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   24-JAN-2024, entry version 153.
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; 10090-ENSMUSP00000101857; -.
DR   ProteomicsDB; 265333; -.
DR   Antibodypedia; 19763; 258 antibodies from 31 providers.
DR   Ensembl; ENSMUST00000053245.7; ENSMUSP00000053665.7; ENSMUSG00000013483.15.
DR   Ensembl; ENSMUST00000106250.8; ENSMUSP00000101857.2; ENSMUSG00000013483.15.
DR   GeneID; 170720; -.
DR   KEGG; mmu:170720; -.
DR   UCSC; uc007mqk.1; mouse.
DR   AGR; MGI:2386258; -.
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; 4213113at2759; -.
DR   PhylomeDB; Q99KF0; -.
DR   TreeFam; TF315606; -.
DR   BioGRID-ORCS; 170720; 7 hits in 78 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 cell types or tissues.
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   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 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   PANTHER; PTHR14559; CASPASE RECRUITMENT DOMAIN FAMILY; 1.
DR   PANTHER; PTHR14559:SF1; CASPASE RECRUITMENT DOMAIN-CONTAINING PROTEIN 14; 1.
DR   Pfam; PF00619; CARD; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50209; CARD; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   Genevisible; Q99KF0; MM.
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
//