CRACD_MOUSE
ID CRACD_MOUSE Reviewed; 1207 AA.
AC Q5PR69; E9QLP4; Q80TH6; Q8C7K8; Q8C7R0; Q8C9F2; Q8CDM6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Capping protein-inhibiting regulator of actin dynamics {ECO:0000312|MGI:MGI:2444817};
DE AltName: Full=Cancer-related regulator of actin dynamics {ECO:0000303|PubMed:30361697};
GN Name=Cracd {ECO:0000312|MGI:MGI:2444817};
GN Synonyms=Crad {ECO:0000303|PubMed:30361697},
GN Kiaa1211 {ECO:0000250|UniProtKB:Q6ZU35};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 347-1207 (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 496-1207 (ISOOFRM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 817-1207 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 862-1207 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, Spinal cord, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-28; SER-132; THR-398;
RP SER-409; SER-426 AND SER-783, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=30361697; DOI=10.1038/s41556-018-0215-z;
RA Jung Y.S., Wang W., Jun S., Zhang J., Srivastava M., Kim M.J., Lien E.M.,
RA Shang J., Chen J., McCrea P.D., Zhang S., Park J.I.;
RT "Deregulation of CRAD-controlled cytoskeleton initiates mucinous colorectal
RT cancer via beta-catenin.";
RL Nat. Cell Biol. 20:1303-1314(2018).
CC -!- FUNCTION: Involved in epithelial cell integrity by acting on the
CC dynamics of the actin cytoskeleton (PubMed:30361697). Positively
CC regulates the actin polymerization, by inhibiting the interaction of
CC actin-capping proteins with actin (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZU35, ECO:0000269|PubMed:30361697}.
CC -!- SUBUNIT: Directly interacts with actin-capping proteins CAPZA1, CAPZA2
CC and CAPZB; this interaction decreases the binding of capping proteins
CC to actin. {ECO:0000250|UniProtKB:Q6ZU35}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:30361697}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5PR69-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5PR69-2; Sequence=VSP_034472;
CC -!- TISSUE SPECIFICITY: Expressed in the small intestine (at protein
CC level). {ECO:0000269|PubMed:30361697}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice display adenoma development in the
CC small intestine in an age-dependent manner. They also develop pulmonary
CC lesions resembling early small cell lung cancer and solid-
CC pseudopapillary neoplasm of the pancreas. Tumors from mutant animals
CC show increased expression of Wnt/beta-catenin target genes without the
CC alteration of other signaling pathways. Intestinal tumors exhibit
CC disorganized and decreased levels of F-actin.
CC {ECO:0000269|PubMed:30361697}.
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DR EMBL; AC166328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC086807; AAH86807.1; -; mRNA.
DR EMBL; AK122469; BAC65751.1; -; mRNA.
DR EMBL; AK029850; BAC26643.1; -; mRNA.
DR EMBL; AK042228; BAC31199.1; -; mRNA.
DR EMBL; AK049629; BAC33846.1; -; mRNA.
DR EMBL; AK050000; BAC34025.1; -; mRNA.
DR RefSeq; NP_001157265.1; NM_001163793.1.
DR AlphaFoldDB; Q5PR69; -.
DR SMR; Q5PR69; -.
DR BioGRID; 236322; 1.
DR STRING; 10090.ENSMUSP00000113947; -.
DR iPTMnet; Q5PR69; -.
DR PhosphoSitePlus; Q5PR69; -.
DR MaxQB; Q5PR69; -.
DR PaxDb; Q5PR69; -.
DR PeptideAtlas; Q5PR69; -.
DR PRIDE; Q5PR69; -.
DR ProteomicsDB; 268922; -. [Q5PR69-1]
DR ProteomicsDB; 268923; -. [Q5PR69-2]
DR GeneID; 320827; -.
DR KEGG; mmu:320827; -.
DR UCSC; uc008xvh.2; mouse. [Q5PR69-1]
DR CTD; 57482; -.
DR MGI; MGI:2444817; Cracd.
DR eggNOG; KOG1808; Eukaryota.
DR InParanoid; Q5PR69; -.
DR BioGRID-ORCS; 320827; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Rdh16; mouse.
DR PRO; PR:Q5PR69; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5PR69; protein.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0010669; P:epithelial structure maintenance; IMP:UniProtKB.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IMP:UniProtKB.
DR GO; GO:2000813; P:negative regulation of barbed-end actin filament capping; ISS:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
DR InterPro; IPR028030; DUF4592.
DR Pfam; PF15262; DUF4592; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1207
FT /note="Capping protein-inhibiting regulator of actin
FT dynamics"
FT /id="PRO_0000342476"
FT REGION 48..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..476
FT /note="Required for interaction with actin-capping
FT proteins"
FT /evidence="ECO:0000250|UniProtKB:Q6ZU35"
FT REGION 617..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..288
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 398
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZU35"
FT MOD_RES 555
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZU35"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 949
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZU35"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZU35"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZU35"
FT VAR_SEQ 1034..1036
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034472"
FT CONFLICT 353
FT /note="E -> D (in Ref. 2; AAH86807)"
FT /evidence="ECO:0000305"
FT CONFLICT 817
FT /note="E -> P (in Ref. 4; BAC33846)"
FT /evidence="ECO:0000305"
FT CONFLICT 1105
FT /note="L -> V (in Ref. 4; BAC31199)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="R -> T (in Ref. 4; BAC34025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1207 AA; 132286 MW; 25B2E070B3C3AD5E CRC64;
MGARAFSHDS IFIPDGGAES EQTVQAMSQD NILGKVKTLQ RQLGKNIKFG QRPSNAIPMK
KAGSTDASSE EDFVLTSPME IVTQQDIVPS DTENKSSDTP SSSSPLNLPE AGSDMEEKVA
PVKPSRPKRH LSSAGTIESV NLDAIPLAIA RLDNSAARHK LAVKPKNQRV SRKHRWLAQD
RQNEPGSFES QSSLDQNGQL GEDKHIWHGE EPEPLESHEE KRLHEEYWRE LEAKCKRQKA
EAAEKRRQEE QRRQALERRL WEESLRQELL EEEEEGEEEE EVKEEGEEGE EVGLQPRAGK
VPPEEGHQSG PEEQRCTEQE LGGADDPARL EAEERRREQE EAERQAEKLR QREAESQEEE
LRQREAERQR AQEEDAKGML QEEEEEAKRI EELKGKETPE PLVEEGPQSP EGESQPWLTD
DADQRSPLQR DLEKPGERER EDLESAGQRE IAEEPRGEGE PAEQSGDLDA HCGGVDGEGK
ETAQTDSPQP QERQMEGTPA PEENEATAAD IDRKVEELRW QEVDERQTMP RPYTFQVSSG
SRQILFPKVN LSPVTPAKDA SLAPAAQEPP APRGAASHAL PSALSIPHTA ILVTGAQLCG
PAVNLSQIKD TACKSLLGLS EEKRPMDVPT VESRAGSGKS RPAPESPSNA AALAEWASIR
SRILKNSEGD QRGDREPARA GDEPVPRARC DSRGNVRRTP PVNAKFSIMP AWQKFSDSGA
ETFRQSLDGE SGRKKPGLAP SEETAPQPHA AAQQEVSQEP PDTTDGCKFA KDLPSFLVPG
LPSPQKAASR TESTTTLDSE TTSDVGNPDP AMPGGEEKAS PFGIKLRRTN YSLRFHCDQQ
AEQKKKKRHS STGDSVGGAT PATGSVSGES EPEATFLKHG PSLPQERKPA LSPRKDSAES
HSSGHYVAVA QSGLPPASGQ TPAPEQDRAV SKMPSMQKPA LAPKPASQTP PSSPLSKLSR
PHLVELLARR AGKLDSEPSE TAKESSDNQP PSPSLPEELK GQKRDEKDVP EKKPASPPLP
AGQQERPSLI PETGRKEKPV LQSRHSLDGS KVTEKVETAQ PLWITLALQK QKGFREQQAT
REERKQAREA KQAEKLSKET VSVSLQPGSS RASKTAPVHK PAAPSEEKKP ETAVSRLQRR
EQLKKSNTLP TSVTVEISDS APSAALVKDV TKRFSTPDAA PVSTEPAWLA LAKRKAKAWS
DCPQIIK
