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Database: UniProt
Entry: A0A093K5S7_STRCA
LinkDB: A0A093K5S7_STRCA
Original site: A0A093K5S7_STRCA 
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
//
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