CRACD_DANRE
ID CRACD_DANRE Reviewed; 1079 AA.
AC Q5RG44;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Capping protein inhibiting regulator of actin dynamics;
DE AltName: Full=Cancer-related regulator of actin dynamics homolog;
GN Name=crad; ORFNames=si:dkeyp-117h8.2;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Involved in epithelial cell integrity by acting on the
CC maintenance of the actin cytoskeleton. Positively regulates the actin
CC polymerization, by inhibiting the interaction of actin-capping proteins
CC with actin. {ECO:0000250|UniProtKB:Q6ZU35}.
CC -!- SUBUNIT: Directly interacts with actin-capping proteins; this
CC interaction decreases the binding of capping proteins to actin.
CC {ECO:0000250|UniProtKB:Q6ZU35}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6ZU35}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI21314.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR352243; CAI21314.2; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_001334605.1; NM_001347676.1.
DR RefSeq; NP_001334607.1; NM_001347678.1.
DR RefSeq; XP_009300880.1; XM_009302605.2.
DR AlphaFoldDB; Q5RG44; -.
DR STRING; 7955.ENSDARP00000122314; -.
DR PaxDb; Q5RG44; -.
DR Ensembl; ENSDART00000146711; ENSDARP00000122314; ENSDARG00000011602.
DR Ensembl; ENSDART00000182775; ENSDARP00000156539; ENSDARG00000011602.
DR GeneID; 570321; -.
DR KEGG; dre:570321; -.
DR CTD; 57482; -.
DR ZFIN; ZDB-GENE-041210-321; cracd.
DR eggNOG; ENOG502QQWT; Eukaryota.
DR GeneTree; ENSGT00940000161471; -.
DR HOGENOM; CLU_008508_0_0_1; -.
DR InParanoid; Q5RG44; -.
DR OMA; ECKFAKD; -.
DR OrthoDB; 446624at2759; -.
DR PhylomeDB; Q5RG44; -.
DR PRO; PR:Q5RG44; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000011602; Expressed in brain and 15 other tissues.
DR ExpressionAtlas; Q5RG44; baseline.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0010669; P:epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISS: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 3: Inferred from homology;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..1079
FT /note="Capping protein inhibiting regulator of actin
FT dynamics"
FT /id="PRO_0000342477"
FT REGION 1..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1079 AA; 123615 MW; 163A3973AE1DF7E8 CRC64;
MSQENVSDKV RNIQKQIGHN IKFGQRPPSL RKSEGDEGSS DEEEVPQSPL RVLAQVENEP
PETSAKEKSV SHDTVQHRTP VKSPRTKRPP PPGTIESINL DAVPQSVPRL DNTAAKHKLS
VKPKNQRVSR KHRRFTQEFH EDDFSEIQEE FEKDEEVFDS SREDYGIIHG SKEDYEPTEK
SQRQRFHEEE KEHLEIKKRE QEEERKMEKH RRMIEEQRLE EEKRRRQEEE RLQKVEEERK
QREEEERKKR EEEERRREEE ERRLRHEEER KRQEEEERMK KEEEERKRAE EERRQQELLA
ERLRLEEERK REQEERRRKE EEEAEKRRIQ ELQEKRLREE EHRIREEERC RQEEAERKRL
EEEERKRQLQ EEKAGSTDPE WKRKAEELRW REMEERQRPF TFKVSSGEKQ ILFQKVNLTP
VTPATGQQGE TTAETWEGAK ASSPGGPDSP TLSSSLYVPH TAILVTGAQL CGTAVNLDQI
KDTACKSLLG LSEGKKAMGT PPSKSKTSPD RKSGKTKSVF ESSLSTDQSN AAVLAEWASI
RSKIFKGAEE GKYPEYTDQS RRPTSEDLNT VPFSHTNLRK TMSASAKFSI TPARKKFADS
NRNSEIFGQE EGVKTESAFT ETSPVQKELP SLGTKVQSRG SKLVRIADEE CMFAKDLPSF
LVPSPPHGSP KSQRSESGSP IQAESEDSDT KDEDGEQKAQ GGDEQPSPFG IKLRRTNYSL
RFHNEQSAEK KKKRYSAGDS FEGVPVPLTA IDQDSDNSTL SEKSSPISPQ QENIEFQTTV
APSKESRSKF SRSTLPLART EGDNMSPKPP LYQKPATSPK PSEGATPLLS PLPKPGRRTS
GDTISQRTGE AEQVATEQGS DHKGGVTASG PSQKSGQGEE DVKEKKSFFP SISIPWREKT
DRRTELIKKE KPSLQARHSL DSSRSQDKET GPLWITLALQ KQKGFREQQQ NREERRNQRE
AKLAEKQARD RESAGSSPTE DKGNGSSSII SKHQTADENK RPDTLLARFE RRDNLKKANT
LPSSVTVEIT DSTPSPPATK DVTKRFPPGD TTQVSTEPAW LALAKRKAKA WSDCPQIIK
