REC8_CAEEL
ID REC8_CAEEL Reviewed; 781 AA.
AC Q9XUB3; E5QCH7; E5QCH8;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Meiotic recombination protein rec-8 {ECO:0000250|UniProtKB:Q12188};
DE AltName: Full=Cohesin rec-8 {ECO:0000250|UniProtKB:Q12188};
GN Name=rec-8 {ECO:0000312|WormBase:W02A2.6a};
GN ORFNames=W02A2.6 {ECO:0000312|WormBase:W02A2.6a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11390355; DOI=10.1101/gad.192701;
RA Pasierbek P., Jantsch M., Melcher M., Schleiffer A., Schweizer D.,
RA Loidl J.;
RT "A Caenorhabditis elegans cohesion protein with functions in meiotic
RT chromosome pairing and disjunction.";
RL Genes Dev. 15:1349-1360(2001).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=14499625; DOI=10.1016/s0014-4827(03)00266-0;
RA Pasierbek P., Fodermayr M., Jantsch V., Jantsch M., Schweizer D., Loidl J.;
RT "The Caenorhabditis elegans SCC-3 homologue is required for meiotic
RT synapsis and for proper chromosome disjunction in mitosis and meiosis.";
RL Exp. Cell Res. 289:245-255(2003).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12827206; DOI=10.1038/nature01697;
RA Chan R.C., Chan A., Jeon M., Wu T.F., Pasqualone D., Rougvie A.E.,
RA Meyer B.J.;
RT "Chromosome cohesion is regulated by a clock gene paralogue TIM-1.";
RL Nature 423:1002-1009(2003).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, MUTAGENESIS OF THR-625, AND PHOSPHORYLATION AT
RP THR-625.
RX PubMed=11940606; DOI=10.1083/jcb.200110045;
RA Rogers E., Bishop J.D., Waddle J.A., Schumacher J.M., Lin R.;
RT "The aurora kinase AIR-2 functions in the release of chromosome cohesion in
RT Caenorhabditis elegans meiosis.";
RL J. Cell Biol. 157:219-229(2002).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=19574299; DOI=10.1101/gad.1808809;
RA Severson A.F., Ling L., van Zuylen V., Meyer B.J.;
RT "The axial element protein HTP-3 promotes cohesin loading and meiotic axis
RT assembly in C. elegans to implement the meiotic program of chromosome
RT segregation.";
RL Genes Dev. 23:1763-1778(2009).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=21856158; DOI=10.1016/j.cub.2011.07.007;
RA Lightfoot J., Testori S., Barroso C., Martinez-Perez E.;
RT "Loading of meiotic cohesin by SCC-2 is required for early processing of
RT DSBs and for the DNA damage checkpoint.";
RL Curr. Biol. 21:1421-1430(2011).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23401519; DOI=10.1073/pnas.1213888110;
RA Schvarzstein M., Pattabiraman D., Bembenek J.N., Villeneuve A.M.;
RT "Meiotic HORMA domain proteins prevent untimely centriole disengagement
RT during Caenorhabditis elegans spermatocyte meiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E898-E907(2013).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25171895; DOI=10.7554/elife.03467;
RA Severson A.F., Meyer B.J.;
RT "Divergent kleisin subunits of cohesin specify mechanisms to tether and
RT release meiotic chromosomes.";
RL Elife 3:E03467-E03467(2014).
CC -!- FUNCTION: Plays a role in meiotic chromosome cohesion and segregation
CC (PubMed:11390355, PubMed:25171895). Necessary for sister chromatid co-
CC orientation and sister chromatid cohension until meiosis II
CC (PubMed:19574299). May also be required for repair of programmed
CC meiotic double stranded breaks (PubMed:11390355). During
CC spermatogenesis, likely involved in spermatocyte centriole cohesion,
CC thus preventing their separation during the second meiotic division
CC (PubMed:23401519). {ECO:0000269|PubMed:11390355,
CC ECO:0000269|PubMed:19574299, ECO:0000269|PubMed:23401519,
CC ECO:0000269|PubMed:25171895}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:11390355,
CC ECO:0000269|PubMed:11940606, ECO:0000269|PubMed:12827206,
CC ECO:0000269|PubMed:14499625, ECO:0000269|PubMed:21856158,
CC ECO:0000269|PubMed:23401519, ECO:0000269|PubMed:25171895}. Nucleus
CC {ECO:0000269|PubMed:11390355, ECO:0000269|PubMed:21856158,
CC ECO:0000269|PubMed:25171895}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:23401519}. Note=Colocalizes with smc-1 along
CC synapsed chromosomes during meiotic pachytene and diakinesis
CC (PubMed:12827206). Loaded onto chromosomes upon entry into meiosis
CC (PubMed:21856158). Localizes to chromosomes until meiotic anaphase II
CC and to microtubules throughout meiotic divisions (PubMed:23401519).
CC {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158,
CC ECO:0000269|PubMed:23401519}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:W02A2.6a};
CC IsoId=Q9XUB3-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:W02A2.6b};
CC IsoId=Q9XUB3-2; Sequence=VSP_057601;
CC Name=c {ECO:0000312|WormBase:W02A2.6c};
CC IsoId=Q9XUB3-3; Sequence=VSP_057600;
CC -!- TISSUE SPECIFICITY: Expressed in premeiotic and meiotic gonadal cells
CC (PubMed:11390355, PubMed:25171895). Expressed in spermatocytes
CC (PubMed:23401519). {ECO:0000269|PubMed:11390355,
CC ECO:0000269|PubMed:23401519, ECO:0000269|PubMed:25171895}.
CC -!- PTM: Phosphorylated by air-2 in vitro. {ECO:0000269|PubMed:11940606}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down results high embryonic
CC lethality (PubMed:11390355). F1 worms have an extended lifespan, an
CC increased incidence of males phenotype and improved survival to toxic
CC oxidative stress (PubMed:11390355). Worms have defective meiotic
CC chromosome cohesion and chromatid segregation (PubMed:12827206,
CC PubMed:11390355). {ECO:0000269|PubMed:11390355,
CC ECO:0000269|PubMed:12827206}.
CC -!- SIMILARITY: Belongs to the rad21 family. Highly divergent.
CC {ECO:0000305}.
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DR EMBL; Z82286; CAB05309.1; -; Genomic_DNA.
DR EMBL; Z82286; CBY25206.1; -; Genomic_DNA.
DR EMBL; Z82286; CBY25207.1; -; Genomic_DNA.
DR PIR; T26080; T26080.
DR RefSeq; NP_001255727.1; NM_001268798.1. [Q9XUB3-1]
DR RefSeq; NP_001255728.1; NM_001268799.1. [Q9XUB3-2]
DR RefSeq; NP_001255729.1; NM_001268800.1. [Q9XUB3-3]
DR AlphaFoldDB; Q9XUB3; -.
DR DIP; DIP-25674N; -.
DR IntAct; Q9XUB3; 1.
DR STRING; 6239.W02A2.6a; -.
DR iPTMnet; Q9XUB3; -.
DR EPD; Q9XUB3; -.
DR PaxDb; Q9XUB3; -.
DR PeptideAtlas; Q9XUB3; -.
DR EnsemblMetazoa; W02A2.6a.1; W02A2.6a.1; WBGene00004333. [Q9XUB3-1]
DR EnsemblMetazoa; W02A2.6b.1; W02A2.6b.1; WBGene00004333. [Q9XUB3-2]
DR EnsemblMetazoa; W02A2.6c.1; W02A2.6c.1; WBGene00004333. [Q9XUB3-3]
DR GeneID; 178295; -.
DR KEGG; cel:CELE_W02A2.6; -.
DR CTD; 178295; -.
DR WormBase; W02A2.6a; CE21236; WBGene00004333; rec-8. [Q9XUB3-1]
DR WormBase; W02A2.6b; CE45697; WBGene00004333; rec-8. [Q9XUB3-2]
DR WormBase; W02A2.6c; CE45566; WBGene00004333; rec-8. [Q9XUB3-3]
DR eggNOG; ENOG502TG65; Eukaryota.
DR HOGENOM; CLU_017209_0_0_1; -.
DR InParanoid; Q9XUB3; -.
DR OMA; ANFHENI; -.
DR OrthoDB; 1463478at2759; -.
DR PRO; PR:Q9XUB3; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00004333; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0090619; C:meiotic spindle pole; IDA:UniProtKB.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR GO; GO:0000795; C:synaptonemal complex; IDA:WormBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; ISS:WormBase.
DR GO; GO:0006302; P:double-strand break repair; IDA:WormBase.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:WormBase.
DR GO; GO:0016344; P:meiotic chromosome movement towards spindle pole; IMP:WormBase.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IMP:WormBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; TAS:WormBase.
DR GO; GO:0030997; P:regulation of centriole-centriole cohesion; IMP:UniProtKB.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0007130; P:synaptonemal complex assembly; IDA:WormBase.
DR InterPro; IPR039781; Rad21/Rec8-like.
DR InterPro; IPR006910; Rad21_Rec8_N.
DR PANTHER; PTHR12585; PTHR12585; 1.
DR Pfam; PF04825; Rad21_Rec8_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA repair; Meiosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..781
FT /note="Meiotic recombination protein rec-8"
FT /evidence="ECO:0000305"
FT /id="PRO_0000432844"
FT REGION 374..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 625
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11940606"
FT VAR_SEQ 1..757
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057600"
FT VAR_SEQ 1..194
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057601"
FT MUTAGEN 625
FT /note="T->A: Reduced overall phosphorylation."
FT /evidence="ECO:0000269|PubMed:11940606"
SQ SEQUENCE 781 AA; 89884 MW; 81C6E8BFCF4AAF40 CRC64;
MVVSAEVIRK DAVFHVAWIL GTGDSKKLSR REILDQNLPE LCHSIIEMVP ERHRGSATKT
GLYLLSLLTY GTVLIHQVQV DFLKRDVEKL KELMKKKSFI LLMAERFDRN QELQRKEDKF
ARLRSKPIMC VEELDRVDLA HLQAIGDELG INGNPGDFIM MDALPNMNQW IDNNSELNAI
YGCVEPYLRE KEITMHSTFV EGNGSNEHNK ERRNDAVIAD FSQLLFPEIP EITLGEKFPI
DVDSRKRSAI LQEEQEEALQ LPKEASEIVQ EEPTKFVSIA LLPSETVEQP APQEPIQEPI
QPIIEEPAPQ LELPQPELPP QLDAIDLVTI PASQQDMVVE YLQLINDLPD DENSRLPPLP
KDLELFEDVI LPPPAKKSKV EEEEDALERA RRRPSSRPVT PINQTDLTDL HSTVRPEDPS
FAIDSQIHDV LPQRKKSKRN LPIIHSDDLE IDEAVQKVLQ ADYSSLVRKK EDVIAKIPPK
TDAVAVLMNL PEPVFSIGYR LPPEVRDMFK ACYNQAVGSP VSDDEEDEDE EEEEEYKYAK
VCLLSPNRIV EDTLLLEEQP RQPEEFPSTD NINPPRQLQE NPVFENLEYE APPHPIRTAR
TPTPIKDLKY SVISLFPTPE KRRETSIIAE LNLDPIPVEE IDPLLTMRTE EELENVRRRQ
KSSLGVQFMR TDDLEEDTRR NRLFEDEERT RDAREDELFF YSSGSLLPNN RLNIHKELLN
EAEARYPEWV NFNEFTADHD RKKAATAFEG LLLSLKNMKV EAKQEDPYFP ILVRHISHEE
M
