OPTN_DANRE
ID OPTN_DANRE Reviewed; 517 AA.
AC Q5RI56; Q6P3H5; Q7SXF4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Optineurin;
GN Name=optn; ORFNames=si:ch211-240l19.3, zgc:66386, zgc:77868;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2003) 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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RI56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RI56-2; Sequence=VSP_013265;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI11882.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX321885; CAI11882.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC055628; AAH55628.1; -; mRNA.
DR EMBL; BC063986; AAH63986.1; -; mRNA.
DR RefSeq; NP_001093536.2; NM_001100066.2.
DR AlphaFoldDB; Q5RI56; -.
DR SMR; Q5RI56; -.
DR STRING; 7955.ENSDARP00000099052; -.
DR iPTMnet; Q5RI56; -.
DR PaxDb; Q5RI56; -.
DR PRIDE; Q5RI56; -.
DR GeneID; 336159; -.
DR KEGG; dre:336159; -.
DR CTD; 10133; -.
DR ZFIN; ZDB-GENE-030131-8103; optn.
DR eggNOG; ENOG502QTG2; Eukaryota.
DR InParanoid; Q5RI56; -.
DR OrthoDB; 745047at2759; -.
DR PhylomeDB; Q5RI56; -.
DR Reactome; R-DRE-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-DRE-8854214; TBC/RABGAPs.
DR PRO; PR:Q5RI56; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
DR GO; GO:0007409; P:axonogenesis; IMP:ZFIN.
DR GO; GO:0042742; P:defense response to bacterium; IMP:ZFIN.
DR GO; GO:0090161; P:Golgi ribbon formation; IBA:GO_Central.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IBA:GO_Central.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0051648; P:vesicle localization; IMP:ZFIN.
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 Alternative splicing; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Endosome; Golgi apparatus; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..517
FT /note="Optineurin"
FT /id="PRO_0000058064"
FT ZN_FING 487..517
FT /note="CCHC NOA-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT REGION 216..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..127
FT /evidence="ECO:0000255"
FT COILED 174..453
FT /evidence="ECO:0000255"
FT COMPBIAS 220..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 495
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 515
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT VAR_SEQ 151..231
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_013265"
FT CONFLICT 94
FT /note="K -> R (in Ref. 2; AAH55628)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="N -> S (in Ref. 2; AAH55628)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="S -> G (in Ref. 2; AAH55628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 59062 MW; 5613F8B04C116795 CRC64;
MNGDISHPRG SGPGNLGSLE ETLQQMNTLI KENRDLKEAL KQTNLSMKER FEGLSAWKEK
QKEERDFLEQ RLEEARTRLN TMDVENEALK NQVKELEKSG AECLHTELEA LRGQILRIQA
EKNDLVAMNS ELQLKMGQGS PSNSFIEIRI ADDDLKVTKD LSSVPEASAF SMPKAESEEQ
TVRQLLRSLR AETDEKERLQ LTLQEARGRI AELESKLEHA DSSAQTSLPS AAETNASTEV
KNLEDQLLKL CNELKQAQIK LDEAESMKRN LQDRCKDLEQ DLGTLKTQLG DKQKVQAEND
CLKVQMESLQ AAIKLEQKKT QDEKNNLNQL KDAYTKLFED YSELQEEKKK RESCVSKDDY
DELQTRFATA EKALADKQQK IDEMKMELFQ KEKDLETISV FQAQAEIYSS DFYAERAARE
KIHEEKERLA TQLEYVKKQN SQLQEEMESL GRHSMSEMQR RHVPRGANPQ GPTAPNNLPG
GRGEWQQQNI PDHACPKCGE VLPDLDSLQI HIMDCII
