ID A0A093K5S7_STRCA Unreviewed; 667 AA.
AC A0A093K5S7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=E3 ubiquitin-protein ligase Midline-1 {ECO:0000256|ARBA:ARBA00013586};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING finger protein Midline-1 {ECO:0000256|ARBA:ARBA00031380};
DE AltName: Full=RING-type E3 ubiquitin transferase Midline-1 {ECO:0000256|ARBA:ARBA00033203};
DE AltName: Full=Tripartite motif-containing protein 18 {ECO:0000256|ARBA:ARBA00032675};
GN ORFNames=N308_12582 {ECO:0000313|EMBL:KFV85794.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV85794.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV85794.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV85794.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002369}.
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; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; KL206793; KFV85794.1; -; Genomic_DNA.
DR RefSeq; XP_009681970.1; XM_009683675.1.
DR RefSeq; XP_009681971.1; XM_009683676.1.
DR RefSeq; XP_009681972.1; XM_009683677.1.
DR RefSeq; XP_009681973.1; XM_009683678.1.
DR AlphaFoldDB; A0A093K5S7; -.
DR STRING; 441894.ENSSCUP00000022313; -.
DR Ensembl; ENSSCUT00000029595; ENSSCUP00000022313; ENSSCUG00000016351.
DR GeneID; 104149814; -.
DR KEGG; scam:104149814; -.
DR CTD; 4281; -.
DR OrthoDB; 5383069at2759; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IEA:Ensembl.
DR GO; GO:0035372; P:protein localization to microtubule; IEA:Ensembl.
DR CDD; cd19836; Bbox1_MID1_C-I; 1.
DR CDD; cd19822; Bbox2_MID1_C-I; 1.
DR CDD; cd00063; FN3; 1.
DR CDD; cd16753; RING-HC_MID1; 1.
DR CDD; cd12892; SPRY_PRY_TRIM18; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR047095; MID1_Bbox1_Zfn.
DR InterPro; IPR027727; MID1_Bbox2_Zfn.
DR InterPro; IPR040859; Midline-1_COS.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR027370; Znf-RING_euk.
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; PTHR24099:SF23; E3 UBIQUITIN-PROTEIN LIGASE MIDLINE-1; 1.
DR PANTHER; PTHR24099; E3 UBIQUITIN-PROTEIN LIGASE TRIM36-RELATED; 1.
DR Pfam; PF18568; COS; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF57850; RING/U-box; 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 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 10..60
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 170..212
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 320..379
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 381..491
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 466..659
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 472..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 209..247
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 472..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 75417 MW; 5A4AD252FCD6302F CRC64;
METLESELTC PICLELFEDP LLLPCAHSLC FNCAHRILVS HCATNESVES ITAFQCPTCR
YVITLSQRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSET RRERAFDSNS MSSCEKVLCQ
FCDQDPAQEA VKTCVTCEVS YCEECLKATH PNKKPFTGHR LIEPIPDSHI RGLMCLEHED
EKVNMYCVTD DQLICALCKL VGRHRDHQVA ALSERYDKLK QNLESNLTNL IKRNTELETL
LAKLIQTCQH VEVNASRQET KLMEECDQLI EIIQQRRQII GTKIKEGKVV RLRKLAQQIA
NCKQCIERST SLISQAEQSL KENDHARFLQ TAKNITERVS MATASSQVLI PEINLNDTFD
TFALDFTREK KLLECLDYLT APNPPTIREE LCTASYDTIT VHWTSDDEFS VVSYELQYTI
FTGQANVVSL CNSADSWMIV PNIKQNHYTV HGLQSGTKYI FVVKAINQAG SRNSEPGKLK
TNSQPFKLDP KSAHRKLKVS HDNLTVERDE TSSKKSHTPE RFTSQGSYGV AGNVFIDSGR
HYWEVVISGS TWYAIGISYK SAPKHEWIGK NSASWVLCRC NNTWVVRHNS KEIPIEPAPH
LRRVGILLDY DNGSLAFYDA LNSLHLYTFD ITFGQPVCPT FTVWNKCLTI ITGLPIPDHL
DSSEQLA
//