PYDC1_HUMAN
ID PYDC1_HUMAN Reviewed; 89 AA.
AC Q8WXC3; B2R8L4; Q8NFP8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Pyrin domain-containing protein 1 {ECO:0000305};
DE AltName: Full=PAAD-only protein 1 {ECO:0000303|PubMed:12656673};
DE AltName: Full=Pyrin-only protein 1 {ECO:0000303|PubMed:12656673};
DE AltName: Full=cellular POP1 {ECO:0000303|PubMed:17178784};
DE Short=cPOP1 {ECO:0000303|PubMed:17178784};
GN Name=PYDC1 {ECO:0000312|HGNC:HGNC:30261};
GN Synonyms=ASC2 {ECO:0000303|PubMed:12656673}, ASCI,
GN POP1 {ECO:0000303|PubMed:12656673}, PYC1 {ECO:0000312|EMBL:AAN03745.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11786556; DOI=10.1074/jbc.m112208200;
RA Manji G.A., Wang L., Geddes B.J., Brown M., Merriam S., Al-Garawi A.,
RA Mak S., Lora J.M., Briskin M., Jurman M., Cao J., DiStefano P.S.,
RA Bertin J.;
RT "PYPAF1: a PYRIN-containing APAF1-like protein that assembles with ASC and
RT activates NF-kB.";
RL J. Biol. Chem. 277:11570-11575(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, PHOSPHORYLATION, AND INTERACTION WITH PYCARD/ASC.
RC TISSUE=Heart;
RX PubMed=12656673; DOI=10.1042/bj20030304;
RA Stehlik C., Krajewska M., Welsh K., Krajewski S., Godzik A., Reed J.C.;
RT "The PAAD/PYRIN-only protein POP1/ASC2 is a modulator of ASC-mediated
RT nuclear-factor-kappa B and pro-caspase-1 regulation.";
RL Biochem. J. 373:101-113(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Martinon F., Hofmann K., Tschopp J.;
RT "Pyc1 a novel regulator of the inflammasome.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP INTERACTION WITH PYCARD, AND SUBCELLULAR LOCATION.
RX PubMed=17178784; DOI=10.1128/iai.01315-06;
RA Dorfleutner A., Bryan N.B., Talbott S.J., Funya K.N., Rellick S.L.,
RA Reed J.C., Shi X., Rojanasakul Y., Flynn D.C., Stehlik C.;
RT "Cellular pyrin domain-only protein 2 is a candidate regulator of
RT inflammasome activation.";
RL Infect. Immun. 75:1484-1492(2007).
RN [8]
RP FUNCTION.
RX PubMed=24871464; DOI=10.1038/gene.2014.30;
RA Porter K.A., Duffy E.B., Nyland P., Atianand M.K., Sharifi H., Harton J.A.;
RT "The CLRX.1/NOD24 (NLRP2P) pseudogene codes a functional negative regulator
RT of NF-kappaB, pyrin-only protein 4.";
RL Genes Immun. 15:392-403(2014).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=16905547; DOI=10.1074/jbc.m605458200;
RA Natarajan A., Ghose R., Hill J.M.;
RT "Structure and dynamics of ASC2, a pyrin domain-only protein that regulates
RT inflammatory signaling.";
RL J. Biol. Chem. 281:31863-31875(2006).
CC -!- FUNCTION: Associates with PYCARD/ASC and modulates its ability to
CC collaborate with MEFV/pyrin and NLRP3/cryopyrin in NF-kappa-B and pro-
CC caspase-1 activation. Suppresses kinase activity of NF-kappa-B
CC inhibitor kinase (IKK) complex, expression of NF-kappa-B inducible
CC genes and inhibits NF-kappa-B activation by cytokines and LPS.
CC {ECO:0000269|PubMed:12656673, ECO:0000269|PubMed:24871464}.
CC -!- SUBUNIT: Interacts with PYCARD/ASC (via pyrin domain).
CC {ECO:0000269|PubMed:12656673, ECO:0000269|PubMed:17178784}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12656673}.
CC Note=Recruited to specks formed by PYCARD within the cytoplasm.
CC {ECO:0000269|PubMed:17178784}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in monocytes, macrophages
CC and granulocytes. {ECO:0000269|PubMed:12656673}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:12656673}.
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DR EMBL; AF454669; AAL58439.1; -; mRNA.
DR EMBL; AY163727; AAO23114.1; -; mRNA.
DR EMBL; AF467809; AAN03745.1; -; mRNA.
DR EMBL; AK313418; BAG36211.1; -; mRNA.
DR EMBL; CH471192; EAW52147.1; -; Genomic_DNA.
DR EMBL; BC105033; AAI05034.1; -; mRNA.
DR EMBL; BC105035; AAI05036.1; -; mRNA.
DR CCDS; CCDS10710.1; -.
DR RefSeq; NP_690865.1; NM_152901.3.
DR PDB; 2HM2; NMR; -; Q=1-89.
DR PDB; 4QOB; X-ray; 2.70 A; A/B=1-89.
DR PDBsum; 2HM2; -.
DR PDBsum; 4QOB; -.
DR AlphaFoldDB; Q8WXC3; -.
DR SMR; Q8WXC3; -.
DR BioGRID; 129281; 2.
DR IntAct; Q8WXC3; 1.
DR STRING; 9606.ENSP00000304336; -.
DR BioMuta; PYDC1; -.
DR DMDM; 74730989; -.
DR EPD; Q8WXC3; -.
DR MassIVE; Q8WXC3; -.
DR PaxDb; Q8WXC3; -.
DR PeptideAtlas; Q8WXC3; -.
DR PRIDE; Q8WXC3; -.
DR ProteomicsDB; 75005; -.
DR Antibodypedia; 27781; 168 antibodies from 16 providers.
DR DNASU; 260434; -.
DR Ensembl; ENST00000302964.4; ENSP00000304336.4; ENSG00000169900.8.
DR GeneID; 260434; -.
DR KEGG; hsa:260434; -.
DR MANE-Select; ENST00000302964.4; ENSP00000304336.4; NM_152901.4; NP_690865.1.
DR UCSC; uc002ebo.4; human.
DR CTD; 260434; -.
DR DisGeNET; 260434; -.
DR GeneCards; PYDC1; -.
DR HGNC; HGNC:30261; PYDC1.
DR HPA; ENSG00000169900; Group enriched (brain, skin).
DR MIM; 615700; gene.
DR neXtProt; NX_Q8WXC3; -.
DR OpenTargets; ENSG00000169900; -.
DR PharmGKB; PA142671111; -.
DR VEuPathDB; HostDB:ENSG00000169900; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000164730; -.
DR HOGENOM; CLU_163053_0_0_1; -.
DR InParanoid; Q8WXC3; -.
DR OMA; QLVASYY; -.
DR OrthoDB; 574602at2759; -.
DR PhylomeDB; Q8WXC3; -.
DR PathwayCommons; Q8WXC3; -.
DR SignaLink; Q8WXC3; -.
DR BioGRID-ORCS; 260434; 13 hits in 1072 CRISPR screens.
DR EvolutionaryTrace; Q8WXC3; -.
DR GenomeRNAi; 260434; -.
DR Pharos; Q8WXC3; Tbio.
DR PRO; PR:Q8WXC3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8WXC3; protein.
DR Bgee; ENSG00000169900; Expressed in right hemisphere of cerebellum and 105 other tissues.
DR Genevisible; Q8WXC3; HS.
DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL.
DR GO; GO:0008385; C:IkappaB kinase complex; IDA:HGNC-UCL.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IDA:HGNC-UCL.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:HGNC-UCL.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:HGNC-UCL.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:HGNC-UCL.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IDA:HGNC-UCL.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR002398; Pept_C14.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01289; PYRIN; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50824; DAPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..89
FT /note="Pyrin domain-containing protein 1"
FT /id="PRO_0000280593"
FT DOMAIN 1..89
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT CONFLICT 37
FT /note="E -> G (in Ref. 3; AAN03745)"
FT /evidence="ECO:0000305"
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:4QOB"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:4QOB"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:4QOB"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:4QOB"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:4QOB"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:4QOB"
SQ SEQUENCE 89 AA; 10107 MW; 4CDF6D672DDDD98E CRC64;
MGTKREAILK VLENLTPEEL KKFKMKLGTV PLREGFERIP RGALGQLDIV DLTDKLVASY
YEDYAAELVV AVLRDMRMLE EAARLQRAA
