ID OPTN_XENLA Reviewed; 532 AA.
AC Q5M7B7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 27-NOV-2024, entry version 65.
DE RecName: Full=Optineurin;
GN Name=optn;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably part of the TNF-alpha signaling pathway that can
CC shift the equilibrium toward induction of cell death. May act by
CC regulating membrane trafficking and cellular morphogenesis.
CC {ECO:0000250, ECO:0000250|UniProtKB:Q96CV9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CV9}.
CC Golgi apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle,
CC autophagosome {ECO:0000250}.
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DR EMBL; BC088724; AAH88724.1; -; mRNA.
DR RefSeq; NP_001088901.1; NM_001095432.1.
DR AlphaFoldDB; Q5M7B7; -.
DR SMR; Q5M7B7; -.
DR DNASU; 496250; -.
DR GeneID; 496250; -.
DR KEGG; xla:496250; -.
DR AGR; Xenbase:XB-GENE-943661; -.
DR CTD; 496250; -.
DR Xenbase; XB-GENE-943661; optn.L.
DR OrthoDB; 5406882at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 496250; Expressed in zone of skin and 19 other cell types or tissues.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090161; P:Golgi ribbon formation; IEA:TreeGrafter.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IEA:TreeGrafter.
DR GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IEA:TreeGrafter.
DR CDD; cd09803; UBAN; 1.
DR FunFam; 1.20.5.990:FF:000009; Optineurin; 1.
DR Gene3D; 1.20.5.390; L1 transposable element, trimerization domain; 2.
DR Gene3D; 1.20.5.990; Nemo cc2-lz domain - 1d5 darpin complex; 1.
DR InterPro; IPR032419; CC2-LZ_dom.
DR InterPro; IPR021063; NEMO_N.
DR InterPro; IPR034735; NEMO_ZF.
DR InterPro; IPR051301; Optineurin/NFkB_EssMod.
DR PANTHER; PTHR31553; NF-KAPPA-B ESSENTIAL MODULATOR; 1.
DR PANTHER; PTHR31553:SF2; OPTINEURIN; 1.
DR Pfam; PF16516; CC2-LZ; 1.
DR Pfam; PF11577; NEMO; 1.
DR Pfam; PF18414; zf_C2H2_10; 1.
DR PROSITE; PS51801; ZF_CCHC_NOA; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..532
FT /note="Optineurin"
FT /id="PRO_0000058073"
FT ZN_FING 502..532
FT /note="CCHC NOA-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT COILED 27..143
FT /evidence="ECO:0000255"
FT COILED 195..466
FT /evidence="ECO:0000255"
FT BINDING 510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 513
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
SQ SEQUENCE 532 AA; 61514 MW; 4BF9AEA4BED7AD39 CRC64;
MENELLNHPH NNNMVNGHQD APYDALSMKN DAEMLEQIKQ LLMENNNLKE TMKQMNQEMK
ERLEELLKRH NQHLLDLNSA NEVLRKELQS LKEKIATSNQ GSAVCSTSEE ASENKQLKNQ
LTRLQAEKAD LLGLISELQL KLGSFSEDSF VEIGFSERES GEIVNEEKAN KILSDHNISY
RTNSIKEEGG GTEPEEVAIS RLLRSLREET QKVERLEKEL FSANKRLAEL EKQTSEFCDK
GVQTEQESEQ SQSEVIISSE VDILKEKVKS LNKELQETND KLNEAKQFKN SLQEKCILLD
KRLQENQVDL EEKQSLRYSI KKLELQVESQ ESEIKLEQNK TEAEKNQLGI LQVSYDKLNS
EYQELRIREI EKVSKVEFNE LLEKLDVCEK ALAKKQFEID EMREMDTKHE EDKETIELLR
AQVDVYCADF HAERSARENI HQEKEQLATR LAYMIQEYEK LKEEMMGKQS IEQLQRRHGA
TSLLDASEGP YLVARGAANM EQPSITVYTC PKCNLTVPDM DTLQIHVMDC IT
//
