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Database: UniProt
Entry: A0A6P8UE56_GYMAC
LinkDB: A0A6P8UE56_GYMAC
Original site: A0A6P8UE56_GYMAC 
ID   A0A6P8UE56_GYMAC        Unreviewed;      1300 AA.
AC   A0A6P8UE56;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   05-FEB-2025, entry version 20.
DE   SubName: Full=Protein NLRC3-like isoform X4 {ECO:0000313|RefSeq:XP_034075284.1};
GN   Name=LOC117548245 {ECO:0000313|RefSeq:XP_034075284.1};
OS   Gymnodraco acuticeps (Antarctic dragonfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Bathydraconidae; Gymnodraco.
OX   NCBI_TaxID=8218 {ECO:0000313|Proteomes:UP000515161, ECO:0000313|RefSeq:XP_034075284.1};
RN   [1] {ECO:0000313|RefSeq:XP_034075284.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (OCT-2024) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00004187}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004193}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004193}. Inflammasome
CC       {ECO:0000256|ARBA:ARBA00004110}.
CC   -!- SIMILARITY: Belongs to the NLRP family.
CC       {ECO:0000256|ARBA:ARBA00008665}.
CC   -!- SIMILARITY: Belongs to the NOD1-NOD2 family.
CC       {ECO:0000256|ARBA:ARBA00038296}.
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DR   RefSeq; XP_034075284.1; XM_034219393.1.
DR   Proteomes; UP000515161; Unplaced.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0061702; C:canonical inflammasome complex; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0012501; P:programmed cell death; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   FunFam; 3.40.50.300:FF:001524; Si:dkey-126g1.7; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001315; CARD.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR025307; FIIND_dom.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR029495; NACHT-assoc.
DR   InterPro; IPR007111; NACHT_NTPase.
DR   InterPro; IPR051261; NLR.
DR   InterPro; IPR041267; NLRP_HD2.
DR   InterPro; IPR041075; NOD1/2_WH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24106; NACHT, LRR AND CARD DOMAINS-CONTAINING; 1.
DR   Pfam; PF00619; CARD; 1.
DR   Pfam; PF13553; FIIND; 1.
DR   Pfam; PF14484; FISNA; 1.
DR   Pfam; PF13516; LRR_6; 2.
DR   Pfam; PF05729; NACHT; 1.
DR   Pfam; PF17776; NLRC4_HD2; 1.
DR   Pfam; PF17779; NOD2_WH; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00114; CARD; 1.
DR   SMART; SM01288; FISNA; 1.
DR   SMART; SM00368; LRR_RI; 3.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS50209; CARD; 1.
DR   PROSITE; PS51830; FIIND; 1.
DR   PROSITE; PS50837; NACHT; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Inflammasome {ECO:0000256|ARBA:ARBA00023233};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Necrosis {ECO:0000256|ARBA:ARBA00022590};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000515161};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          110..152
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          251..385
FT                   /note="NACHT"
FT                   /evidence="ECO:0000259|PROSITE:PS50837"
FT   DOMAIN          915..1194
FT                   /note="FIIND"
FT                   /evidence="ECO:0000259|PROSITE:PS51830"
FT   DOMAIN          1210..1300
FT                   /note="CARD"
FT                   /evidence="ECO:0000259|PROSITE:PS50209"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1300 AA;  147851 MW;  1AE27B25D7434C66 CRC64;
     MKLVMKQREE LQTGKDVESE RRKSNCQTPF YTSAEQQEEN RCSVTGFSLR LEKMSDFKVE
     EEDKSQFLSG LCGSEQSEEE PPDFRDEPGP SDTKGKRKSP VPVEEQLSSC ALCQDVLKDP
     VSTSCGHWFC RQCITSYWEQ RPPSGDSCCP QCGERWNILQ TERGLQEVLD EHRLSLRRRC
     ERVTEGTDES ETLLNRIFTE LYITQGQSEE VNTQHEVRQL ETASKKKPLH DTPIKCQDIF
     QASPDQQTPI RAVLTNGVAG VGKSFSVQKF TLDWAEGLGN QDVSLVIPLS FRELNLIKGE
     QYSLLRLLHV FHPTLQKVTA EQLAVCKVLF IFDGLDESRL SLDFTNNEVV SDVSQQSSVN
     VLLTNLIRGK LLSSALVWIT SRPAAANQIP PECVDRVTEV RGFTDAQKEE YFRRRWSDED
     LSSRIISHIK SSRSLHIMCL IPVFCWITAA VLDHMLTTDQ RGQLPKTLTD MYAHFLLVQT
     KRKKQKYEEG HETSPQQLTE ADRELLLKLG RLAFEHLEKG DIMFYQEDLQ RCGLGVTEAL
     VHSGVCTEIF KRESVIFQKT VYCFVHLSIQ EFLAAVYMLH CYTNRDTEVL KDFLQGYYSN
     RYNRDQDYPS LDVFLEGAME KSLQSKNGHL DLFVRFLHGL SLESNQRLLG GLLGRTGKRP
     TIIERLFRGR LGRTDNRPET IQRAISNLKE MSSYNISPER SINIFHCLTE MKDHSVTQEI
     TEFLKSGNRS EELSEIHCSA LAYMLQMSEE VLDELDLRKY NTSDEGRRRL IPAVRNCRKA
     ELTDCRLSET DCEVVASALK SNPSHLRDLD LSRNALEDSG VELLSSGLKS PICRLEALRL
     ELCSLSEISC SALISALKSN LHLRHLDLSY NNLKDSGVKL RDLLESPDCR LETLRINGET
     FRAKIQKTCD SDVEQEVKTD REAPQSFSPE LTTESSYRFR CPGPGEFQCA STGLVFVMAQ
     EAELLYRAVP WEESLLQSAG KQAAGPLFDV KSSDEAAVCQ LHLPHSETED ALLLDGLLSV
     VHITDEGLSI LEPLEVTRTH VVVKVLHLSP FGLIIDKLKR LLKWRINGQV LVFLRPPGRE
     EQILDVFLLH NNVPEEEVVK KHKRAVNIPI SSDCELDIDH SYSVHCEPEG FFIQPESKTF
     KSMFGPNYHP TFQVSLMTST ERVFLKVQNQ GGNEVWNYRV SLEDPRKELS QRNVPAESRV
     PAESRIPAES RVPAKEWLLS VRTEFIQRVS LSVLKDLLDK LFQSEVINES EMESAKTKSR
     NDGAREVVDV VRNKGAAASR VLINALRELD PLLYEELNSS
//
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