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Database: UniProt
Entry: A0A2Y9IKW3_ENHLU
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ID   A0A2Y9IKW3_ENHLU        Unreviewed;      1035 AA.
AC   A0A2Y9IKW3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=NACHT, LRR and PYD domains-containing protein 3 {ECO:0000256|ARBA:ARBA00040040};
GN   Name=LOC111139817 {ECO:0000313|RefSeq:XP_022347944.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022347944.1};
RN   [1] {ECO:0000313|RefSeq:XP_022347944.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022347944.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00034440};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00034440};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center {ECO:0000256|ARBA:ARBA00004267}. Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004394}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion
CC       {ECO:0000256|ARBA:ARBA00004173}. Secreted
CC       {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the NLRP family.
CC       {ECO:0000256|ARBA:ARBA00008665}.
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DR   RefSeq; XP_022347944.1; XM_022492236.1.
DR   AlphaFoldDB; A0A2Y9IKW3; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   CDD; cd00116; LRR_RI; 1.
DR   CDD; cd08320; Pyrin_NALPs; 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   InterPro; IPR004020; DAPIN.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR029495; NACHT-assoc.
DR   InterPro; IPR007111; NACHT_NTPase.
DR   InterPro; IPR041267; NLRP_HD2.
DR   InterPro; IPR041075; NOD2_WH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45690; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 12; 1.
DR   PANTHER; PTHR45690:SF19; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 3; 1.
DR   Pfam; PF14484; FISNA; 1.
DR   Pfam; PF13516; LRR_6; 5.
DR   Pfam; PF05729; NACHT; 1.
DR   Pfam; PF17776; NLRC4_HD2; 1.
DR   Pfam; PF17779; NOD2_WH; 1.
DR   Pfam; PF02758; PYRIN; 1.
DR   SMART; SM01288; FISNA; 1.
DR   SMART; SM00368; LRR_RI; 9.
DR   SMART; SM01289; PYRIN; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS50824; DAPIN; 1.
DR   PROSITE; PS50837; NACHT; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          1..93
FT                   /note="Pyrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50824"
FT   DOMAIN          215..531
FT                   /note="NACHT"
FT                   /evidence="ECO:0000259|PROSITE:PS50837"
SQ   SEQUENCE   1035 AA;  118757 MW;  F58438FFF83C13B7 CRC64;
     MNMASVRCKL AHYLEDLEDA DFKKFKMHLQ DYPSQKGCRP LPRSQTEKAD HMDLATLMID
     FNGEEKAWAM AVWIFAAINR RDLYEKAKRD APECDNVHVV CREESLEEEW MGLLGYLTRI
     SICKKRKDYC KKYKKHVRSR FQCIKDRNAR LGESVNLNKR YTRLRLVKEH QSQQEREHEL
     LAIGRTSART LDSPVSSLNM ELLFEPDDQH SEPVHTVVFQ GAAGIGKTIL ARKIMLDWAS
     EKIYQDRFDY LFYIHCREVS LGTRRSLGDL IVSCCPDPNP PIYKIVSKPS RILFLMDGFD
     ELQGAFDEHT ETLCTNWQKV ERGDILLSSL IRKRLLPEAS LLITTRPVAL EKLQHLLDRP
     RHVEILGFSE AKRKEYFFKY FSDEQQATEA FRLIQENEIL FTMCFIPLVC WIVCTGLKQQ
     MDSGKSLAQT SKTTTAVYVF FLSSLLQSRG ENQKHQVSAN IWGLCSLAAD GIWNQKILFE
     ECDLRNHGLQ RADVSAFLRM NLFQKEVDCE KFYSFIHMTF QEFFAAMYYL LEEEEQGRLR
     NLPWRSSKLP NRDVTVLLEN YGKFEKGYLI FVVRFLFGLV NQERTSYLEK KLSCKISQHI
     RLELLKWIKE KAKAKNLQIQ PSQLELFYCL YEMQEEDFVQ KAMGHFPKIE ISLSTRMDHV
     VSSFCIENCH NVESLSLRLL HNSSKEEEEE EEEEGEMQHS EVDHCVRLDP HAACTHRLVN
     CHVTLSLWQG LFSVLSTNSL NLTELNLSDN ALGDPGVQVL CEMLQRPGCN IRRLWLGRCC
     LSHHCCFNIS SVLSSNQKLM ELDLSHNALG DFGIRLLCVG LRHLFCNLKK LWLVSCCLTS
     ACCEDLASVL STNQSLTRLY LGENALGDAG VGILCEKAKH PQCKLQKLGL MNSGLTSGCC
     SALSSVLSTN QKLTHLYLRG NALGDTGVKL LCEGLLHPNC KLQILELDGC SLTSHCCWDL
     STLLTSNKSL RELSLGSNDL GDLGVMLLCE VLKQQGCLLK SLKLCEMYFN YDTKCALEAL
     QEEKPELSIV FEPFW
//
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