ID A0A3Q1CX56_AMPOC Unreviewed; 536 AA.
AC A0A3Q1CX56;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Optineurin {ECO:0000256|ARBA:ARBA00018548, ECO:0000256|RuleBase:RU367122};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000030388.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000030388.1}
RP IDENTIFICATION.
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 AlphaFoldDB; A0A3Q1CX56; -.
DR STRING; 80972.ENSAOCP00000030388; -.
DR Ensembl; ENSAOCT00000025350.1; ENSAOCP00000030388.1; ENSAOCG00000021349.1.
DR GeneTree; ENSGT00530000063808; -.
DR OMA; DMKQEMF; -.
DR OrthoDB; 5406882at2759; -.
DR Proteomes; UP000257160; Unplaced.
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:UP000257160};
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 506..536
FT /note="CCHC NOA-type"
FT /evidence="ECO:0000259|PROSITE:PS51801"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 259..414
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 439..473
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 536 AA; 61118 MW; ECDF79A729C15475 CRC64;
MASGGPMMNG DISRSPNQSG TLEETLQQMN ILIQENRDLK EALRQTNLTM KERFEGLSVW
REKQKQERDF LEGRLEEARG RMETLSLQNQ ELSKRLEESE RAGGAPGGRQ SAEMDALRAQ
LARLQAEKND LVALNSELQL KAEQDSREDS FIEIIKVSDG GIDGLNEACG AERSRRPDLS
MTSSRMDSEE VTVSQLLQSL RNETQRGERL QAELQACAAR IRELEERKLS TEESTQTAEP
ETTEAKEDPR KEDKAASEVE NLKSQMMTLF KELQQAQSKL DEAEGMKKNL QDRCREVEQD
VVTLKAQLVE KQAVQSENDR LKLQLGSMQA QSLMEQRKAG EERNNLAQLK DAYTKLFEDY
TELKDERKKR QAQLVEKDVV DELQQRLTAA EEALAVKQNK IDDMKQEMFQ KEKELETISV
FQAQAEVYSS DFYAERAARE KLHEEKERLA AQLEYIKKQN SQLQEEMDSL GRRSLNEMQR
RHVPPAGNPH GAGASLVGRG TDWQHQGNIP EHACPKCNEI LPDLDSLQIH IMDCIN
//