ID G1SRQ8_RABIT Unreviewed; 521 AA.
AC G1SRQ8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Optineurin {ECO:0000256|ARBA:ARBA00018548, ECO:0000256|RuleBase:RU367122};
GN Name=OPTN {ECO:0000313|Ensembl:ENSOCUP00000005877.4};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000005877.4, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000005877.4, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000005877.4,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000005877.4}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000005877.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AAGW02026698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02026699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02026700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02026701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1SRQ8; -.
DR SMR; G1SRQ8; -.
DR STRING; 9986.ENSOCUP00000005877; -.
DR PaxDb; 9986-ENSOCUP00000005877; -.
DR Ensembl; ENSOCUT00000006796.4; ENSOCUP00000005877.4; ENSOCUG00000006794.4.
DR eggNOG; ENOG502QTG2; Eukaryota.
DR GeneTree; ENSGT00530000063808; -.
DR HOGENOM; CLU_034097_1_0_1; -.
DR InParanoid; G1SRQ8; -.
DR TreeFam; TF326608; -.
DR Proteomes; UP000001811; Chromosome 16.
DR Bgee; ENSOCUG00000006794; Expressed in testis and 15 other cell types or tissues.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0034620; P:cellular response to unfolded protein; IEA:Ensembl.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
DR GO; GO:0090161; P:Golgi ribbon formation; IEA:Ensembl.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IEA:Ensembl.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0001920; P:negative regulation of receptor recycling; IEA:Ensembl.
DR GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:1904417; P:positive regulation of xenophagy; IEA:Ensembl.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IEA:Ensembl.
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 Autophagy {ECO:0000256|ARBA:ARBA00023006};
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:UP000001811};
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 491..521
FT /note="CCHC NOA-type"
FT /evidence="ECO:0000259|PROSITE:PS51801"
FT REGION 203..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..34
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 60..123
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 254..443
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 203..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 60243 MW; 1CD47900F944985A CRC64;
KPGHFHAEEL LQQMKELLTE NHQLKEAMKL NNQAMKGRFE ELSAWSEKQK EERQFFELQS
KESKERIMAL SHENKKLKEE LGKLKGELEK SFERPTGHCR FPKWEAEQEM DQLKTQVARL
QADMRGIVSG LQLKLNSSGN SDHSFVELRM EEAEANGTVK EIKNKNSPGP TRTDSIKTNY
LEFKELTVSQ FLLCLKEGTQ RVSSFEKRAN DRSESETQTE GSMQKENEEE KGTESVGNEV
EMLNLQVTSL FKELQEAHTK LSEAELMKKR LQEKCQALDR KNSATPSELS EKQELIYNNK
KLELQVESMR SEIKMEQAKT ENEKSKLATL QSTHNKLLQE HNSALKTIEE LTRKESEKVD
KVVLQQLNEK LELAEKALAS KQLQMDEMKQ TIAKQEEDLE TMAVLRAQME VYCSDFHAER
AAREKIHEEK EQLALQLAIL LKENNAFEDG GSRQSLMEMQ SRHGARTNDP DQQAYLVQRG
AEDRDWQQQQ QWNIPIHSCP RCGEVLPDID TLQIHVMDCI I
//
