ID   A0A091UFN0_PHORB        Unreviewed;       531 AA.
AC   A0A091UFN0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Optineurin {ECO:0000256|ARBA:ARBA00018548, ECO:0000256|RuleBase:RU367122};
GN   ORFNames=N337_11778 {ECO:0000313|EMBL:KFQ89549.1};
OS   Phoenicopterus ruber ruber.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Phoenicopteriformes; Phoenicopteridae;
OC   Phoenicopterus.
OX   NCBI_TaxID=9218 {ECO:0000313|EMBL:KFQ89549.1, ECO:0000313|Proteomes:UP000053700};
RN   [1] {ECO:0000313|EMBL:KFQ89549.1, ECO:0000313|Proteomes:UP000053700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N337 {ECO:0000313|EMBL:KFQ89549.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act by regulating membrane trafficking and cellular
CC       morphogenesis. {ECO:0000256|RuleBase:RU367122}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000256|RuleBase:RU367122}. Golgi apparatus
CC       {ECO:0000256|RuleBase:RU367122}. Golgi apparatus, trans-Golgi network
CC       {ECO:0000256|ARBA:ARBA00004601, ECO:0000256|RuleBase:RU367122}.
CC       Cytoplasmic vesicle, autophagosome {ECO:0000256|ARBA:ARBA00004419,
CC       ECO:0000256|RuleBase:RU367122}. Cytoplasmic vesicle
CC       {ECO:0000256|RuleBase:RU367122}. Recycling endosome
CC       {ECO:0000256|RuleBase:RU367122}. Endosome
CC       {ECO:0000256|ARBA:ARBA00004177}. Vesicle
CC       {ECO:0000256|ARBA:ARBA00004373}.
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DR   EMBL; KK433403; KFQ89549.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091UFN0; -.
DR   Proteomes; UP000053700; Unassembled WGS sequence.
DR   GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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-UniRule.
DR   CDD; cd09803; UBAN; 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   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   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367122};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW   ECO:0000256|RuleBase:RU367122};
KW   Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|RuleBase:RU367122};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|RuleBase:RU367122};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367122};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053700};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367122};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01142}.
FT   DOMAIN          501..531
FT                   /note="CCHC NOA-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51801"
FT   REGION          87..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          184..218
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          267..332
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          377..411
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        89..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   531 AA;  61287 MW;  5AA4588831A36D40 CRC64;
     MAAPALSTYT PEEMVQQMKE LITENNELKE AMKVHNQAMK DRYEELSIWR EKQKEEREFY
     ELKFKEAKQC LLAKCIENEQ LQQQLQSLKE REEGAEMEGR TAPEKKVRQL KSQVQRLQAE
     KADLLAIISE LQVKLNISSA EDSFVEIGMN VSEGNKKNTV TCGQKLWSKP ADELKNLESE
     ELTVSQLLCC LRNETQKREK LEKELQDHRE RYELFSFKAA AVTKSVTDQK QTEISVTTDQ
     DKLHISSWVG SEVETLNLQV CALFKELQEA HEKLKEAELI QKKLQEKCQV LERKSSAAAS
     ELEEKQQLIY TVKKLELQVE SMQAEVKLEQ AKTHEEKARC SSLQDAYGKL LPELTVARKT
     IDEMKLKELD RVDKAVVEQL NAKVELAEQA LAAKQLQIDE MKQIIAKQEE DLETMAVLRA
     QMEVYCSDFH AERAAREKIH EEKEQLAVQL AYLLKEQQNL EDFGRNSLAE MQNRHGARAP
     DREHSPHLVQ QGTGSQDWPE QRNISMYSCP KCEEILPDLD TLQIHVMDCI N
//