ID   CEFIP_MOUSE             Reviewed;        1412 AA.
AC   D3Z1D3;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Cardiac-enriched FHL2-interacting protein {ECO:0000303|PubMed:28717008};
GN   Name=CEFIP {ECO:0000303|PubMed:28717008};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=28717008; DOI=10.1074/jbc.m117.786764;
RA   Dierck F., Kuhn C., Rohr C., Hille S., Braune J., Sossalla S., Molt S.,
RA   van der Ven P.F.M., Fuerst D.O., Frey N.;
RT   "The novel cardiac z-disc protein CEFIP regulates cardiomyocyte hypertrophy
RT   by modulating calcineurin signaling.";
RL   J. Biol. Chem. 292:15180-15191(2017).
CC   -!- FUNCTION: Plays an important role in cardiomyocyte hypertrophy via
CC       activation of the calcineurin/NFAT signaling pathway.
CC       {ECO:0000269|PubMed:28717008}.
CC   -!- SUBUNIT: Interacts with FHL2. {ECO:0000250|UniProtKB:Q711Q0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC       {ECO:0000269|PubMed:28717008}.
CC   -!- TISSUE SPECIFICITY: Expressed in the heart and skeletal muscle (at
CC       protein level). {ECO:0000269|PubMed:28717008}.
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DR   EMBL; CT009541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS49437.1; -.
DR   RefSeq; NP_001182026.1; NM_001195097.1.
DR   RefSeq; XP_006518377.1; XM_006518314.3.
DR   RefSeq; XP_006518378.1; XM_006518315.3.
DR   RefSeq; XP_006518379.1; XM_006518316.3.
DR   RefSeq; XP_006518380.1; XM_006518317.3.
DR   RefSeq; XP_006518381.1; XM_006518318.3.
DR   RefSeq; XP_006518382.1; XM_006518319.3.
DR   AlphaFoldDB; D3Z1D3; -.
DR   STRING; 10090.ENSMUSP00000093741; -.
DR   iPTMnet; D3Z1D3; -.
DR   PhosphoSitePlus; D3Z1D3; -.
DR   MaxQB; D3Z1D3; -.
DR   PaxDb; D3Z1D3; -.
DR   PRIDE; D3Z1D3; -.
DR   ProteomicsDB; 307835; -.
DR   Antibodypedia; 50031; 26 antibodies from 10 providers.
DR   Ensembl; ENSMUST00000096038; ENSMUSP00000093741; ENSMUSG00000071540.
DR   GeneID; 100504518; -.
DR   KEGG; mmu:100504518; -.
DR   UCSC; uc007szg.2; mouse.
DR   MGI; MGI:3588196; 3425401B19Rik.
DR   VEuPathDB; HostDB:ENSMUSG00000071540; -.
DR   eggNOG; ENOG502QVE3; Eukaryota.
DR   GeneTree; ENSGT00730000111333; -.
DR   HOGENOM; CLU_255771_0_0_1; -.
DR   InParanoid; D3Z1D3; -.
DR   OMA; HYSPPFN; -.
DR   OrthoDB; 416362at2759; -.
DR   PhylomeDB; D3Z1D3; -.
DR   TreeFam; TF336978; -.
DR   BioGRID-ORCS; 100504518; 1 hit in 71 CRISPR screens.
DR   PRO; PR:D3Z1D3; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; D3Z1D3; protein.
DR   Bgee; ENSMUSG00000071540; Expressed in interventricular septum and 19 other tissues.
DR   GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR   GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR   InterPro; IPR027838; DUF4585.
DR   Pfam; PF15232; DUF4585; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1412
FT                   /note="Cardiac-enriched FHL2-interacting protein"
FT                   /id="PRO_0000444578"
FT   REGION          106..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          877..923
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          935..1255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1344..1412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..175
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..485
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..650
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..697
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..798
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        905..923
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1045..1070
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1173..1197
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1344..1360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         120
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q711Q0"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q711Q0"
FT   MOD_RES         473
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q711Q0"
FT   MOD_RES         813
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q711Q0"
SQ   SEQUENCE   1412 AA;  154478 MW;  0080CC0DAB94AC93 CRC64;
     MMQGNKKCTD GFSDTSSIGS VLDEADREVS NLTDRAFRSL CISEDTSFHD SDLALSPDVT
     SQVSGTFHQE TVGHANRKSG IWSQLPSQGT EHSGWAATFQ QQPKYVQGEE KYPKTSPLPT
     PVQRRLEVPI SGLRSSSKPI SKVSSLIRSF DRTETQSCDS RPPPSKPPAL KNPPKFAHPP
     ESGVNFCFDS AFLTVRRVPA EVSNTHQGSH QSGRAPGEQE SPKNPEIASH SSDSLLRTPD
     HVAGSFEPRY PSPPLKPATA EPGRGKEWIP RRTFLHSENS AFESWDTHQP KLRERKDIAE
     TTPESKAPKH YEDMPLLKEP YPAESKGSPY QARANCAQEE NRSPSGSQST SGAWGARDPG
     SQLFPVEGNA SQIDPQVKRS KAPWRKPKTG KGGTDGPPDA LEDKKQPNRR GLPLYSKLNP
     QGQLPENGVL DMPEESNDHY NPPFNISKLL TPIISTKHVL ETSDTQPVEI SPSPPGQLNG
     YQEKESSEAQ SRDSYKSKAP SLLFNLKDVR KRVKSTYSPL PLLKGFDEKT RGKLDSKQEP
     LSNGVTLPDG LEENPPTELL PDNVPGVLHS STQKDPAINS RESFAVSHPT FSSPSASSQT
     HFCVNGEAAE SNSNEKEEAN GESELDPSKG GGHPDCRENL PRKHLSLKLF NRESEMGPAM
     AEMKPHQLEN GLSRSVSQET ETERETGFQS LPLNQKFSPG PLSPEEEDVF YSDSQSDFTP
     CRQTKAKFST SSSDQSFASF EDQQKVCFTE GPQEDRKSHV SAGDKQRDET AVEKEESQQC
     ASRNEHRGVD EQRQEEIQRK AQGVSGGRPR KASAEDLSAR GSWMGADKDT AHTHAKDPTP
     LPASTNKHRL FPIKDNTLRA TPVIKPIILP LLRTVSSEDS LSSGHQENEL PKQLWGEDAG
     GLSASESQEM PNTPLSNNDV PGTQHRCMVC EDVQEDPVHT AAQDETSQQT RKGSFSFLPP
     VEEENRMKPS PDTAGEGLAQ EKSKSADLGK LGVPQRIPTI ALLPDDLEDS PPSLPQHTYW
     EEQGFKGHFL SAPRAGPSGR RLVPSEAETS PNPSSLGESS TCSPAASSIW EEASQAAGEH
     WQRQEPPGPN PWASPGPTGL TRREDMTHGL TWEAEGSDPS DFRALSPRGI LLADAAEKPE
     PPALLEKAAG KPPAVPPKTE KALRRAKKLA SKRRKSDQLL EKHTEAWEGK SFTEDTQGTE
     RRPVSPGKGP RPRFPAIRSL PPPTHRHSVS CGWEPTGRRP WGPQSLTPLP PYPATQKVLQ
     DPQSGQYFVF DVPLQVKIKT FYDPETGKYV KVSVPSSEEA SSEPPLQDAL AAPYLLYPGF
     RPVPVTSVMP LRCSSQLAAP TFLRQGSGHR PQSSQGSRLQ PPPERLGEST QHASGQCPRG
     PSHSPEKESA EAPRLSIIST DDLEDFATEG VS