CAR14_MOUSE
ID CAR14_MOUSE Reviewed; 999 AA.
AC Q99KF0;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Caspase recruitment domain-containing protein 14;
DE AltName: Full=Bcl10-interacting MAGUK protein 2;
DE Short=Bimp2;
GN Name=Card14; Synonyms=Bimp2;
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=FVB/N; TISSUE=Mammary gland;
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).
CC -!- FUNCTION: Acts as a scaffolding protein that can activate the
CC inflammatory transcription factor NF-kappa-B and p38/JNK MAP kinase
CC signaling pathways. Forms a signaling complex with BCL10 and MALT1, and
CC activates MALT1 proteolytic activity and inflammatory gene expression.
CC MALT1 is indispensable for CARD14-induced activation of NF-kappa-B and
CC p38/JNK MAP kinases. May play a role in signaling mediated by TRAF2,
CC TRAF3 and TRAF6 and protects cells against apoptosis.
CC {ECO:0000250|UniProtKB:Q9BXL6}.
CC -!- SUBUNIT: Interacts (via CARD domain) with BCL10 (via CARD domain).
CC Forms a complex with MALT1 and BCL10; resulting in the formation of a
CC CBM (CARD14-BLC10-MALT1) complex. Interacts with TRAF2, TRAF3 and
CC TRAF6. {ECO:0000250|UniProtKB:Q9BXL6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BXL6}.
CC -!- DOMAIN: A linker region between the coiled-coil and PDZ region holds
CC the protein in an inactive state. {ECO:0000250|UniProtKB:Q9BXL6}.
CC -!- CAUTION: Supposed to contain a SH3 domain which is not detected by
CC PROSITE, Pfam or SMART. {ECO:0000305}.
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DR EMBL; AF363457; AAK60137.1; -; mRNA.
DR EMBL; BC004692; AAH04692.1; -; mRNA.
DR EMBL; BC029102; AAH29102.1; -; mRNA.
DR CCDS; CCDS25715.1; -.
DR RefSeq; NP_570956.1; NM_130886.3.
DR RefSeq; XP_006532439.1; XM_006532376.1.
DR AlphaFoldDB; Q99KF0; -.
DR SMR; Q99KF0; -.
DR BioGRID; 228392; 2.
DR STRING; 10090.ENSMUSP00000101857; -.
DR iPTMnet; Q99KF0; -.
DR PhosphoSitePlus; Q99KF0; -.
DR MaxQB; Q99KF0; -.
DR PaxDb; Q99KF0; -.
DR PRIDE; Q99KF0; -.
DR ProteomicsDB; 265333; -.
DR Antibodypedia; 19763; 211 antibodies from 31 providers.
DR Ensembl; ENSMUST00000053245; ENSMUSP00000053665; ENSMUSG00000013483.
DR Ensembl; ENSMUST00000106250; ENSMUSP00000101857; ENSMUSG00000013483.
DR GeneID; 170720; -.
DR KEGG; mmu:170720; -.
DR UCSC; uc007mqk.1; mouse.
DR CTD; 79092; -.
DR MGI; MGI:2386258; Card14.
DR VEuPathDB; HostDB:ENSMUSG00000013483; -.
DR eggNOG; KOG0708; Eukaryota.
DR GeneTree; ENSGT00940000160777; -.
DR HOGENOM; CLU_009760_0_0_1; -.
DR InParanoid; Q99KF0; -.
DR OMA; VVWTEQN; -.
DR OrthoDB; 115953at2759; -.
DR PhylomeDB; Q99KF0; -.
DR TreeFam; TF315606; -.
DR BioGRID-ORCS; 170720; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Card14; mouse.
DR PRO; PR:Q99KF0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99KF0; protein.
DR Bgee; ENSMUSG00000013483; Expressed in epithelium of tongue and 55 other tissues.
DR Genevisible; Q99KF0; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0050700; F:CARD domain binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00619; CARD; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..999
FT /note="Caspase recruitment domain-containing protein 14"
FT /id="PRO_0000144089"
FT DOMAIN 15..107
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT DOMAIN 572..655
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 803..986
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 409..565
FT /note="Maintains the protein in an inactive state"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL6"
FT COILED 125..411
FT /evidence="ECO:0000255"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXL6"
FT CONFLICT 736..743
FT /note="QAQQQLLA -> HLLEDHRS (in Ref. 2; AAH04692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 999 AA; 113497 MW; D18350DA12430255 CRC64;
MAELCRMDST LTALDEEMLW DMLESHRCRI VQSICPSRLT PYLRQAKVLG QLDEEEILHS
SRFTNSAMRV GHLLDLLKAR GKNGAIAFLE SLKFHNPDVY TLVTGLQSDI DFSTFSGLME
TSKLTECLAG AISSLQEELA QEKAQKEVLL RRCQQLKERL GLAEAHAEGL RQLEVDHSRM
KREVSTHFHE VLKLKDEMLN LSLHYSNALR EKELAATRCH SLQEELYLVK QELQRASLVS
SCERESRERS LKMASNLEPQ GEELNRLKEE NEKLRSMTFS LVEKDILEQS LDEARESKQE
LVDRIHSLRE RAVAAERQQK QYWEEKEQTL LQFRKTQVDC ELYKEKMTML QGQVAELQKE
RDQAYTARDR AQMEISQRLV EKDALRRRVF ELTEQVCELR TQLRRLQAEA PGGPKQEAGA
RELCLRGKQR LVRMHAVCPP DDSDCSLLSS TESRLWWDLN STSSREQMDS FRSSSPMPPS
QQSLYKRVAE DFLEDPESLS FPEVLEMRLQ GATVDDTDTD LEFEMIDGAD LSQTEDSLQG
SSRSLNVSES SVPVRRRPAR KILSQVTVLA FQGDALLEQI GVIGGNLTGI FIHRVTPGSA
ADEMALRPGT QIMMVDYKPT KPSLRATLEN TTLEQAVGLL RRVNGSCYLS VKINTEGYKN
LIQDLDAKVV TSGDSFYIRV NLAMQRGGDG ELQTHCNDIL HVTDTMFQGR SCWHAHHVNP
YTMKDMEPGT IPNYSQAQQQ LLALIQDMTQ RCTVPRKPPG GPQKLVRIVS VDKAAVSPLT
SSFDQSQWDS GKEEGGPSVC FWSESCFTLA PYTLVHPHRP ARPRPVLFVP RLVGRILGKK
LCLLQGFKQC SAEYLSQEEY ATWSQRGDII QEGESIGDHH WITRHAVESL MNMSTHALLD
VRLDSVRVLH RMDMFPIIIH VSVNEKTAKK LRKGLHRLGS SEEQFLEVAR QEEGELDRVP
CLYSSLAPDS WSDLDSLLSC VRLAIADEQK KVVWTESPC
