SINA_DROWI
ID SINA_DROWI Reviewed; 331 AA.
AC Q8I147; B4MX87;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=E3 ubiquitin-protein ligase sina;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase sina {ECO:0000305};
DE AltName: Full=Seven in absentia protein;
GN Name=sina; ORFNames=GK20872;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tucson 14030-0814.10;
RX PubMed=12537575; DOI=10.1186/gb-2002-3-12-research0086;
RA Bergman C.M., Pfeiffer B.D., Rincon-Limas D.E., Hoskins R.A., Gnirke A.,
RA Mungall C.J., Wang A.M., Kronmiller B., Pacleb J.M., Park S., Stapleton M.,
RA Wan K.H., George R.A., de Jong P.J., Botas J., Rubin G.M., Celniker S.E.;
RT "Assessing the impact of comparative genomic sequence data on the
RT functional annotation of the Drosophila genome.";
RL Genome Biol. 3:RESEARCH0086.1-RESEARCH0086.20(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that is required for
CC specification of R7 photoreceptor cell fate in the eye by mediating the
CC ubiquitination and subsequent proteasomal degradation of Tramtrack
CC (ttk). E3 Ubiquitin ligases accept ubiquitin from an E2 ubiquitin-
CC conjugating enzyme in the form of a thioester and then directly
CC transfers the ubiquitin to targeted substrates. Acts via the formation
CC of a complex with ebi and phyl that ubiquitinates the transcription
CC repressor ttk, a general inhibitor of photoreceptor differentiation, in
CC a subset of photoreceptor cells in the eye, leading to the
CC differentiation of cells into neurons. Also involved in external
CC sensory organ development. {ECO:0000250|UniProtKB:P21461}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of some E3 complex at least composed of sina, ebi
CC and phyl. Interacts with eff. {ECO:0000250|UniProtKB:P21461}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21461}. Nucleus
CC {ECO:0000250|UniProtKB:P21461}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. {ECO:0000250}.
CC -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
CC interaction with substrate proteins. It is related to the TRAF family.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000305}.
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DR EMBL; AY190961; AAO01124.1; -; Genomic_DNA.
DR EMBL; CH963876; EDW76920.1; -; Genomic_DNA.
DR RefSeq; XP_002065934.1; XM_002065898.2.
DR AlphaFoldDB; Q8I147; -.
DR SMR; Q8I147; -.
DR STRING; 7260.FBpp0250015; -.
DR EnsemblMetazoa; FBtr0251523; FBpp0250015; FBgn0064264.
DR GeneID; 6642991; -.
DR KEGG; dwi:6642991; -.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_028215_0_0_1; -.
DR InParanoid; Q8I147; -.
DR OMA; ADHEDAC; -.
DR OrthoDB; 780610at2759; -.
DR PhylomeDB; Q8I147; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007798; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:EnsemblMetazoa.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:EnsemblMetazoa.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035883; P:enteroendocrine cell differentiation; IEA:EnsemblMetazoa.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0045676; P:regulation of R7 cell differentiation; ISS:UniProtKB.
DR GO; GO:0007423; P:sensory organ development; ISS:UniProtKB.
DR GO; GO:0045500; P:sevenless signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR InterPro; IPR004162; SINA-like_animal.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR45877; PTHR45877; 1.
DR Pfam; PF03145; Sina; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Developmental protein; Metal-binding; Nucleus;
KW Reference proteome; Sensory transduction; Transferase;
KW Ubl conjugation pathway; Vision; Zinc; Zinc-finger.
FT CHAIN 1..331
FT /note="E3 ubiquitin-protein ligase sina"
FT /id="PRO_0000056177"
FT ZN_FING 90..125
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 142..202
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 32..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..331
FT /note="SBD"
FT COMPBIAS 34..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 331 AA; 34964 MW; 64893444AB702BC5 CRC64;
MSNKINPKRR EPTAAAAAAV AAGVGGGVGG GASGVATANT NTTGSSSTGG SSSAGTTSSA
NTSSSSSSSL SSAGGGDAGM SADLTSLFEC PVCFDYVLPP ILQCSSGHLV CVSCRSKLTC
CPTCRGPLAN IRNLAMEKVA SNVKFPCKHS GYGCTASLVY TEKTEHEETC ECRPYLCPCP
GASCKWQGPL DLVMQHLMMS HKSITTLQGE DIVFLATDIN LPGAVDWVMM QSCFGHHFML
VLEKQEKYDG HQQFFAIVQL IGSRKEAENF VYRLELNGNR RRLTWEAMPR SIHEGVASAI
HNSDCLVFDT SIAQLFADNG NLGINVTISL V
