ID A0A3Q7TR60_VULVU Unreviewed; 574 AA.
AC A0A3Q7TR60;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Optineurin {ECO:0000256|ARBA:ARBA00018548, ECO:0000256|RuleBase:RU367122};
GN Name=OPTN {ECO:0000313|RefSeq:XP_025872268.1,
GN ECO:0000313|RefSeq:XP_025872274.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025872268.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025872268.1, ECO:0000313|RefSeq:XP_025872274.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025872268.1,
RC ECO:0000313|RefSeq:XP_025872274.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025872268.1,
RC ECO:0000313|RefSeq:XP_025872274.1};
RG RefSeq;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_025872268.1; XM_026016483.1.
DR RefSeq; XP_025872274.1; XM_026016489.1.
DR STRING; 9627.ENSVVUP00000007813; -.
DR Ensembl; ENSVVUT00000010320; ENSVVUP00000007819; ENSVVUG00000005909.
DR KEGG; vvp:112933320; -.
DR OMA; DMKQEMF; -.
DR OrthoDB; 5406882at2759; -.
DR Proteomes; UP000286640; 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:UP000286640};
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 544..574
FT /note="CCHC NOA-type"
FT /evidence="ECO:0000259|PROSITE:PS51801"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 90..153
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 231..261
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 293..496
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 65683 MW; 8E312DD8130F237C CRC64;
MSHQPLSCLT AKGDSSNETT GNGPPDLAHP NLDTFTPEEL LQQMKELLTE NHQLKEAMKL
NNQAMKGRFE ELSAWTEKQK EERLYFEVQS KEAKERLMAL SHENEKLKEE LEKLKGKTEM
SLKDPAGDLK APKAEADQEV EQLKTQVAYL QAEKADLLGI VSELQLKLNS GGPSEDSFVE
IRIAEGEADV AVREIRTSPG PTRTDSIDTN KSTEGARNYL EFEKLTVSQL LLCLREENQK
VERLKTALKE AKERVLYFEK KASGGSEIET QTEESTEKER EEEKGPETVG SEVETLNRQV
TTLFKELQEA HTKLSEAELM KKRLQEKCQT LERKNSATPA ELNEKQELVY NNKKLELQVE
SMRSEIKMEQ AKTEEEKSKL ATLQLTHNKL LQEYNNSLKT IEELKRKESE KVDKVILQEL
SEKLELAEKA LASKQLQMDE MKQTIAKQEE DLETMTVLRA QMEVYCSDFH AERAAREKIH
EEKEQLALQL AILLKENNAF EDGGSRQSLM EMQSRHGART SDPDQQAYLV QRGTEDRSWQ
RQQQRNIPIH SCPKCGEVLP DIDTLQIHVM DCII
//
