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   03-AUG-2022, entry version 57.
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   CTD; 496250; -.
DR   Xenbase; XB-GENE-943661; optn.L.
DR   OrthoDB; 745047at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 496250; Expressed in zone of skin and 19 other tissues.
DR   GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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:0006914; P:autophagy; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR032419; CC2-LZ_dom.
DR   InterPro; IPR021063; NEMO_N.
DR   InterPro; IPR034735; NEMO_ZF.
DR   InterPro; IPR032939; Optineurin.
DR   PANTHER; PTHR31553:SF2; PTHR31553:SF2; 1.
DR   Pfam; PF16516; CC2-LZ; 1.
DR   Pfam; PF11577; NEMO; 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