R113A_BOVIN
ID R113A_BOVIN Reviewed; 343 AA.
AC Q67ER4; Q2HJ85;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=E3 ubiquitin-protein ligase RNF113A;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:O15541};
DE AltName: Full=RING finger protein 113A;
DE AltName: Full=Zinc finger protein 183;
GN Name=RNF113A; Synonyms=ZNF183;
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 [MRNA].
RC TISSUE=Kidney;
RA Huang C.-H., Chen Y.;
RT "Sequence and structure of zinc finger protein 183 homologs.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome. E3 ubiquitin-protein ligase that catalyzes the transfer of
CC ubiquitin onto target proteins. Catalyzes polyubiquitination of
CC SNRNP200/BRR2 with non-canonical 'Lys-63'-linked polyubiquitin chains.
CC Plays a role in DNA repair via its role in the synthesis of 'Lys-63'-
CC linked polyubiquitin chains that recruit ALKBH3 and the ASCC complex to
CC sites of DNA damage by alkylating agents. Ubiquitinates CXCR4, leading
CC to its degradation, and thereby contributes to the termination of CXCR4
CC signaling. {ECO:0000250|UniProtKB:O15541}.
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:0000250|UniProtKB:O15541};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:O15541}.
CC -!- SUBUNIT: Component of pre-catalytic and catalytic spliceosome
CC complexes. Interacts (via N-terminus) with the spliceosome subunit
CC SNRNP200/BRR2. {ECO:0000250|UniProtKB:O15541}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15541}. Nucleus
CC speckle {ECO:0000250|UniProtKB:O15541}. Note=Colocalizes with ASCC2 in
CC nuclear foci after DNA damage by alkylating agents. In the absence of
CC DNA damage, colocalizes with the spliceosome components SNRNP200/BRR2
CC and PRPF8 in nuclear speckles. {ECO:0000250|UniProtKB:O15541}.
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DR EMBL; AY363106; AAR97519.1; -; mRNA.
DR EMBL; BC113255; AAI13256.1; -; mRNA.
DR RefSeq; NP_001007808.1; NM_001007807.1.
DR AlphaFoldDB; Q67ER4; -.
DR SMR; Q67ER4; -.
DR STRING; 9913.ENSBTAP00000007927; -.
DR PaxDb; Q67ER4; -.
DR PRIDE; Q67ER4; -.
DR GeneID; 493640; -.
DR KEGG; bta:493640; -.
DR CTD; 7737; -.
DR eggNOG; KOG1813; Eukaryota.
DR HOGENOM; CLU_050460_1_0_1; -.
DR InParanoid; Q67ER4; -.
DR OrthoDB; 1420266at2759; -.
DR TreeFam; TF313469; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0018276; P:isopeptide cross-linking via N6-glycyl-L-lysine; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0034247; P:snoRNA splicing; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039971; CWC24-like.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12930; PTHR12930; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; DNA damage; DNA repair; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O15541"
FT CHAIN 2..343
FT /note="E3 ubiquitin-protein ligase RNF113A"
FT /id="PRO_0000056303"
FT ZN_FING 196..224
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 262..300
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 2..60
FT /note="Important for interaction with SNRNP200/BRR2"
FT /evidence="ECO:0000250|UniProtKB:O15541"
FT REGION 23..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..61
FT /note="Important for interaction with CXCR4"
FT /evidence="ECO:0000250|UniProtKB:O15541"
FT REGION 323..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O15541"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15541"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15541"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15541"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15541"
FT CONFLICT 147
FT /note="Q -> K (in Ref. 2; AAI13256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 38849 MW; 0204E9734770AB89 CRC64;
MAEQLSPGKT TDQVCTFLFK KPGRKVAAGR RKRPICNQES GDSSSSSDEG NTVVRPEKKR
AVHNPMIQKT RGSGKQKVAY GDLSSEEEEE NKSESLGVVY KSTRSAKPVG PEDMGATAVY
ELDTEKERDA QAIFERSQKI QEELRGQEDD KIYRGINNYQ KFMKPKDTSM GNASSGMVRK
GPIRAPEHLR ATVRWDYQPD ICKDYKETGF CGFGDSCKFL HDRSDYKHGW QIERELDEGR
YGVYEDENYE VGSDEEEIPF KCFICRQTFQ NPVVTKCRHY FCESCALQHF RTTPRCYVCD
QQTNGVFNPA KELIAKLEKH RAAEGGGASG FPEDPDEDPV PIT
