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 03-APR-2013, entry version 91.
DE RecName: Full=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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 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; 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 Pfam; PF00041; fn3; 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; SSF49899; ConA_like_lec_gl; 1.
DR SUPFAM; SSF49265; FN_III-like; 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 Midline-1.
FT /FTId=PRO_0000056230.
FT DOMAIN 320 379 COS.
FT DOMAIN 380 481 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
//
