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Database: UniProt
Entry: A0A1U8D0B9_ALLSI
LinkDB: A0A1U8D0B9_ALLSI
Original site: A0A1U8D0B9_ALLSI 
ID   A0A1U8D0B9_ALLSI        Unreviewed;       566 AA.
AC   A0A1U8D0B9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Optineurin {ECO:0000256|ARBA:ARBA00018548, ECO:0000256|RuleBase:RU367122};
GN   Name=LOC102372550 {ECO:0000313|RefSeq:XP_014374732.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014374732.1};
RN   [1] {ECO:0000313|RefSeq:XP_014374732.1}
RP   IDENTIFICATION.
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}.
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DR   RefSeq; XP_014374732.1; XM_014519246.2.
DR   AlphaFoldDB; A0A1U8D0B9; -.
DR   STRING; 38654.A0A1U8D0B9; -.
DR   GeneID; 102372550; -.
DR   KEGG; asn:102372550; -.
DR   eggNOG; ENOG502QTG2; Eukaryota.
DR   InParanoid; A0A1U8D0B9; -.
DR   OrthoDB; 5406882at2759; -.
DR   Proteomes; UP000189705; 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:UP000189705};
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          536..566
FT                   /note="CCHC NOA-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51801"
FT   COILED          110..200
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          226..367
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          412..453
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   566 AA;  65183 MW;  086762AFFA23DF9C CRC64;
     MPFAACFSPR RPQCKKLAAV MSSCPAENGK CPNSEMENGT HDMAPSTFSM YTPEEMVQQM
     KELITENNEL KEAMKLHNQA MKDRYEELSV WREKQKEERE FFESKFKEAK NCLQAKCVEN
     EELRKQLQNL KERKEGPEME LAQLKTQMTR LQAEKADLVA IISELQLKLN ISGEDSFVEI
     RMMEGEVSRA LRENQDINSQ GTSDVAAFMD KSMDEVKNLE SEELTVSQLL HCLRNETQQR
     ESLEKELQEH KERLLKLEKA ASDQLEIGTQ TEWENEEDKS SETVGSEIET LNLQVSALFK
     ELQEAHSKLK EAELIQKKLQ EKCQILERKS AAVSTDQDEK QQLLYTIKKL ELQVESMQSE
     IKLEQAKTQE EKTKCAALQE AYSKLLPEFT DALSTVEELK SKESERVEKV VVEELNKKLE
     LAEKALATKQ LQLDEIKQTI AKQEEDLETM AVLRAQMELY CSDFHAERAA REKIHEEKEQ
     LAVQLAYLLK DQSNLEDLGR NSLVEMQSRH GARTSLDRER LPHLVRRGTG GQDWQQSNIP
     MHSCPKCGEI LPDIDTLQIH VMDCII
//
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