PYDC5_HUMAN
ID PYDC5_HUMAN Reviewed; 113 AA.
AC W6CW81;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Pyrin domain-containing protein 5 {ECO:0000305};
DE AltName: Full=Pyrin domain-only protein 3 {ECO:0000303|PubMed:24531343};
GN Name=PYDC5 {ECO:0000312|HGNC:HGNC:53781};
GN Synonyms=POP3 {ECO:0000303|PubMed:24531343};
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], TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH
RP AIM2; IFI16 AND NLRP3, AND FUNCTION.
RX PubMed=24531343; DOI=10.1038/ni.2829;
RA Khare S., Ratsimandresy R.A., de Almeida L., Cuda C.M., Rellick S.L.,
RA Misharin A.V., Wallin M.C., Gangopadhyay A., Forte E., Gottwein E.,
RA Perlman H., Reed J.C., Greaves D.R., Dorfleutner A., Stehlik C.;
RT "The PYRIN domain-only protein POP3 inhibits ALR inflammasomes and
RT regulates responses to infection with DNA viruses.";
RL Nat. Immunol. 15:343-353(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
CC -!- FUNCTION: Functions as an inhibitor of DNA virus-induced activation of
CC AIM2-like receptors (ALR) inflammasome through interaction with AIM2.
CC {ECO:0000269|PubMed:24531343}.
CC -!- SUBUNIT: Interacts with AIM2; disrupts assembly of the ALR inflammasome
CC complex (PubMed:24531343). Interacts with IFI16 (PubMed:24531343).
CC Interacts with NLRP3 (PubMed:24531343). {ECO:0000269|PubMed:24531343}.
CC -!- TISSUE SPECIFICITY: Expressed in monocytic cell lines and primary
CC macrophages but not in B or T cells. {ECO:0000269|PubMed:24531343}.
CC -!- INDUCTION: Up-regulated in response to IFNB1 or virus infection.
CC {ECO:0000269|PubMed:24531343}.
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DR EMBL; KF562078; AHI87498.1; -; mRNA.
DR EMBL; AL359753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001306939.1; NM_001320010.1.
DR AlphaFoldDB; W6CW81; -.
DR SMR; W6CW81; -.
DR PRIDE; W6CW81; -.
DR DNASU; 107181291; -.
DR GeneID; 107181291; -.
DR KEGG; hsa:107181291; -.
DR CTD; 107181291; -.
DR DisGeNET; 107181291; -.
DR GeneCards; PYDC5; -.
DR HGNC; HGNC:53781; PYDC5.
DR neXtProt; NX_W6CW81; -.
DR OrthoDB; 1304994at2759; -.
DR Pharos; W6CW81; Tbio.
DR PRO; PR:W6CW81; -.
DR Proteomes; UP000005640; Unplaced.
DR GO; GO:0097169; C:AIM2 inflammasome complex; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0002218; P:activation of innate immune response; IBA:GO_Central.
DR GO; GO:0035458; P:cellular response to interferon-beta; IDA:UniProtKB.
DR GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:UniProtKB.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR040205; HIN-200.
DR PANTHER; PTHR12200; PTHR12200; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50824; DAPIN; 1.
PE 1: Evidence at protein level;
KW Inflammatory response; Reference proteome.
FT CHAIN 1..113
FT /note="Pyrin domain-containing protein 5"
FT /id="PRO_0000445598"
FT DOMAIN 1..52
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
SQ SEQUENCE 113 AA; 12732 MW; 9DE02DE80B8A1840 CRC64;
MESKYKEILL LTSLDNITDE ELDRFKCFLP DEFNIATGKL HTLNSTSSQL DLKRWHGVCS
EEDRIFQKLN YMLVAKCLRE EQETGICGSP SSARSVSQSR LGLSFHGISG NAC
