ID   ZSWM8_BOVIN             Reviewed;        1413 AA.
AC   A7E305;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Zinc finger SWIM domain-containing protein 8 {ECO:0000305};
GN   Name=ZSWIM8 {ECO:0000250|UniProtKB:A7E2V4};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Substrate recognition component of a SCF-like E3 ubiquitin-
CC       protein ligase complex that promotes target-directed microRNA
CC       degradation (TDMD), a process that mediates degradation of microRNAs
CC       (miRNAs). The SCF-like E3 ubiquitin-protein ligase complex acts by
CC       catalyzing ubiquitination and subsequent degradation of AGO proteins
CC       (AGO1, AGO2, AGO3 and/or AGO4), thereby exposing miRNAs for
CC       degradation. Specifically recognizes and binds AGO proteins when they
CC       are engaged with a TDMD target. May also act as a regulator of axon
CC       guidance: specifically recognizes misfolded ROBO3 and promotes its
CC       ubiquitination and subsequent degradation.
CC       {ECO:0000250|UniProtKB:A7E2V4}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:A7E2V4}.
CC   -!- SUBUNIT: Component of the SCF-like E3 ubiquitin-protein ligase complex
CC       which contains CUL3, RBX1, ELOB, ELOC and ZSWIM8.
CC       {ECO:0000250|UniProtKB:A7E2V4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q3UHH1}.
CC   -!- SIMILARITY: Belongs to the ZSWIM8 family. {ECO:0000305}.
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DR   EMBL; BC151646; AAI51647.1; -; mRNA.
DR   RefSeq; NP_001095619.1; NM_001102149.1.
DR   AlphaFoldDB; A7E305; -.
DR   SMR; A7E305; -.
DR   PaxDb; A7E305; -.
DR   PRIDE; A7E305; -.
DR   GeneID; 533041; -.
DR   KEGG; bta:533041; -.
DR   CTD; 23053; -.
DR   eggNOG; KOG3615; Eukaryota.
DR   HOGENOM; CLU_001052_0_0_1; -.
DR   InParanoid; A7E305; -.
DR   OrthoDB; 88229at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:2000627; P:positive regulation of miRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   InterPro; IPR007527; Znf_SWIM.
DR   PROSITE; PS50966; ZF_SWIM; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..1413
FT                   /note="Zinc finger SWIM domain-containing protein 8"
FT                   /id="PRO_0000311801"
FT   ZN_FING         172..208
FT                   /note="SWIM-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00325"
FT   REGION          45..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..745
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..787
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHH1"
FT   MOD_RES         724
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   MOD_RES         738
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHH1"
FT   MOD_RES         741
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UHH1"
FT   MOD_RES         745
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   MOD_RES         852
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
FT   MOD_RES         1412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A7E2V4"
SQ   SEQUENCE   1413 AA;  152380 MW;  262057EA0198782F CRC64;
     MELMFAEWED GERFSFEDSD RFEEDSLCSF ISEAESLCQN WRGWRKQSAG PNSPTGGGGG
     GGSGGTRMRD GLVIPLVELS AKQVAFHIPF EVVEKVYPPV PEQLQLRIAF WSFPENEEDI
     RLYSCLANGS ADEFQRGDQL FRMRAVKDPL QIGFHLSATV VPPQMVPPKG AYNVAVMFDR
     CRVTSCSCTC GAGAKWCTHV VALCLFRIHN ASAVCLRAPV SESLSRLQRD QLQKFAQYLI
     SELPQQILPT AQRLLDELLS SQSTAINTVC GAPDPTAGPS ASDQSTWYLD ESTLTDNIKK
     TLHKFCGPSP VVFSDVNSMY LSSTEPPAAA EWACLLRPLR GREPEGVWNL LSIVREMFKR
     RDSNAAPLLE ILTVELAQDL LANPPDLKVE PPPAKGKKNK VSTSRQTWVA TNTLTKAAFL
     LTVLSERPEH HNLAFRVGMF ALELQRPPAS TKALEVKLAY QESEVATLLK KIPLGPSEMS
     TVRCRAEELR EGTLCDYRPV LPLMLASFIF DVLCAPVVSP TGSRPPSRNW NNEMPGDEEL
     GFEAAVAALG MKTTVSEAEH PLLCEGTRRE KGDLALALMI TYKDDQARLK KILDKLLDRE
     SQTHKPQTLS SFYSSSRPAT ASQRSPSKHG GPSAPGALQP LTSGSAGPAQ PGSVAGAGPG
     PTEGFTEKNV PESSPHSPCE GLPPEAALTP RPEGKVPSRL ALGSRGGYNG RGWGSPGRPK
     KKHTGMASID SSAPETTSDS SPTLSRRPLR GGWAPTSWGR GQDSDSISSS SSDSLGSSSS
     SGSRRASASG GARAKTVEVG RYKGRRPESH APHVPNQPSE AAAHFYFELA KTVLIKAGGN
     SSTSIFTHPS SSGGHQGPHR NLHLCAFEIG LYALGLHNFV SPNWLSRTYS SHVSWITGQA
     MEIGSAALTI LVECWDGHLT PPEVASLADR ASRARDSNMV RAAAELALSC LPHAHALNPN
     EIQRALVQCK EQDNLMLEKA CMAVEEAAKG GGVYPEVLFE VAHQWFWLYE QTAGGSSTAR
     EGATSCSASG IRAAGEAGRG LPEGRGGPGT EPVTVAAAAV TAATVVPVIS VGSSLYPGPG
     LGHGHSPGLH PYTALQPHLP CSPQYLTHPA HPAHPMPHMP RPAVFPVASS AYPQGVHPAF
     LGAQYPYSVT PPSLAATAVS FPVPSMAPIT VHPYHTEPGL PLPTSVALSS VHPASTFPAI
     QGASLPALTT QPSPLVSGGF PPPEEETHSQ PVNPHSLHHL HAAYRVGMLA LEMLGRRAHN
     DHPNNFSRSP PYTDDVKWLL GLAAKLGVNY VHQFCVGAAK GVLSPFVLQE IVMETLQRLS
     PAHAHNHLRA PAFHQLVQRC QQAYMQYIHH RLIHLTPADY DDFVNAIRSA RSAFCLTPMG
     MMQFNDILQN LKRSKQTKEL WQRVSLEMTT FSP