RCC2_DANRE
ID RCC2_DANRE Reviewed; 495 AA.
AC Q6NYE2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein RCC2 homolog;
GN Name=rcc2; ORFNames=zgc:77115;
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 MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25074804; DOI=10.1242/jcs.154864;
RA Williamson R.C., Cowell C.A., Hammond C.L., Bergen D.J., Roper J.A.,
RA Feng Y., Rendall T.C., Race P.R., Bass M.D.;
RT "Coronin-1C and RCC2 guide mesenchymal migration by trafficking Rac1 and
RT controlling GEF exposure.";
RL J. Cell Sci. 127:4292-4307(2014).
CC -!- FUNCTION: Multifunctional protein that may affect its functions by
CC regulating the activity of small GTPases, such as RAC1 and RALA.
CC Required for normal progress through the cell cycle, both during
CC interphase and during mitosis. Required for normal attachment of
CC kinetochores to mitotic spindles. Required for normal organization of
CC the microtubule cytoskeleton in interphase cells. Interferes with the
CC activation of RAC1 by guanine nucleotide exchange factors. Prevents
CC accumulation of active, GTP-bound RAC1, and suppresses RAC1-mediated
CC reorganization of the actin cytoskeleton and formation of membrane
CC protrusions (By similarity). Required for normal cellular responses to
CC contacts with the extracellular matrix of adjacent cells, and for
CC directional cell migration (PubMed:25074804).
CC {ECO:0000250|UniProtKB:Q9P258, ECO:0000269|PubMed:25074804}.
CC -!- SUBUNIT: Interacts with RAC1. Interacts with CORO1C.
CC {ECO:0000250|UniProtKB:Q9P258}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9P258}. Nucleus {ECO:0000250|UniProtKB:Q9P258}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9P258}. Chromosome,
CC centromere {ECO:0000250|UniProtKB:Q9P258}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250|UniProtKB:Q9P258}. Chromosome
CC {ECO:0000250|UniProtKB:Q9P258}. Midbody {ECO:0000250|UniProtKB:Q9P258}.
CC Cell membrane {ECO:0000250|UniProtKB:Q9P258}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q9P258}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9P258}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown in single-cell embryos does
CC not lead to gross anatomical defects, but causes subtle defects in the
CC migration of neural crest cells, so that cells populate also the
CC pharyngeal pouch, instead of being restricted to pharyngeal arches.
CC {ECO:0000269|PubMed:25074804}.
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DR EMBL; BC066628; AAH66628.1; -; mRNA.
DR RefSeq; NP_998341.1; NM_213176.1.
DR RefSeq; XP_005162219.1; XM_005162162.3.
DR RefSeq; XP_017209027.1; XM_017353538.1.
DR AlphaFoldDB; Q6NYE2; -.
DR SMR; Q6NYE2; -.
DR STRING; 7955.ENSDARP00000004838; -.
DR PaxDb; Q6NYE2; -.
DR PRIDE; Q6NYE2; -.
DR Ensembl; ENSDART00000010647; ENSDARP00000004838; ENSDARG00000011510.
DR Ensembl; ENSDART00000170713; ENSDARP00000141590; ENSDARG00000115981.
DR GeneID; 406455; -.
DR KEGG; dre:406455; -.
DR CTD; 55920; -.
DR ZFIN; ZDB-GENE-040426-2213; rcc2.
DR eggNOG; KOG1427; Eukaryota.
DR GeneTree; ENSGT00940000156151; -.
DR HOGENOM; CLU_005210_7_0_1; -.
DR InParanoid; Q6NYE2; -.
DR OMA; YGCLSGI; -.
DR OrthoDB; 1062377at2759; -.
DR PhylomeDB; Q6NYE2; -.
DR TreeFam; TF101168; -.
DR Reactome; R-DRE-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR Reactome; R-DRE-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q6NYE2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000011510; Expressed in early embryo and 28 other tissues.
DR ExpressionAtlas; Q6NYE2; baseline and differential.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
DR Gene3D; 2.130.10.30; -; 2.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR028641; RCC2.
DR InterPro; IPR000408; Reg_chr_condens.
DR PANTHER; PTHR46207; PTHR46207; 1.
DR Pfam; PF00415; RCC1; 4.
DR PRINTS; PR00633; RCCNDNSATION.
DR SUPFAM; SSF50985; SSF50985; 1.
DR PROSITE; PS00626; RCC1_2; 2.
DR PROSITE; PS50012; RCC1_3; 5.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cell membrane; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Membrane; Mitosis; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..495
FT /note="Protein RCC2 homolog"
FT /id="PRO_0000206654"
FT REPEAT 76..138
FT /note="RCC1 1"
FT REPEAT 141..192
FT /note="RCC1 2"
FT REPEAT 194..244
FT /note="RCC1 3"
FT REPEAT 246..320
FT /note="RCC1 4"
FT REPEAT 321..374
FT /note="RCC1 5"
FT REPEAT 376..420
FT /note="RCC1 6"
FT REPEAT 421..474
FT /note="RCC1 7"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..298
FT /note="Required for interaction with RAC1"
FT /evidence="ECO:0000250|UniProtKB:Q9P258"
SQ SEQUENCE 495 AA; 54152 MW; 8AC9A686AA071074 CRC64;
MPRKKVTDVS GNGGLKRKRG GGKKKEREFS SDDEFDDYEQ ENTKKPGKPA AKAGLQPVTV
ADDVKEKIKL EVPKVKGQLL IFGATNWDLI GRKEVPKQQA AFRNLGQNLW GPHRYGCLSD
VQVSCVVSGP CAAHSLIITT EGKLWSWGRN DKGQLGHGDT KRLEAPKLIE GLGEEVIVAA
ACGRNHTLAL TENGTVYTFG ENKLGQLGQG NQTDAVLSPA TIQYNGQPIV KVACGAEFSM
IVDCKGNLYS FGCPEYGQLG HNSDGKFIAR AQRIEFDCEL IPRRVAIFIE KTKDGQVLPV
PNVVARDVAC GANHTLVLDS QKRVFSWGFG GYGRLGHAEQ KDEMVPRLVK LFDFPGRGAT
QIYCGYQCSF ALSEMGGLFF WGVTNTSRES TMYPKAVQDL CGWKIRSLAC GKSSIIVAAD
DSTISWGPSP TFGELGYGDN KPKSSTTAQE VKTLDGVYSE QVVMGYSHSL VIARQDTEQE
KEKLKKLPEY NPRTL
