ID A0A060XEI8_ONCMY Unreviewed; 534 AA.
AC A0A060XEI8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Optineurin {ECO:0000256|ARBA:ARBA00018548, ECO:0000256|RuleBase:RU367122};
GN ORFNames=GSONMT00035189001 {ECO:0000313|EMBL:CDQ75260.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ75260.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ75260.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ75260.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-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; FR905038; CDQ75260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060XEI8; -.
DR STRING; 8022.A0A060XEI8; -.
DR PaxDb; 8022-A0A060XEI8; -.
DR Proteomes; UP000193380; 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:UP000193380};
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 504..534
FT /note="CCHC NOA-type"
FT /evidence="ECO:0000259|PROSITE:PS51801"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 440..474
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 235..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 61369 MW; 94D40691E7354736 CRC64;
MASSSPMVNG EVSRGPSSHP GHSPTTGTLE ETLQQMNRLI QENRDLKEAL KQTNMSMKER
FEGLSVWREK QREEKEFLEE RLDEARGRVE ALSSHNQELS MKVEELEGEG KGQAETANQN
AELEALHAQL VRLQAEKSDL VAMNSELQLK AGQGSEDDSF IEIRIAREDT GKDLYHNERD
PRYDMSVSRQ ESEELTVSQL LQSLRKETQR VERLQIELQA TRSRITELEE KETNTESSTQ
TSLLPEVEPQ QNSGKEKAVS EVEDLKAQMM TLFNELQQAQ SKLDEAEGMK MNLQDRCRDV
ERDVVTLKAQ LVEKQEVQSE NDRLKLQVDS MKAQSQLEQR KAGEERTNLT QLKDAYTKLF
EDYNELKQES KNREPLVTKE VGDLQTRLDA AEKALAAKQQ QIDVMKQEIY QKEKELETIS
VFQAQAEVYS SDFYAERAAR EKIHEEKERL FAQLEFVKKQ NTQLQDEMDS LGRQSLSDMQ
RRHMPRGGNM QGARGGDARD WQQQGNIPEH VCPKCNEILP DLDSLQIHIM DCII
//
