RA21A_DANRE
ID RA21A_DANRE Reviewed; 643 AA.
AC Q6TEL1; Q7ZW30;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Double-strand-break repair protein rad21 homolog A;
DE AltName: Full=SCC1 homolog;
DE Contains:
DE RecName: Full=64-kDa C-terminal product;
DE AltName: Full=64-kDa carboxy-terminal product {ECO:0000250|UniProtKB:O60216};
GN Name=rad21a; Synonyms=rad21, SCC1;
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 [MRNA].
RC TISSUE=Kidney marrow;
RX PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA Look A.T., Chen Z.;
RT "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 277-GLY--VAL-643.
RX PubMed=17567667; DOI=10.1242/dev.002485;
RA Horsfield J.A., Anagnostou S.H., Hu J.K., Cho K.H., Geisler R.,
RA Lieschke G., Crosier K.E., Crosier P.S.;
RT "Cohesin-dependent regulation of Runx genes.";
RL Development 134:2639-2649(2007).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25575569; DOI=10.1053/j.gastro.2014.12.034;
RA Bonora E., Bianco F., Cordeddu L., Bamshad M., Francescatto L., Dowless D.,
RA Stanghellini V., Cogliandro R.F., Lindberg G., Mungan Z., Cefle K.,
RA Ozcelik T., Palanduz S., Ozturk S., Gedikbasi A., Gori A., Pippucci T.,
RA Graziano C., Volta U., Caio G., Barbara G., D'Amato M., Seri M.,
RA Katsanis N., Romeo G., De Giorgio R.;
RT "Mutations in RAD21 disrupt regulation of APOB in patients with chronic
RT intestinal pseudo-obstruction.";
RL Gastroenterology 148:771-782(2015).
CC -!- FUNCTION: Double-strand-break repair protein rad21 homolog: As a member
CC of the cohesin complex, involved in sister chromatid cohesion from the
CC time of DNA replication in S phase to their segregation in mitosis, a
CC function that is essential for proper chromosome segregation, post-
CC replicative DNA repair, and the prevention of inappropriate
CC recombination between repetitive regions. The cohesin complex may also
CC play a role in spindle pole assembly during mitosis (By similarity). In
CC interphase, cohesins may function in the control of gene expression by
CC binding to numerous sites within the genome (By similarity). May
CC control RUNX gene expression, including that of RUNX1 and RUNX3
CC (PubMed:17567667). May play a role in embryonic gut development,
CC possibly through the regulation of enteric neuron development
CC (PubMed:25575569). {ECO:0000250|UniProtKB:O60216,
CC ECO:0000250|UniProtKB:Q61550, ECO:0000269|PubMed:17567667,
CC ECO:0000269|PubMed:25575569}.
CC -!- FUNCTION: [64-kDa C-terminal product]: May promote apoptosis.
CC {ECO:0000250|UniProtKB:O60216}.
CC -!- SUBUNIT: Component of the cohesin complex, which consists of an SMC1
CC and SMC3 heterodimer core and 2 non-Smc subunits RAD21 and STAG1/SA1,
CC STAG2/SA2 or STAG3/SA3. {ECO:0000250|UniProtKB:O60216}.
CC -!- SUBCELLULAR LOCATION: [Double-strand-break repair protein rad21 homolog
CC A]: Nucleus {ECO:0000250|UniProtKB:O60216}. Nucleus matrix
CC {ECO:0000250|UniProtKB:O60216}. Chromosome
CC {ECO:0000250|UniProtKB:O60216}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:O60216}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:O60216}. Note=Associates with chromatin. Before
CC prophase, scattered along chromosome arms. During prophase and
CC prometaphase, most cohesins dissociate from the arms of condensing
CC chromosome, possibl through PLK1-mediated phosphorylation (By
CC similarity). A small amount of cohesin remains in centromeric regions
CC and is removed from chromosomes only at the onset of anaphase. At
CC anaphase, cleavage by separase/ESPL1 leads to the dissociation of
CC cohesin from chromosomes and chromosome separation (By similarity).
CC {ECO:0000250|UniProtKB:O60216, ECO:0000250|UniProtKB:O93310}.
CC -!- SUBCELLULAR LOCATION: [64-kDa C-terminal product]: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:O60216}. Nucleus {ECO:0000250|UniProtKB:O60216}.
CC -!- DEVELOPMENTAL STAGE: Detected at the oocyte stage. Expressed throughout
CC the embryo in early embryogenesis, with particularly robust expression
CC in the brain and posterior tail regions at 26 hpf. At 48 hpf, strongly
CC expressed in discrete areas of the brain, the mandibular cartilage and
CC branchial arches, the otic vesicle and developing pectoral fins.
CC {ECO:0000269|PubMed:17567667}.
CC -!- PTM: Cleaved at the onset of anaphase; this cleavage is required for
CC sister chromatid separation and cytokinesis. Cleaved by caspases at the
CC beginning of apoptosis. {ECO:0000250|UniProtKB:O60216}.
CC -!- PTM: May be phosphorylated; may become hyperphosphorylated in M phase
CC of cell cycle. The large dissociation of cohesin from chromosome arms
CC during prophase may be partly due to its phosphorylation by PLK1.
CC {ECO:0000250|UniProtKB:O93310}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC abnormal embryonic development (PubMed:17567667). At 5 dpf, morphants
CC exhibit delayed food transit along the gut and depletion of enteric
CC neurons (PubMed:25575569). {ECO:0000269|PubMed:17567667,
CC ECO:0000269|PubMed:25575569}.
CC -!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY423040; AAQ98016.1; -; mRNA.
DR EMBL; FP015828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC045311; AAH45311.1; -; mRNA.
DR EMBL; BC164557; AAI64557.1; -; mRNA.
DR RefSeq; NP_955889.1; NM_199595.1.
DR AlphaFoldDB; Q6TEL1; -.
DR SMR; Q6TEL1; -.
DR STRING; 7955.ENSDARP00000009867; -.
DR PaxDb; Q6TEL1; -.
DR PRIDE; Q6TEL1; -.
DR Ensembl; ENSDART00000005927; ENSDARP00000009867; ENSDARG00000006092.
DR Ensembl; ENSDART00000190554; ENSDARP00000156767; ENSDARG00000006092.
DR GeneID; 322275; -.
DR KEGG; dre:322275; -.
DR CTD; 322275; -.
DR ZFIN; ZDB-GENE-030131-994; rad21a.
DR eggNOG; KOG1213; Eukaryota.
DR GeneTree; ENSGT00940000154655; -.
DR HOGENOM; CLU_015775_1_1_1; -.
DR InParanoid; Q6TEL1; -.
DR OMA; IIHESSA; -.
DR OrthoDB; 1253899at2759; -.
DR PhylomeDB; Q6TEL1; -.
DR TreeFam; TF101215; -.
DR PRO; PR:Q6TEL1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000006092; Expressed in mature ovarian follicle and 56 other tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:ZFIN.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:ZFIN.
DR GO; GO:0008015; P:blood circulation; IMP:ZFIN.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:ZFIN.
DR GO; GO:0048484; P:enteric nervous system development; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:ZFIN.
DR GO; GO:0060037; P:pharyngeal system development; IMP:ZFIN.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:ZFIN.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:ZFIN.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IBA:GO_Central.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0003187; P:ventriculo bulbo valve morphogenesis; IMP:ZFIN.
DR Gene3D; 1.10.10.580; -; 1.
DR InterPro; IPR039781; Rad21/Rec8-like.
DR InterPro; IPR006909; Rad21/Rec8_C_eu.
DR InterPro; IPR006910; Rad21_Rec8_N.
DR InterPro; IPR023093; ScpA-like_C.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12585; PTHR12585; 1.
DR Pfam; PF04824; Rad21_Rec8; 1.
DR Pfam; PF04825; Rad21_Rec8_N; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Activator; Apoptosis; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Developmental protein;
KW DNA damage; DNA repair; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..643
FT /note="Double-strand-break repair protein rad21 homolog A"
FT /id="PRO_0000446304"
FT CHAIN 276..643
FT /note="64-kDa C-terminal product"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT /id="PRO_0000446305"
FT REGION 234..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 275..276
FT /note="Cleavage; by caspases"
FT /evidence="ECO:0000250|UniProtKB:O60216"
FT MUTAGEN 277..643
FT /note="Missing: Down-regulation of RUNX1 and RUNX3
FT expression. In embryos carrying the nonsense mutant, early
FT neurogenesis is abnormal; the trigeminal ganglia fail to
FT develop properly, the number of Rohon-Beard mechanosensory
FT neurons is reduced and no visible blood circulation
FT develops. From the 20-somite stage, embryos start to
FT exhibit developmental delay, which becomes increasingly
FT apparent until they arrest in development at around 35 hpf.
FT They die at around 3 dpf. The developmental phenotype may
FT be due to a cellular block at M phase."
FT /evidence="ECO:0000269|PubMed:17567667"
FT CONFLICT 592
FT /note="S -> G (in Ref. 3; AAH45311/AAI64557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 643 AA; 72271 MW; 1DBF4AA7D4263D1A CRC64;
MFYAHFVLSK RGPLAKIWLA AHWDKKLTKA HVFECNLESS VESIISPKVK MALRTSGHLL
LGVVRIYHRK AKYLLADCNE AFIKIKMAFR PGVVDLPEDN REAAYNAITL PEEFHDFDQP
LPDLDDIDVA QQFTLNQSRV EEITMREEVG NISLMTDNDF GDFGMDDREM MREENAFGDI
IHESSAANLL LEAEPGPAHL PDKTPNLDYD DFGDNNLENS DGGILMDKIL SNEDGGGIFD
DPPAITDSVM MPQDHGDDDD DFDNFSPAGG PDSPDSGPVE PLPNTTDQTD QTEQTTLVPN
EDEAFALEPI DITVKETKAK RKRKLIVDSL KELDSKTIRA QLSDYSDIVT TLDLAPPTKK
LMMWKETGGV EKLFSLPAQP LWNGRLLKMF TRCLTPLVPD ELRKRRKGGE ADSLEDFLKE
LENPEVPREE VLGHRSDVID QTIMEEPSML QASSMEGSRT ALDESMMPPP SRQRGLKRKS
LETLEKDAVL PPMGVLEQTL QPLDQSVLSH QLEMPQVELP PEDTTNLSRL IPELDLLDEK
SKDKDKDDSD EEGEEGQGGD QDQEERRWNK RTQQMLHGLQ RVVAKTGAQS ISLLELCRNN
NKKQAAAKFY SFLVLKKQQA IDLTQTEPYS DIIAAPGPRF HIV
