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Caspase recruitment domain-containing protein 16 (Caspase recruitment domain-only protein 1) (CARD-only protein 1) (Caspase-1 inhibitor COP) (Pseudo interleukin-1 beta converting enzyme) (Pseudo-ICE) (Pseudo-IL1B-converting enzyme)

 CAR16_HUMAN             Reviewed;         197 AA.
Q5EG05; Q96RJ9;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
05-DEC-2018, entry version 107.
RecName: Full=Caspase recruitment domain-containing protein 16;
AltName: Full=Caspase recruitment domain-only protein 1;
Short=CARD-only protein 1;
AltName: Full=Caspase-1 inhibitor COP;
AltName: Full=Pseudo interleukin-1 beta converting enzyme;
Short=Pseudo-ICE;
Short=Pseudo-IL1B-converting enzyme;
Name=CARD16; Synonyms=COP, COP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
AND INTERACTION WITH CASP1 AND RIPK2.
PubMed=11536016; DOI=10.1038/sj.cdd.4400881;
Druilhe A., Srinivasula S.M., Razmara M., Ahmad M., Alnemri E.S.;
"Regulation of IL-1beta generation by Pseudo-ICE and ICEBERG, two
dominant negative caspase recruitment domain proteins.";
Cell Death Differ. 8:649-657(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Wang P.Z., Wang F., Wang X., Wu J.;
"Novel splicing variants of some human genes.";
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, TISSUE SPECIFICITY, SUBUNIT, AND INTERACTION WITH CASP1 AND
RIPK2.
PubMed=11432859; DOI=10.1074/jbc.M101415200;
Lee S.H., Stehlik C., Reed J.C.;
"Cop, a caspase recruitment domain-containing protein and inhibitor of
caspase-1 activation processing.";
J. Biol. Chem. 276:34495-34500(2001).
[7]
INTERACTION WITH CARD8.
PubMed=11821383; DOI=10.1074/jbc.M107811200;
Razmara M., Srinivasula S.M., Wang L., Poyet J.-L., Geddes B.J.,
DiStefano P.S., Bertin J., Alnemri E.S.;
"CARD-8 protein, a new CARD family member that regulates caspase-1
activation and apoptosis.";
J. Biol. Chem. 277:13952-13958(2002).
[8]
INDUCTION.
PubMed=16354923; DOI=10.1523/JNEUROSCI.4181-05.2005;
Wang X., Wang H., Figueroa B.E., Zhang W.-H., Huo C., Guan Y.,
Zhang Y., Bruey J.-M., Reed J.C., Friedlander R.M.;
"Dysregulation of receptor interacting protein-2 and caspase
recruitment domain only protein mediates aberrant caspase-1 activation
in Huntington's disease.";
J. Neurosci. 25:11645-11654(2005).
[9]
FUNCTION, AND INTERACTION WITH CASP4.
PubMed=16920334; DOI=10.1016/j.bbadis.2006.06.015;
Wang X., Narayanan M., Bruey J.-M., Rigamonti D., Cattaneo E.,
Reed J.C., Friedlander R.M.;
"Protective role of Cop in Rip2/caspase-1/caspase-4-mediated HeLa cell
death.";
Biochim. Biophys. Acta 1762:742-754(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Caspase inhibitor. Acts as a regulator of procaspase-
1/CASP1 activation implicated in the regulation of the proteolytic
maturation of pro-interleukin-1 beta (IL1B) and its release during
inflammation. Inhibits the release of IL1B in response to LPS in
monocytes. Also induces NF-kappa-B activation during the pro-
inflammatory cytokine response. Also able to inhibit CASP1-
mediated neuronal cell death, TNF-alpha, hypoxia-, UV-, and
staurosporine-mediated cell death but not ER stress-mediated cell
death. Acts by preventing activation of caspases CASP1 and CASP4,
possibly by preventing the interaction between CASP1 and RIPK2.
{ECO:0000269|PubMed:11432859, ECO:0000269|PubMed:11536016,
ECO:0000269|PubMed:16920334}.
-!- SUBUNIT: Homooligomer. Interacts with CASP1, CASP4, CARD8 and
RIPK2. {ECO:0000269|PubMed:11432859, ECO:0000269|PubMed:11536016,
ECO:0000269|PubMed:11821383, ECO:0000269|PubMed:16920334}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q5EG05-1; Sequence=Displayed;
Name=2;
IsoId=Q5EG05-2; Sequence=VSP_035216;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
placenta, spleen, lymph node and bone marrow. Weakly or not
expressed in thymus. {ECO:0000269|PubMed:11432859,
ECO:0000269|PubMed:11536016}.
-!- INDUCTION: Down-regulated in patients suffering of Huntington
disease. {ECO:0000269|PubMed:16354923}.
-----------------------------------------------------------------------
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EMBL; AF367017; AAK71682.1; -; mRNA.
EMBL; AY885669; AAW78563.1; -; mRNA.
EMBL; AK311902; BAG34843.1; -; mRNA.
EMBL; CH471065; EAW67062.1; -; Genomic_DNA.
EMBL; BC117478; AAI17479.1; -; mRNA.
EMBL; BC117480; AAI17481.1; -; mRNA.
CCDS; CCDS31661.1; -. [Q5EG05-1]
CCDS; CCDS41705.1; -. [Q5EG05-2]
RefSeq; NP_001017534.1; NM_001017534.1. [Q5EG05-1]
RefSeq; NP_443121.1; NM_052889.2. [Q5EG05-2]
UniGene; Hs.348365; -.
ProteinModelPortal; Q5EG05; -.
SMR; Q5EG05; -.
BioGrid; 125339; 3.
IntAct; Q5EG05; 1.
MINT; Q5EG05; -.
STRING; 9606.ENSP00000364858; -.
iPTMnet; Q5EG05; -.
PhosphoSitePlus; Q5EG05; -.
BioMuta; CARD16; -.
DMDM; 74722547; -.
MaxQB; Q5EG05; -.
PaxDb; Q5EG05; -.
PeptideAtlas; Q5EG05; -.
PRIDE; Q5EG05; -.
ProteomicsDB; 62773; -.
ProteomicsDB; 62774; -. [Q5EG05-2]
Ensembl; ENST00000375704; ENSP00000364856; ENSG00000204397. [Q5EG05-2]
Ensembl; ENST00000375706; ENSP00000364858; ENSG00000204397. [Q5EG05-1]
Ensembl; ENST00000525374; ENSP00000433700; ENSG00000204397. [Q5EG05-2]
GeneID; 114769; -.
KEGG; hsa:114769; -.
UCSC; uc001pio.2; human. [Q5EG05-1]
CTD; 114769; -.
DisGeNET; 114769; -.
EuPathDB; HostDB:ENSG00000204397.7; -.
GeneCards; CARD16; -.
HGNC; HGNC:33701; CARD16.
HPA; HPA053981; -.
HPA; HPA062805; -.
MIM; 615680; gene.
neXtProt; NX_Q5EG05; -.
OpenTargets; ENSG00000204397; -.
PharmGKB; PA164717628; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000159114; -.
HOGENOM; HOG000111300; -.
HOVERGEN; HBG006113; -.
InParanoid; Q5EG05; -.
KO; K12806; -.
OMA; CITDICE; -.
OrthoDB; EOG091G0L5Y; -.
PhylomeDB; Q5EG05; -.
TreeFam; TF330675; -.
ChiTaRS; CARD16; human.
GeneWiki; COP1; -.
GenomeRNAi; 114769; -.
PRO; PR:Q5EG05; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000204397; Expressed in 171 organ(s), highest expression level in leukocyte.
CleanEx; HS_CARD16; -.
ExpressionAtlas; Q5EG05; baseline and differential.
Genevisible; Q5EG05; HS.
GO; GO:0097179; C:protease inhibitor complex; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0050700; F:CARD domain binding; IPI:UniProtKB.
GO; GO:0089720; F:caspase binding; IPI:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0071494; P:cellular response to UV-C; IDA:UniProtKB.
GO; GO:0097340; P:inhibition of cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; IDA:UniProtKB.
GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR002398; Pept_C14.
PANTHER; PTHR10454; PTHR10454; 1.
Pfam; PF00619; CARD; 1.
SMART; SM00114; CARD; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50209; CARD; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Polymorphism;
Protease inhibitor; Reference proteome; Thiol protease inhibitor.
CHAIN 1 197 Caspase recruitment domain-containing
protein 16.
/FTId=PRO_0000349180.
DOMAIN 1 91 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
VAR_SEQ 92 197 ALQAVQDNPAMPTCSSPEGRIKLCFLEDAQRIWKQKLQRCH
VQNTIIKWSERYTSGSFEMQWLFLRTNFIERFWRNILLLPL
HKGSLYPRIPGLGKELQTGTHKLS -> GPIPGN (in
isoform 2). {ECO:0000303|PubMed:11536016,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_035216.
VARIANT 33 33 R -> S (in dbSNP:rs35966314).
/FTId=VAR_046279.
VARIANT 37 37 Q -> K (in dbSNP:rs1042744).
/FTId=VAR_046280.
VARIANT 56 56 A -> D (in dbSNP:rs34534919).
/FTId=VAR_046281.
VARIANT 167 167 N -> I (in dbSNP:rs542571).
/FTId=VAR_046282.
SEQUENCE 197 AA; 22625 MW; 5DCAC6A9B2FAE82F CRC64;
MADKVLKEKR KLFIHSMGEG TINGLLDELL QTRVLNQEEM EKVKRENATV MDKTRALIDS
VIPKGAQACQ ICITYICEED SYLAETLGLS AALQAVQDNP AMPTCSSPEG RIKLCFLEDA
QRIWKQKLQR CHVQNTIIKW SERYTSGSFE MQWLFLRTNF IERFWRNILL LPLHKGSLYP
RIPGLGKELQ TGTHKLS


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