SINA_DROER
ID SINA_DROER Reviewed; 314 AA.
AC P61093; B3NDG7;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=GG13584;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.0;
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 14021-0224.01;
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; AY190936; AAO00989.1; -; Genomic_DNA.
DR EMBL; CH954178; EDV52029.1; -; Genomic_DNA.
DR RefSeq; XP_001973003.1; XM_001972967.2.
DR AlphaFoldDB; P61093; -.
DR SMR; P61093; -.
DR STRING; 7220.FBpp0132130; -.
DR EnsemblMetazoa; FBtr0133638; FBpp0132130; FBgn0064599.
DR GeneID; 6544148; -.
DR KEGG; der:6544148; -.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_028215_0_0_1; -.
DR OMA; ADHEDAC; -.
DR OrthoDB; 780610at2759; -.
DR PhylomeDB; P61093; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008711; 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; 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 Sensory transduction; Transferase; Ubl conjugation pathway; Vision; Zinc;
KW Zinc-finger.
FT CHAIN 1..314
FT /note="E3 ubiquitin-protein ligase sina"
FT /id="PRO_0000056174"
FT ZN_FING 73..108
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 125..185
FT /note="SIAH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..314
FT /note="SBD"
FT COMPBIAS 22..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179
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"
SQ SEQUENCE 314 AA; 33707 MW; B58D7D5E8DA2F958 CRC64;
MSNKINPKRR EPTAAAAGAG ATGVATNTST STGSSSAGNT SSANTSSSSS SSLSSAGGGD
AGMSADLTSL FECPVCFDYV LPPILQCSSG HLVCVSCRSK LTCCPTCRGP LANIRNLAME
KVASNVKFPC KHSGYGCTAS LVYTEKTEHE ETCECRPYLC PCPGASCKWQ GPLDLVMQHL
MMSHKSITTL QGEDIVFLAT DINLPGAVDW VMMQSCFGHH FMLVLEKQEK YDGHQQFFAI
VQLIGSRKEA ENFVYRLELN GNRRRLTWEA MPRSIHEGVA SAIHNSDCLV FDTSIAQLFA
DNGNLGINVT ISLV
