SINA_DROVI
ID SINA_DROVI Reviewed; 314 AA.
AC P29304;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 117.
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;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1946441; DOI=10.1073/pnas.88.22.10203;
RA Neufeld T.P., Carthew R.W., Rubin G.M.;
RT "Evolution of gene position: chromosomal arrangement and sequence
RT comparison of the Drosophila melanogaster and Drosophila virilis sina and
RT Rh4 genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10203-10207(1991).
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; M77282; AAA28899.1; -; Genomic_DNA.
DR PIR; A41544; A41544.
DR AlphaFoldDB; P29304; -.
DR SMR; P29304; -.
DR STRING; 7244.FBpp0226759; -.
DR eggNOG; KOG3002; Eukaryota.
DR UniPathway; UPA00143; -.
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_0000056176"
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 27..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..314
FT /note="SBD"
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; 33804 MW; 66EA1FE8814250EB CRC64;
MSNKINPKRR EPTVAAAVAA ATAVVATNTS SSTGSSAGNT SSANTSSSSS SSLSSAGGGD
AGMSADLTSL FECPVCFDYV LPPILQCSSG HLVCVSCRSK LTCCPTCRGP LANIRNLAME
EVASNVKFPC KHSGYGCTAS LVYTEKTEHE ETCECRPYLC PCPGASCKWQ GPLDLVMQHL
MMSHKSITTL QGEDIVFLAT DINLPGAVDW VMMQSCFGHH FMLVLEKQEK YDGHQQFFAI
VQLIGSRKEA ENFVYRLELN GNRRRLTWEA MPRSIHEGVA SAIHNSDCLV FDTSIAQLFA
DNGNLGINVT ISLV
