NALP5_MOUSE
ID NALP5_MOUSE Reviewed; 1163 AA.
AC Q9R1M5; Q3UXD0; Q53ZD5; Q6VSF9; Q6VSG0; Q6VSG1; Q6VSG2; Q6VSG3; Q6VSG4;
AC Q6VSG5; Q6XZF2; Q7TPU9; Q9JLR2;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=NACHT, LRR and PYD domains-containing protein 5;
DE AltName: Full=Maternal antigen that embryos require;
DE Short=Mater protein;
DE AltName: Full=Ooplasm-specific protein 1;
DE Short=OP1;
GN Name=Nlrp5; Synonyms=Mater, Nalp5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND DEVELOPMENTAL STAGE.
RC STRAIN=NIH Swiss; TISSUE=Ovary;
RX PubMed=10433232; DOI=10.1210/endo.140.8.6911;
RA Tong Z.-B., Nelson L.M.;
RT "A mouse gene encoding an oocyte antigen associated with autoimmune
RT premature ovarian failure.";
RL Endocrinology 140:3720-3726(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), AND VARIANTS ASP-59; LEU-94;
RP LYS-139; PRO-308; GLN-1029 AND 1055-ASN-ASN-1056.
RC STRAIN=129/Sv;
RX PubMed=10754103; DOI=10.1007/s003350010053;
RA Tong Z.-B., Nelson L.M., Dean J.;
RT "Mater encodes a maternal protein in mice with a leucine-rich repeat domain
RT homologous to porcine ribonuclease inhibitor.";
RL Mamm. Genome 11:281-287(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=A/J, and C57BL/6J;
RX PubMed=12133995; DOI=10.4049/jimmunol.169.3.1640;
RA Roper R.J., Ma R.Z., Biggins J.E., Butterfield R.J., Michael S.D.,
RA Tung K.S.K., Doerge R.W., Teuscher C.;
RT "Interacting quantitative trait loci control loss of peripheral tolerance
RT and susceptibility to autoimmune ovarian dysgenesis after day 3 thymectomy
RT in mice.";
RL J. Immunol. 169:1640-1646(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 5; 6; 7 AND 8).
RC STRAIN=A/J, C57BL/6J, CBA/J, and SWR/J;
RX PubMed=15481533;
RA Cheng H., Zhang X.J., Liu H.B., Zhang Y., Huang Z.F., Ma R.L.;
RT "Identification and characterization of alternatively splicing variants for
RT murine mater gene.";
RL Yi Chuan Xue Bao 31:795-800(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 397-722.
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [7]
RP FUNCTION.
RX PubMed=11062459; DOI=10.1038/81547;
RA Tong Z.-B., Gold L., Pfeifer K.E., Dorward H., Lee E., Bondy C.A., Dean J.,
RA Nelson L.M.;
RT "Mater, a maternal effect gene required for early embryonic development in
RT mice.";
RL Nat. Genet. 26:267-268(2000).
RN [8]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=14670992; DOI=10.1210/en.2003-1160;
RA Tong Z.-B., Gold L., De Pol A., Vanevski K., Dorward H., Sena P.,
RA Palumbo C., Bondy C.A., Nelson L.M.;
RT "Developmental expression and subcellular localization of mouse MATER, an
RT oocyte-specific protein essential for early development.";
RL Endocrinology 145:1427-1434(2004).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE SCMC COMPLEX WITH KHDC3; OOEP AND TLE6, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=18804437; DOI=10.1016/j.devcel.2008.07.010;
RA Li L., Baibakov B., Dean J.;
RT "A subcortical maternal complex essential for preimplantation mouse
RT embryogenesis.";
RL Dev. Cell 15:416-425(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22357545; DOI=10.1095/biolreprod.111.093583;
RA Fernandes R., Tsuda C., Perumalsamy A.L., Naranian T., Chong J.,
RA Acton B.M., Tong Z.B., Nelson L.M., Jurisicova A.;
RT "NLRP5 mediates mitochondrial function in mouse oocytes and embryos.";
RL Biol. Reprod. 86:1-10(2012).
RN [11]
RP FUNCTION, INTERACTION WITH TUBB3, AND DISRUPTION PHENOTYPE.
RX PubMed=24374158; DOI=10.1016/j.ydbio.2013.12.025;
RA Kim B., Zhang X., Kan R., Cohen R., Mukai C., Travis A.J., Coonrod S.A.;
RT "The role of MATER in endoplasmic reticulum distribution and calcium
RT homeostasis in mouse oocytes.";
RL Dev. Biol. 386:331-339(2014).
RN [12]
RP FUNCTION, INTERACTION WITH CFL1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25208553; DOI=10.1038/ncomms5887;
RA Yu X.J., Yi Z., Gao Z., Qin D., Zhai Y., Chen X., Ou-Yang Y., Wang Z.B.,
RA Zheng P., Zhu M.S., Wang H., Sun Q.Y., Dean J., Li L.;
RT "The subcortical maternal complex controls symmetric division of mouse
RT zygotes by regulating F-actin dynamics.";
RL Nat. Commun. 5:4887-4887(2014).
RN [13]
RP IDENTIFICATION IN THE SCMC COMPLE WITH OOEP; TL6 AND KHDC3, INTERACTION
RP WITH ZBED3, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28992324; DOI=10.1093/jmcb/mjx035;
RA Gao Z., Zhang X., Yu X., Qin D., Xiao Y., Yu Y., Xiang Y., Nie X., Lu X.,
RA Liu W., Yi Z., Li L.;
RT "Zbed3 participates in the subcortical maternal complex and regulates the
RT distribution of organelles.";
RL J. Mol. Cell Biol. 10:74-88(2018).
RN [14]
RP INTERACTION WITH TLE6, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=31575650; DOI=10.1242/dev.183616;
RA Qin D., Gao Z., Xiao Y., Zhang X., Ma H., Yu X., Nie X., Fan N., Wang X.,
RA Ouyang Y., Sun Q.Y., Yi Z., Li L.;
RT "The subcortical maternal complex protein Nlrp4f is involved in cytoplasmic
RT lattice formation and organelle distribution.";
RL Development 146:0-0(2019).
RN [15]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=31118423; DOI=10.1038/s41467-019-10171-7;
RA Vogt E.J., Tokuhiro K., Guo M., Dale R., Yang G., Shin S.W., Movilla M.J.,
RA Shroff H., Dean J.;
RT "Anchoring cortical granules in the cortex ensures trafficking to the
RT plasma membrane for post-fertilization exocytosis.";
RL Nat. Commun. 10:2271-2271(2019).
RN [16]
RP INDUCTION (MICROBIAL INFECTION).
RX PubMed=32731337; DOI=10.3390/microorganisms8081136;
RA Wang J., Liu T., Mahmmod Y.S., Yang Z., Tan J., Ren Z., Zhang X., Yang X.,
RA Zhang X.X., Yuan Z.G.;
RT "Transcriptome Analysis of Testes and Uterus: Reproductive Dysfunction
RT Induced by Toxoplasma gondii in Mice.";
RL Microorganisms 8:0-0(2020).
CC -!- FUNCTION: As a member of the subcortical maternal complex (SCMC), plays
CC an essential role for zygotes to progress beyond the first embryonic
CC cell divisions via regulation of actin dynamics (PubMed:11062459,
CC PubMed:18804437, PubMed:25208553). Required for the formation of F-
CC actin cytoplasmic lattices (CPL) in oocytes, which in turn are
CC responsible for symmetric division of zygotes via the regulation of
CC mitotic spindle formation and positioning (PubMed:25208553). Required
CC for the localization of cortical granules to the cortex of oocytes, via
CC association with the cortical actin scaffold (PubMed:31118423).
CC Required for cortical actin clearance prior to oocyte exocytosis and
CC prevention of polyspermy (PubMed:31118423). Involved in regulating
CC post-fertilization Ca(2+) release and endoplasmic reticulum storage
CC (ER) storage via regulation of cellular localization (PubMed:24374158).
CC May be involved in the localization of mitochondria to the cytoplasm
CC and perinuclear region in oocytes and early stage embryos, independent
CC of its role in CPL formation (PubMed:22357545).
CC {ECO:0000269|PubMed:11062459, ECO:0000269|PubMed:18804437,
CC ECO:0000269|PubMed:22357545, ECO:0000269|PubMed:24374158,
CC ECO:0000269|PubMed:25208553, ECO:0000269|PubMed:31118423}.
CC -!- SUBUNIT: Component of the subcortical maternal complex (SCMC), at least
CC composed of NLRP5, KHDC3, OOEP, and TLE6 (PubMed:18804437,
CC PubMed:28992324, PubMed:31575650). Within the complex, interacts with
CC OOEP, KHDC3 and TLE6 (PubMed:18804437, PubMed:28992324,
CC PubMed:31575650). The SCMC may facilitate translocation of its
CC components between the nuclear and cytoplasmic compartments (By
CC similarity). As part of the SCMC interacts with the SCMC-associated
CC protein ZBED3 (PubMed:28992324). As part of the SCMC interacts with the
CC SCMC-associated protein CFL1/Cofilin-1 (PubMed:25208553). Interacts
CC with PRKCE (By similarity). Interacts with TUBB3 at cytoskeleton
CC microtubules (PubMed:24374158). {ECO:0000250|UniProtKB:P59047,
CC ECO:0000269|PubMed:18804437, ECO:0000269|PubMed:24374158,
CC ECO:0000269|PubMed:25208553, ECO:0000269|PubMed:28992324,
CC ECO:0000269|PubMed:31575650}.
CC -!- INTERACTION:
CC Q9R1M5; Q9CWU5: Khdc3; NbExp=3; IntAct=EBI-2905719, EBI-2905804;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, Cortical
CC granule {ECO:0000250|UniProtKB:P59047}. Mitochondrion
CC {ECO:0000269|PubMed:14670992}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:14670992}. Cytoplasm {ECO:0000269|PubMed:14670992,
CC ECO:0000269|PubMed:28992324, ECO:0000269|PubMed:31575650}. Golgi
CC apparatus {ECO:0000250|UniProtKB:P59047}. Note=Located in mitochondria
CC and nucleoli in primary follicle oocytes (PubMed:14670992). Colocalizes
CC with ZBED3 and NLRP4F in the oocyte subcortex (PubMed:25208553,
CC PubMed:28992324, PubMed:31575650). Not detected in oocyte mitochondria
CC in type 2 follicles (PubMed:14670992). In the subcortical cytoplasm of
CC early embryos from the 1-cell to the blastocyst stages
CC (PubMed:14670992, PubMed:25208553). From the 2-cell stage, still
CC detected in the subcortex, but excluded from cell-cell contact regions
CC (PubMed:14670992). Expression largely disappears in blastocysts
CC (PubMed:25208553). {ECO:0000269|PubMed:14670992,
CC ECO:0000269|PubMed:25208553, ECO:0000269|PubMed:28992324,
CC ECO:0000269|PubMed:31575650}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=D;
CC IsoId=Q9R1M5-1; Sequence=Displayed;
CC Name=2; Synonyms=C;
CC IsoId=Q9R1M5-2; Sequence=VSP_024728;
CC Name=3; Synonyms=B;
CC IsoId=Q9R1M5-3; Sequence=VSP_024727;
CC Name=4; Synonyms=A;
CC IsoId=Q9R1M5-4; Sequence=VSP_024726;
CC Name=5; Synonyms=E;
CC IsoId=Q9R1M5-5; Sequence=VSP_024727, VSP_024729;
CC Name=6; Synonyms=G;
CC IsoId=Q9R1M5-6; Sequence=VSP_024727, VSP_024733;
CC Name=7; Synonyms=H;
CC IsoId=Q9R1M5-7; Sequence=VSP_024727, VSP_024731, VSP_024732;
CC Name=8; Synonyms=F;
CC IsoId=Q9R1M5-8; Sequence=VSP_024727, VSP_024730;
CC -!- DEVELOPMENTAL STAGE: Expression is first detected in oocytes of type 3A
CC primary follicles (PubMed:14670992, PubMed:31118423). Transcripts
CC accumulate during oogenesis (PubMed:14670992). Expressed in the
CC cytoplasm of germinal vesicle oocytes before becoming concentrated in
CC the subcortex of metaphase 2 oocytes (PubMed:28992324,
CC PubMed:31118423). During meiotic maturation, the vast majority of the
CC transcripts are degraded and virtually none is detected by 2-cell stage
CC embryogenesis (PubMed:14670992, PubMed:18804437). The protein however
CC persists during preimplantation up to the blastocyst stage
CC (PubMed:14670992, PubMed:18804437). At 2-cell stage, excluded from
CC cell-cell contact regions (PubMed:18804437). Continuous exclusion from
CC these regions during preimplantation development leads to the absence
CC of the protein from the inner cells of the morula and the inner cell
CC mass of the blastocyst (PubMed:18804437). Expressed in ovaries at
CC birth, expression peaks at postnatal day 10 (P10), expression is then
CC decreased at P17 and further decreased at P21 (PubMed:10433232,
CC PubMed:31575650). {ECO:0000269|PubMed:10433232,
CC ECO:0000269|PubMed:14670992, ECO:0000269|PubMed:18804437,
CC ECO:0000269|PubMed:28992324, ECO:0000269|PubMed:31118423,
CC ECO:0000269|PubMed:31575650}.
CC -!- INDUCTION: (Microbial infection) Reduced by T.gondii in the testes and
CC uterus. {ECO:0000269|PubMed:32731337}.
CC -!- PTM: Phosphorylated by PRKCE. {ECO:0000250|UniProtKB:P59047}.
CC -!- DISRUPTION PHENOTYPE: Mice appear phenotypically normal with no
CC apparent defects in ovarian development, oocyte maturation or ovulation
CC (PubMed:14670992, PubMed:22357545). Cortical granules are scattered
CC throughout the cytoplasm in oocytes and ovulated eggs
CC (PubMed:31118423). Reduced abundance of intact MYH9/MyoIIA and MYO5A,
CC the dense cortical actin scaffold remained present prior to exocytosis
CC (PubMed:31118423). Increase in polyspermy in the perivitelline space
CC resulting from a decrease in efficacy of the zona pellucida block.
CC Increase in multiple pronuclei and delay in cortical granule exocytosis
CC and ZP2 cleavage (PubMed:31118423). Embryos form unequal sized
CC blastomeres due to smaller, dysmorphic, and displaced mitotic spindles
CC resulting in asymmetric division (PubMed:25208553). Increase in
CC apoptotic cells in blastomeres which progress beyond the 8-cell stage
CC (PubMed:22357545). Decrease in thickness of subcortical F-actin in
CC zygotes, thickening of F-actin bundles in the cytoplasm and loss of F-
CC actin cytoplasmic lattices (PubMed:25208553). Increase in subcortical
CC mitochondrial clustering of mitochondria in 2-cell embryos
CC (PubMed:22357545). Increase in mitochondria activity, shown by an
CC increase in membrane potential and reactive oxygen species
CC (PubMed:22357545). Decrease in expression of the SCMC-associated
CC protein ZBED3 in the cytoplasm of oocytes (PubMed:28992324). In
CC knockdown mice M2 oocytes show a diffuse ER distribution pattern with a
CC reduced number of cortical ER clusters and random movement of lipid
CC droplets during oocyte maturation (PubMed:24374158). Reduces tubulin
CC localization to the cellular microtubular architecture
CC (PubMed:24374158). Decrease in storage and release of Ca(2+) from the
CC endoplasmic reticulum, and disruption of Ca(2+) oscillations following
CC oocyte fertilization (PubMed:24374158). diffused localization of
CC ITPR1/IP3R-1 throughout the cytoplasm with reduced clustering at the
CC oocyte cortex (PubMed:24374158). {ECO:0000269|PubMed:14670992,
CC ECO:0000269|PubMed:22357545, ECO:0000269|PubMed:24374158,
CC ECO:0000269|PubMed:25208553, ECO:0000269|PubMed:28992324,
CC ECO:0000269|PubMed:31118423}.
CC -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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 EMBL; AF074018; AAD51762.1; -; mRNA.
DR EMBL; AF143573; AAF64393.1; -; Genomic_DNA.
DR EMBL; AF143559; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143560; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143561; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143562; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143563; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143564; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143565; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143566; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143567; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143568; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143569; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143570; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143571; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AF143572; AAF64393.1; JOINED; Genomic_DNA.
DR EMBL; AY196361; AAO52697.1; -; mRNA.
DR EMBL; AY196362; AAO52698.1; -; mRNA.
DR EMBL; AY329484; AAQ94607.1; -; mRNA.
DR EMBL; AY329485; AAQ94608.1; -; mRNA.
DR EMBL; AY329486; AAQ94609.1; -; mRNA.
DR EMBL; AY329487; AAQ94610.1; -; mRNA.
DR EMBL; AY329488; AAQ94611.1; -; mRNA.
DR EMBL; AY329489; AAQ94612.1; -; mRNA.
DR EMBL; AY329490; AAQ94613.1; -; mRNA.
DR EMBL; AY329491; AAQ94614.1; -; mRNA.
DR EMBL; BC053384; AAH53384.1; -; mRNA.
DR EMBL; AK135731; BAE22633.1; -; mRNA.
DR CCDS; CCDS20929.1; -. [Q9R1M5-5]
DR CCDS; CCDS20930.1; -. [Q9R1M5-3]
DR CCDS; CCDS85233.1; -. [Q9R1M5-6]
DR PIR; A59000; A59000.
DR RefSeq; NP_001034232.1; NM_001039143.2. [Q9R1M5-5]
DR RefSeq; NP_001292786.1; NM_001305857.1. [Q9R1M5-6]
DR RefSeq; NP_035990.1; NM_011860.3. [Q9R1M5-3]
DR AlphaFoldDB; Q9R1M5; -.
DR SMR; Q9R1M5; -.
DR BioGRID; 204829; 3.
DR CORUM; Q9R1M5; -.
DR IntAct; Q9R1M5; 3.
DR STRING; 10090.ENSMUSP00000015866; -.
DR iPTMnet; Q9R1M5; -.
DR PhosphoSitePlus; Q9R1M5; -.
DR MaxQB; Q9R1M5; -.
DR PaxDb; Q9R1M5; -.
DR PRIDE; Q9R1M5; -.
DR ProteomicsDB; 293621; -. [Q9R1M5-1]
DR ProteomicsDB; 293622; -. [Q9R1M5-2]
DR ProteomicsDB; 293623; -. [Q9R1M5-3]
DR ProteomicsDB; 293624; -. [Q9R1M5-4]
DR ProteomicsDB; 293625; -. [Q9R1M5-5]
DR ProteomicsDB; 293626; -. [Q9R1M5-6]
DR ProteomicsDB; 293627; -. [Q9R1M5-7]
DR ProteomicsDB; 293628; -. [Q9R1M5-8]
DR Antibodypedia; 46495; 81 antibodies from 26 providers.
DR DNASU; 23968; -.
DR Ensembl; ENSMUST00000015866; ENSMUSP00000015866; ENSMUSG00000015721. [Q9R1M5-3]
DR Ensembl; ENSMUST00000086341; ENSMUSP00000083524; ENSMUSG00000015721. [Q9R1M5-5]
DR Ensembl; ENSMUST00000108441; ENSMUSP00000104080; ENSMUSG00000015721. [Q9R1M5-6]
DR Ensembl; ENSMUST00000133237; ENSMUSP00000122007; ENSMUSG00000015721. [Q9R1M5-7]
DR Ensembl; ENSMUST00000139661; ENSMUSP00000118638; ENSMUSG00000015721. [Q9R1M5-8]
DR GeneID; 23968; -.
DR KEGG; mmu:23968; -.
DR UCSC; uc009foe.2; mouse. [Q9R1M5-1]
DR UCSC; uc009fof.2; mouse. [Q9R1M5-5]
DR UCSC; uc012fev.2; mouse. [Q9R1M5-6]
DR CTD; 126206; -.
DR MGI; MGI:1345193; Nlrp5.
DR VEuPathDB; HostDB:ENSMUSG00000015721; -.
DR eggNOG; ENOG502SBIG; Eukaryota.
DR GeneTree; ENSGT00940000162898; -.
DR HOGENOM; CLU_002274_2_1_1; -.
DR InParanoid; Q9R1M5; -.
DR OMA; HEHYKES; -.
DR OrthoDB; 114368at2759; -.
DR PhylomeDB; Q9R1M5; -.
DR BioGRID-ORCS; 23968; 0 hits in 58 CRISPR screens.
DR ChiTaRS; Nlrp5; mouse.
DR PRO; PR:Q9R1M5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9R1M5; protein.
DR Bgee; ENSMUSG00000015721; Expressed in primary oocyte and 11 other tissues.
DR Genevisible; Q9R1M5; MM.
DR GO; GO:0045179; C:apical cortex; IDA:MGI.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0060473; C:cortical granule; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:1990917; C:ooplasm; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0106333; C:subcortical maternal complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0060471; P:cortical granule exocytosis; IMP:UniProtKB.
DR GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR GO; GO:0051656; P:establishment of organelle localization; IMP:UniProtKB.
DR GO; GO:0051293; P:establishment of spindle localization; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IMP:UniProtKB.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:MGI.
DR GO; GO:0051302; P:regulation of cell division; IMP:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:0032879; P:regulation of localization; IMP:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR GO; GO:0043487; P:regulation of RNA stability; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR041267; NLRP_HD2.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13516; LRR_6; 4.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17776; NLRC4_HD2; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; Leucine-rich repeat; Mitochondrion; Nucleotide-binding;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1163
FT /note="NACHT, LRR and PYD domains-containing protein 5"
FT /id="PRO_0000080891"
FT DOMAIN 243..565
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT REPEAT 801..822
FT /note="LRR 1"
FT REPEAT 830..851
FT /note="LRR 2"
FT REPEAT 858..878
FT /note="LRR 3"
FT REPEAT 887..906
FT /note="LRR 4"
FT REPEAT 915..935
FT /note="LRR 5"
FT REPEAT 944..964
FT /note="LRR 6"
FT REPEAT 972..993
FT /note="LRR 7"
FT REPEAT 1001..1022
FT /note="LRR 8"
FT REPEAT 1029..1050
FT /note="LRR 9"
FT REPEAT 1058..1079
FT /note="LRR 10"
FT REPEAT 1086..1107
FT /note="LRR 11"
FT REGION 1..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 249..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT VAR_SEQ 1..104
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12133995"
FT /id="VSP_024726"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 3, isoform 5, isoform 6, isoform
FT 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:10433232,
FT ECO:0000303|PubMed:12133995, ECO:0000303|PubMed:15481533,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_024727"
FT VAR_SEQ 25..74
FT /note="RKMTSPENDSKSIQKDQGPEQEQTSESTMGPPEKESKAILKARGLEEEQK
FT -> STMSPSENVSRAILKDSGSEEVEQA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12133995"
FT /id="VSP_024728"
FT VAR_SEQ 181..196
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15481533"
FT /id="VSP_024729"
FT VAR_SEQ 780..1163
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:15481533"
FT /id="VSP_024730"
FT VAR_SEQ 1037..1041
FT /note="NNALG -> WGHVS (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15481533"
FT /id="VSP_024731"
FT VAR_SEQ 1042..1163
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15481533"
FT /id="VSP_024732"
FT VAR_SEQ 1065..1090
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15481533"
FT /id="VSP_024733"
FT VARIANT 59
FT /note="E -> D (in strain: 129/Sv and CBA/J)"
FT /evidence="ECO:0000269|PubMed:10754103"
FT VARIANT 94
FT /note="G -> L (in strain: 129/Sv; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:10754103"
FT VARIANT 139
FT /note="R -> K (in strain: 129/Sv and CBA/J)"
FT /evidence="ECO:0000269|PubMed:10754103"
FT VARIANT 283
FT /note="V -> G (in strain: A/J)"
FT VARIANT 308
FT /note="L -> P (in strain: 129/Sv and CBA/J)"
FT /evidence="ECO:0000269|PubMed:10754103"
FT VARIANT 341
FT /note="S -> T (in strain: A/J)"
FT VARIANT 1029
FT /note="H -> Q (in strain: 129/Sv and CBA/J)"
FT /evidence="ECO:0000269|PubMed:10754103"
FT VARIANT 1055..1056
FT /note="SS -> NN (in strain: 129/Sv and CBA/J)"
FT CONFLICT 567
FT /note="E -> G (in Ref. 5; AAH53384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1163 AA; 131318 MW; EF14379B454E9376 CRC64;
MGPPEKESKA ILKARGLEEE QKSERKMTSP ENDSKSIQKD QGPEQEQTSE STMGPPEKES
KAILKARGLE EEQKSERKMT SPENDSKSIQ KDQGPEQEQT SESTMGPPEK DSKAILKARG
LEEEQKSEST MSPSENVSRA ILKDSGSEEV EQASERKMTS PENDSKSIQK DQGPEQEQTS
ETLQSKEEDE VTEADKDNGG DLQDYKAHVI AKFDTSVDLH YDSPEMKLLS DAFKPYQKTF
QPHTIILHGR PGVGKSALAR SIVLGWAQGK LFQKMSFVIF FSVREIKWTE KSSLAQLIAK
ECPDSWDLVT KIMSQPERLL FVIDGLDDMD SVLQHDDMTL SRDWKDEQPI YILMYSLLRK
ALLPQSFLII TTRNTGLEKL KSMVVSPLYI LVEGLSASRR SQLVLENISN ESDRIQVFHS
LIENHQLFDQ CQAPSVCSLV CEALQLQKKL GKRCTLPCQT LTGLYATLVF HQLTLKRPSQ
SALSQEEQIT LVGLCMMAAE GVWTMRSVFY DDDLKNYSLK ESEILALFHM NILLQVGHNS
EQCYVFSHLS LQDFFAALYY VLEGLEEWNQ HFCFIENQRS IMEVKRTDDT RLLGMKRFLF
GLMNKDILKT LEVLFEYPVI PTVEQKLQHW VSLIAQQVNG TSPMDTLDAF YCLFESQDEE
FVGGALKRFQ EVWLLINQKM DLKVSSYCLK HCQNLKAIRV DIRDLLSVDN TLELCPVVTV
QETQCKPLLM EWWGNFCSVL GSLRNLKELD LGDSILSQRA MKILCLELRN QSCRIQKLTF
KSAEVVSGLK HLWKLLFSNQ NLKYLNLGNT PMKDDDMKLA CEALKHPKCS VETLRLDSCE
LTIIGYEMIS TLLISTTRLK CLSLAKNRVG VKSMISLGNA LSSSMCLLQK LILDNCGLTP
ASCHLLVSAL FSNQNLTHLC LSNNSLGTEG VQQLCQFLRN PECALQRLIL NHCNIVDDAY
GFLAMRLANN TKLTHLSLTM NPVGDGAMKL LCEALKEPTC YLQELELVDC QLTQNCCEDL
ACMITTTKHL KSLDLGNNAL GDKGVITLCE GLKQSSSSLR RLGLGACKLT SNCCEALSLA
ISCNPHLNSL NLVKNDFSTS GMLKLCSAFQ CPVSNLGIIG LWKQEYYARV RRQLEEVEFV
KPHVVIDGDW YASDEDDRNW WKN
