OPTN_CHICK
ID OPTN_CHICK Reviewed; 556 AA.
AC Q90Z16;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Optineurin;
DE AltName: Full=Ag9-C5;
DE AltName: Full=FIP-2;
GN Name=OPTN;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11777338; DOI=10.1006/excr.2001.5413;
RA Li B., Gallin W.J.;
RT "Differential localization of chicken FIP2 homologue, Ag-9C5, in secretory
RT epithelial cells.";
RL Exp. Cell Res. 272:135-145(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12169269; DOI=10.1006/excr.2002.5567;
RA Stroissnigg H., Repitz M., Miloloza A., Linhartova I., Beug H., Wiche G.,
RA Propst F.;
RT "FIP-2, an IkappaB-kinase-gamma-related protein, is associated with the
RT Golgi apparatus and translocates to the marginal band during chicken
RT erythroblast differentiation.";
RL Exp. Cell Res. 278:133-145(2002).
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. May act as
CC autophagy receptor that interacts directly with both the cargo to
CC become degraded and an autophagy modifier of the MAP1 LC3 family.
CC {ECO:0000269|PubMed:11777338, ECO:0000269|PubMed:12169269}.
CC -!- SUBUNIT: Binds to linear ubiquitin chains. Interacts with LC3 family
CC members (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11777338,
CC ECO:0000269|PubMed:12169269}. Cytoplasm, perinuclear region
CC {ECO:0000250}. Golgi apparatus {ECO:0000269|PubMed:12169269}. Golgi
CC apparatus, trans-Golgi network {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle,
CC autophagosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in erythrocytes, skeletal muscle, heart,
CC spleen and brain. Weakly expressed in lung and liver (at protein
CC level). {ECO:0000269|PubMed:11777338, ECO:0000269|PubMed:12169269}.
CC -!- DOMAIN: The LIR (LC3-interacting region) motif mediates the interaction
CC with ATG8 family proteins. {ECO:0000250}.
CC -!- DOMAIN: Ubiquitin-binding motif (UBAN) is essential for its inhibitory
CC function, subcellular localization and interaction with TBK1.
CC {ECO:0000250}.
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DR EMBL; AF380358; AAK69306.1; -; mRNA.
DR EMBL; AF389351; AAM73640.1; -; mRNA.
DR RefSeq; NP_989567.1; NM_204236.1.
DR AlphaFoldDB; Q90Z16; -.
DR SMR; Q90Z16; -.
DR STRING; 9031.ENSGALP00000022287; -.
DR PaxDb; Q90Z16; -.
DR GeneID; 374079; -.
DR KEGG; gga:374079; -.
DR CTD; 10133; -.
DR VEuPathDB; HostDB:geneid_374079; -.
DR eggNOG; ENOG502QTG2; Eukaryota.
DR HOGENOM; CLU_034097_1_0_1; -.
DR InParanoid; Q90Z16; -.
DR OrthoDB; 745047at2759; -.
DR PhylomeDB; Q90Z16; -.
DR PRO; PR:Q90Z16; -.
DR Proteomes; UP000000539; 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:UniProtKB-KW.
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: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 1: Evidence at protein level;
KW Autophagy; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Endosome;
KW Golgi apparatus; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..556
FT /note="Optineurin"
FT /id="PRO_0000058065"
FT ZN_FING 526..556
FT /note="CCHC NOA-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 38..164
FT /evidence="ECO:0000255"
FT COILED 219..487
FT /evidence="ECO:0000255"
FT MOTIF 168..173
FT /note="LIR"
FT MOTIF 453..458
FT /note="UBAN"
FT COMPBIAS 253..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 534
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 537
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01142"
SQ SEQUENCE 556 AA; 64087 MW; 77CDD7F750D01F8F CRC64;
MSSKPQIRPA ENGEHCRSKM ENGMDSMAPP TLSTYTPEEM VQQMKELITE NNELKEAMKL
HNQAMKDRYE ELSIWREKQK EEREFYETKF KEAKQCLLAK CVENEQLQQQ LQSLKEREEG
AEMEGCATPE KEARQLKSKV QRLQAEKADL LAIISELQVK LNIASAEDSF VEIGMNEEVN
RTARENQDNS SEMASNIAVY IRSKSADESK NLESEELTVS QLLCCLRNET QRREKLEKEL
QDHKERLSKM ENETSNCLES GTQTNQEEES SEAIGSEVES LKKQICALFK ELQEAHEKLK
EAELIQKKLQ EKCQTLEKVN SAAATELEEK QQLIYTIKKL ELQVESVQAE VKLEQAKTQD
EKTRYSSLQD AYNKLLAELT EAMKTISEMK VKEHDRVDKV VVEELNAKVL LAEQALAAKQ
LQMDEMKQLI AKQEEDLETM AVLRAQMEVY CSDFHAERAA REKIHEEKEQ LAVQLAYLLK
EQQNLEDLGR SSLAEMQNRH GARAPDREHS PRLVQRGTGS QEWPEQRNIS IYSCPKCEEI
LPDLDTLQIH VMDCIN
