NALP5_BOVIN
ID NALP5_BOVIN Reviewed; 1098 AA.
AC Q647I9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=NACHT, LRR and PYD domains-containing protein 5;
DE AltName: Full=Mater protein homolog;
GN Name=NLRP5; Synonyms=MATER, NALP5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15189828; DOI=10.1095/biolreprod.104.030288;
RA Pennetier S., Uzbekova S., Perreau C., Papillier P., Mermillod P.,
RA Dalbies-Tran R.;
RT "Spatio-temporal expression of the germ cell marker genes MATER, ZAR1,
RT GDF9, BMP15, and VASA in adult bovine tissues, oocytes, and preimplantation
RT embryos.";
RL Biol. Reprod. 71:1359-1366(2004).
RN [2]
RP TISSUE SPECIFICITY.
RC TISSUE=Oocyte;
RX PubMed=16339045; DOI=10.1095/biolreprod.105.045096;
RA Ponsuksili S., Brunner R.M., Goldammer T., Kuhn C., Walz C., Chomdej S.,
RA Tesfaye D., Schellander K., Wimmers K., Schwerin M.;
RT "Bovine NALP5, NALP8, and NALP9 genes: assignment to a QTL region and the
RT expression in adult tissues, oocytes, and preimplantation embryos.";
RL Biol. Reprod. 74:577-584(2006).
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 (By similarity).
CC Required for the formation of F-actin cytoplasmic lattices (CPL) in
CC oocytes, which in turn are responsible for symmetric division of
CC zygotes via the regulation of mitotic spindle formation and positioning
CC (By similarity). Required for the localization of cortical granules to
CC the cortex of oocytes, via association with the cortical actin scaffold
CC (By similarity). Required for cortical actin clearance prior to oocyte
CC exocytosis (By similarity). Involved in regulating post-fertilization
CC Ca(2+) release and endoplasmic reticulum (ER) storage via regulation of
CC ER cellular localization (By similarity). May be involved in the
CC localization of mitochondria to the cytoplasm and perinuclear region in
CC oocytes and early stage embryos, independent of its role in CPL
CC formation (By similarity). {ECO:0000250|UniProtKB:Q9R1M5}.
CC -!- SUBUNIT: Component of the subcortical maternal complex (SCMC), at least
CC composed of NLRP5, KHDC3, OOEP, and TLE6 (By similarity). Within the
CC complex, interacts with OOEP, KHDC3 and TLE6 (By similarity). The SCMC
CC may facilitate translocation of its components between the nuclear and
CC cytoplasmic compartments (By similarity). As part of the SCMC interacts
CC with the SCMC-associated protein ZBED3 (By similarity). As part of the
CC SCMC interacts with the SCMC-associated protein CFL1/Cofilin-1 (By
CC similarity). Interacts with PRKCE (By similarity). Interacts with TUBB3
CC at cytoskeleton microtubules (By similarity).
CC {ECO:0000250|UniProtKB:P59047, ECO:0000250|UniProtKB:Q9R1M5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, Cortical
CC granule {ECO:0000250|UniProtKB:P59047}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9R1M5}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9R1M5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9R1M5}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P59047}.
CC -!- TISSUE SPECIFICITY: Oocyte-specific. {ECO:0000269|PubMed:15189828,
CC ECO:0000269|PubMed:16339045}.
CC -!- PTM: Phosphorylated by PRKCE. {ECO:0000250|UniProtKB:P59047}.
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; AY721594; AAU20764.1; -; mRNA.
DR RefSeq; NP_001007815.1; NM_001007814.2.
DR AlphaFoldDB; Q647I9; -.
DR SMR; Q647I9; -.
DR STRING; 9913.ENSBTAP00000017623; -.
DR PaxDb; Q647I9; -.
DR PRIDE; Q647I9; -.
DR GeneID; 493717; -.
DR KEGG; bta:493717; -.
DR CTD; 126206; -.
DR eggNOG; ENOG502SBIG; Eukaryota.
DR InParanoid; Q647I9; -.
DR OrthoDB; 114368at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005938; C:cell cortex; IDA:AgBase.
DR GO; GO:0060473; C:cortical granule; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0042585; C:germinal vesicle; IDA:AgBase.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0060471; P:cortical granule exocytosis; ISS:UniProtKB.
DR GO; GO:0051656; P:establishment of organelle localization; ISS:UniProtKB.
DR GO; GO:0051293; P:establishment of spindle localization; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; ISS:UniProtKB.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
DR GO; GO:0032879; P:regulation of localization; ISS:UniProtKB.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 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; IPR007111; NACHT_NTPase.
DR InterPro; IPR041267; NLRP_HD2.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
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; SM01289; PYRIN; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus;
KW Leucine-rich repeat; Mitochondrion; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..1098
FT /note="NACHT, LRR and PYD domains-containing protein 5"
FT /id="PRO_0000286969"
FT DOMAIN 1..97
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT DOMAIN 180..503
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT REPEAT 851..871
FT /note="LRR 1"
FT REPEAT 880..900
FT /note="LRR 2"
FT REPEAT 908..928
FT /note="LRR 3"
FT REPEAT 937..958
FT /note="LRR 4"
FT REPEAT 965..985
FT /note="LRR 5"
FT REPEAT 993..1013
FT /note="LRR 6"
FT REPEAT 1021..1041
FT /note="LRR 7"
FT REGION 104..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 186..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
SQ SEQUENCE 1098 AA; 120994 MW; BA6326C0CA65001E CRC64;
MREAKIAPLS NYGLQWCFEQ LGKEEFQTFK ALLKEHASES AACSFPLVQV DRADAESLAS
LLHEHCRASL AWKTSTDIFE KMSLSALSEM ARDEMKKYLL AEISEDSAPT KTDQGPSMKE
VPGPREDPQD SRDYRIHVMT TFSTRLDTPQ RFEEFASECP DAHALSGAFN PDPSGGFRPL
TVVLHGPPGV GKSSLARRLL LFWAQGDLYK GLFSYVFLLR ARDLQGSRET SFAELISKEW
PDAPVPVEKV LSQPERLLIV VDGLEELELT FRDQDSSLLA DWAERQPAPV LAHSLLKKVL
LPECALLLTV QDAGLQRLQA LLRSPRYLWV GGLSVENRMQ LLLGGGKHCR RKTCAWHAGA
DHQEVLDKCQ VPVVCALVRE ALELQGEPGK GLPVPGHTLT GLYATFVFQR LAPKDAGWRA
LSGEERGALK GLCRLAADGV WNAKFVFDGD DLGVHGLQGP ELSALQQASI LLPDGHCGRG
HAFSHLSLQE FFAALFYVLR GVEGDGEGYP LFPQSTKSLT ELRHIDLNVQ LVQMKRFLFG
LVSKEVMRAL ETLLGCPVRP VAKQQLLHWI CLVGQHPAAA ASPDLLEAFY CLFEAQDDEF
VRLALNGFQE VWLQLNRPMD LTVSSFCLRR CQHLRKVRLD VRGTPKDEFA EAWSGAPQGL
KIKTLDEHWE DLCSVLSTHP NLRQLDLSGS VLSKEAMKTL CVKLRQPACK IQNLIFKGAR
VTPGLRHLWM TLIINRNITR LDLTGCRLRE EDVQTACEAL RHPQCALESL RLDRCGLTPA
SCREISQVLA TSGSLKSLSL TGNKVADQGV KSLCDALKVT PCTLQKLILG SCGLTAATCQ
DLASALIENQ GLTHLSLSGD ELGSKGMSLL CRAVKLSSCG LQKLALNACS LDVAGCGFLA
FALMGNRHLT HLSLSMNPLE DPGMNLLCEV MMEPSCPLRD LDLVNCRLTA SCCKSLSNVI
TRSPRLRSLD LAANALGDEG IAALCEGLKQ KNTLTRLGLE ACGLTSEGCK ALSAALTCSR
HLASLNLMRN DLGPRGMTTL CSAFMHPTSN LQTIGLWKEQ YPARVRRLLE QVQRLKPHVV
ISDAWYTEEE EDGPCWRI
