CAR10_MOUSE
ID CAR10_MOUSE Reviewed; 1021 AA.
AC P58660;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Caspase recruitment domain-containing protein 10;
DE AltName: Full=Bcl10-interacting MAGUK protein 1;
DE Short=Bimp1;
GN Name=Card10; Synonyms=Bimp1;
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].
RX PubMed=11387339; DOI=10.1074/jbc.m103824200;
RA McAllister-Lucas L.M., Inohara N., Lucas P.C., Ruland J., Benito A., Li Q.,
RA Chen S., Chen F.F., Yamaoka S., Verma I.M., Mak T.W., Nunez G.;
RT "Bimp1, a MAGUK family member linking protein kinase C activation to Bcl10-
RT mediated NF-kappa B induction.";
RL J. Biol. Chem. 276:30589-30597(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, INTERACTION WITH BCL10 AND MALT1, AND DISRUPTION PHENOTYPE.
RX PubMed=28717989; DOI=10.1007/s13238-017-0441-3;
RA Zhang S., Pan D., Jia X.M., Lin X., Zhao X.;
RT "The CARMA3-BCL10-MALT1 (CBM) complex contributes to DNA damage-induced NF-
RT kappaB activation and cell survival.";
RL Protein Cell 8:856-860(2017).
CC -!- FUNCTION: Scaffold protein that plays an important role in mediating
CC the activation of NF-kappa-B via BCL10 or EGFR.
CC {ECO:0000269|PubMed:28717989}.
CC -!- SUBUNIT: CARD10 and BCL10 bind to each other by CARD-CARD interaction.
CC They both participate in a complex with MALT1, where MALT1 binds to
CC BCL10 (PubMed:28717989). Interacts with TMEM43; this interaction is
CC essential for EGFR-mediated NF-kappa-B activation (By similarity).
CC {ECO:0000250|UniProtKB:Q9BWT7, ECO:0000269|PubMed:28717989}.
CC -!- INTERACTION:
CC P58660; Q8BWG8: Arrb1; NbExp=4; IntAct=EBI-8344379, EBI-641778;
CC P58660; Q91YI4: Arrb2; NbExp=7; IntAct=EBI-8344379, EBI-994161;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, heart followed by
CC brain, lung, liver, skeletal muscle and testis.
CC -!- DISRUPTION PHENOTYPE: Deletion mice show impaired tissue repairing. In
CC addition, more infiltration of inflammatory cells was found in deletion
CC mice compared with control mice. {ECO:0000269|PubMed:28717989}.
CC -!- CAUTION: Supposed to contain a SH3, a PDZ and a guanylate kinase-like
CC domain. But none of these 3 domains are detected by PROSITE, Pfam or
CC SMART. {ECO:0000305}.
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DR EMBL; AF363456; AAK60136.1; -; mRNA.
DR EMBL; BC060203; AAH60203.1; -; mRNA.
DR RefSeq; NP_570929.2; NM_130859.2.
DR AlphaFoldDB; P58660; -.
DR SMR; P58660; -.
DR BioGRID; 222934; 2.
DR DIP; DIP-60780N; -.
DR IntAct; P58660; 3.
DR STRING; 10090.ENSMUSP00000129513; -.
DR iPTMnet; P58660; -.
DR PhosphoSitePlus; P58660; -.
DR MaxQB; P58660; -.
DR PaxDb; P58660; -.
DR PRIDE; P58660; -.
DR ProteomicsDB; 265332; -.
DR Antibodypedia; 25967; 241 antibodies from 29 providers.
DR Ensembl; ENSMUST00000170584; ENSMUSP00000131003; ENSMUSG00000033170.
DR GeneID; 105844; -.
DR KEGG; mmu:105844; -.
DR UCSC; uc007wrj.1; mouse.
DR CTD; 29775; -.
DR MGI; MGI:2146012; Card10.
DR VEuPathDB; HostDB:ENSMUSG00000033170; -.
DR eggNOG; KOG0708; Eukaryota.
DR GeneTree; ENSGT00940000157763; -.
DR HOGENOM; CLU_009760_1_0_1; -.
DR InParanoid; P58660; -.
DR OMA; WWTEPST; -.
DR OrthoDB; 115953at2759; -.
DR PhylomeDB; P58660; -.
DR BioGRID-ORCS; 105844; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Card10; mouse.
DR PRO; PR:P58660; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P58660; protein.
DR Bgee; ENSMUSG00000033170; Expressed in dorsomedial nucleus of hypothalamus and 225 other tissues.
DR ExpressionAtlas; P58660; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0050700; F:CARD domain binding; IBA:GO_Central.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISS:UniProtKB.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd08807; CARD_CARD10_CARMA3; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR042140; CARD_CARD10.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00619; CARD; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50209; CARD; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..1021
FT /note="Caspase recruitment domain-containing protein 10"
FT /id="PRO_0000144085"
FT DOMAIN 23..115
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 138..450
FT /evidence="ECO:0000255"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1021 AA; 114414 MW; 4811A09BDB8F792C CRC64;
MQGRADAGEA DEEAGAGSGS EAEEDALWER IEGVRHRLTR ALNPAKLTPY LRQCRVLDEQ
DEEEVLSTYR FPCRANRTGR LIDILRCRGK RGFEAFLEAL EFYYPEHFTL LTGQEPAQRC
SMILDEEGPE GLTQFLMTEV RRLREARKSQ LHREQQLQAR GRALEEERAG LEQRLREQQQ
AQERCQRLRE DWEAGSLELL RLKDENYMIA MRLAQLSEEK NSAVLRSRDL QLAVDQLKLK
VSRLEEECAL LRRARGPPPG AEEKEREPDG ADLLSELRAE NQRLTASLQE LQEGLQQEMS
RPGAAGSERI LLDILEHDWR EAQDSRQELC QKLHAVQGEL QWAEELRDKY LQEMEDLRLK
HRTLLKDCDL YKHRMATVLA QLEEIEKERD QAIQSRDRIQ LQYSQSLIEK DQYRKQVRGL
EAERDELLTT VTSLEGTKAM LEAQLQRTQG GSCLKACASS HSLCSNLSST WSLSEFPSPL
GGPEATGEAG GSEPHTSEEA TDSEKEINRL SILPFPPSAG SILRRQREED PEPPKRSFSS
MSDITGSVTL KPWSPGLSSS SSSDSVWPLG KPEGLLARGC GLDFLNRSLA IRVSGWSPPA
GLDPQDKSPD SMPGLGDRWS GAVVRRVLSG PGSARTEQKE PRAEGTGLEG AGLEAEAQQR
TLPWNQSSTL PFLLDSKACH SFHEALDAWA KGPGAEPFYI RANFSLPERS DPHALCVKAQ
EILRLVDPAH KRRQEWFCTR VDTLTLRDLD RGTVPNYQRA QQLLEVQEKY LISSRHRSPR
SNLKKRALGL VRPKPAGGTA GDSAEQLPAE PCSELERSLK PYSLVRPLLV SALRPVVLLP
ECLAPRLIRN LLDLPSSRLD FQVCPAESLS GEEQCTSSAP GAPKAWPATA GLGSRIRAIQ
ESVGKKHCLL ELGARGVREL VHSEVYPIVI HVEVTEKNVR EIRGLLGRPG WRDSELLRQC
RGSEQWLWGL PCSWVQVPAH AWGHAEELAK VVRGRILQEQ ARLVWVERGS SRGGSGSSSE
A
