT   16-APR-2014, entry version 97.
DE   RecName: Full=E3 ubiquitin-protein ligase Midline-1;
DE            EC=6.3.2.-;
DE   AltName: Full=RING finger protein Midline-1;
DE   AltName: Full=Tripartite motif-containing protein 18;
GN   Name=Mid1; Synonyms=Fxy, Trim18;
OS   Mus spretus (Western Mediterranean mouse) (Algerian mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10096;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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,
CC       promoting its monoubiquitination, which results in deprotection of
CC       the catalytic subunit of protein phosphatase PP2A, and its
CC       subsequent degradation by polyubiquitination (By similarity).
CC   -!- SUBUNIT: Homodimer or heterodimer with MID2. Interacts with IGBP1
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Microtubule-associated (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC   -!- SIMILARITY: Contains 2 B box-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 COS domain.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR   EMBL; AF186460; AAD56246.1; -; mRNA.
DR   ProteinModelPortal; P82457; -.
DR   SMR; P82457; 87-214, 376-493.
DR   MGI; MGI:1100537; Mid1.
DR   HOVERGEN; HBG056432; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   Gene3D; 4.10.45.10; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR003879; Butyrophylin.
DR   InterPro; IPR008985; ConA-like_lec_gl_sf.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR003961; Fibronectin_type3.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR027727; MID1/MID2.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR018355; SPla/RYanodine_receptor_subgr.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24103:SF148; PTHR24103:SF148; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Ligase; Metal-binding;
KW   Microtubule; Phosphoprotein; Repeat; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    667       E3 ubiquitin-protein ligase Midline-1.
FT                                /FTId=PRO_0000056230.
FT   DOMAIN      320    379       COS.
FT   DOMAIN      381    484       Fibronectin type-III.
FT   DOMAIN      482    659       B30.2/SPRY.
FT   ZN_FING      10     60       RING-type.
FT   ZN_FING     116    165       B box-type 1.
FT   ZN_FING     172    212       B box-type 2.
FT   COILED      205    264       Potential.
FT   METAL       119    119       Zinc 1 (By similarity).
FT   METAL       122    122       Zinc 1 (By similarity).
FT   METAL       134    134       Zinc 2 (By similarity).
FT   METAL       137    137       Zinc 2 (By similarity).
FT   METAL       142    142       Zinc 1 (By similarity).
FT   METAL       145    145       Zinc 1 (By similarity).
FT   METAL       150    150       Zinc 2 (By similarity).
FT   METAL       159    159       Zinc 2 (By similarity).
FT   MOD_RES      92     92       Phosphoserine (By similarity).
SQ   SEQUENCE   667 AA;  75174 MW;  D6EFA1CDEA43CBB9 CRC64;
     METLESELTC PICLELLEDP LLLPCAHSLC FNCAHRILVS HCATNEPVES INAFQCPTCR
     HVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET RRERAFDANT MSSAEKVLCQ
     FCDQDPAQDA VKTCVTCEVS YCDECLKATH PNKKPFTGHR LIEPIPDSHI RGLMCLEHED
     EKVNMYCVTD DQLICALCKL VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL
     LAKLIQTCQH VEVNASRQEA KLTEECDLLI EIIQQRRQII GTKIKEGKVI RLRKLAQQIA
     NCKQCIERSA SLISQAEHSL KENDHARFLQ TAKNITERVS MATASSQVLI PEINLNDTFD
     TFALDFSREK KLLECLDYLT APNPPTIREE LCTASYDTIT VHWTSDDEFS VVSYELQYTI
     FTGQANVVSL CNSADSWMIV PNIKQNHYTV HGLQSGTKYI FMVKAINQAG SRSSEPGKLK
     TNSQPFKLDP KSAHRKLKVS HDNLTVERDE SSSKKSHTPE RFTSQGSYGV AGNVFIDSGR
     HYWEVVISGS TWYAIGLAYK SAPKHEWIGK NSASWALCRC NNNWVVRHNS KEIPIEPAPH
     LRRVGILLDY DNGSIAFYDA LNSIHLYTFD VALAQPVCPT FTVWNKCLTI ITGLPIPDHL
     DCTEQLP
//
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