ID E7FE97_DANRE Unreviewed; 1269 AA.
AC E7FE97; A0A8M9Q1F5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Cohesin subunit SA {ECO:0000256|RuleBase:RU369063};
DE AltName: Full=SCC3 homolog {ECO:0000256|RuleBase:RU369063};
DE AltName: Full=Stromal antigen {ECO:0000256|RuleBase:RU369063};
GN Name=stag2b {ECO:0000313|Ensembl:ENSDARP00000082527,
GN ECO:0000313|RefSeq:XP_021328466.1, ECO:0000313|RefSeq:XP_686812.5,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-2785};
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 {ECO:0000313|Ensembl:ENSDARP00000082527};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000082527}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000082527};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000082527, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000082527};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA 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] {ECO:0000313|RefSeq:XP_021328466.1, ECO:0000313|RefSeq:XP_686812.5}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_021328466.1,
RC ECO:0000313|RefSeq:XP_686812.5};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Component of cohesin complex, a complex required for the
CC cohesion of sister chromatids after DNA replication. The cohesin
CC complex apparently forms a large proteinaceous ring within which sister
CC chromatids can be trapped. At anaphase, the complex is cleaved and
CC dissociates from chromatin, allowing sister chromatids to segregate.
CC {ECO:0000256|RuleBase:RU369063}.
CC -!- SUBUNIT: Part of the cohesin complex which is composed of a heterodimer
CC between a SMC1 protein (SMC1A or SMC1B) and SMC3, which are attached
CC via their hinge domain, and RAD21 which link them at their heads, and
CC one STAG protein. {ECO:0000256|RuleBase:RU369063}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369063}.
CC Chromosome {ECO:0000256|RuleBase:RU369063}. Chromosome, centromere
CC {ECO:0000256|RuleBase:RU369063}.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000256|ARBA:ARBA00005486,
CC ECO:0000256|RuleBase:RU369063}.
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DR EMBL; BX088535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR626891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_021328466.1; XM_021472791.1.
DR RefSeq; XP_686812.5; XM_681720.9.
DR PaxDb; 7955-ENSDARP00000082527; -.
DR Ensembl; ENSDART00000088094.6; ENSDARP00000082527.4; ENSDARG00000053668.6.
DR Ensembl; ENSDART00000180828.1; ENSDARP00000145761.1; ENSDARG00000109728.1.
DR GeneID; 560751; -.
DR AGR; ZFIN:ZDB-GENE-030131-2785; -.
DR CTD; 560751; -.
DR ZFIN; ZDB-GENE-030131-2785; stag2b.
DR eggNOG; KOG2011; Eukaryota.
DR HOGENOM; CLU_005067_1_0_1; -.
DR OrthoDB; 5354237at2759; -.
DR TreeFam; TF314604; -.
DR Proteomes; UP000000437; Chromosome 14.
DR Bgee; ENSDARG00000053668; Expressed in presomitic mesoderm and 23 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:1901532; P:regulation of hematopoietic progenitor cell differentiation; IMP:ZFIN.
DR GO; GO:2001212; P:regulation of vasculogenesis; IMP:ZFIN.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199:SF3; COHESIN SUBUNIT SA-2; 1.
DR PANTHER; PTHR11199; STROMAL ANTIGEN; 1.
DR Pfam; PF21581; SCD; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS51425; SCD; 1.
PE 1: Evidence at protein level;
KW Cell cycle {ECO:0000256|RuleBase:RU369063};
KW Cell division {ECO:0000256|RuleBase:RU369063};
KW Chromosome {ECO:0000256|RuleBase:RU369063};
KW Chromosome partition {ECO:0000256|RuleBase:RU369063};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|RuleBase:RU369063};
KW Proteomics identification {ECO:0007829|PeptideAtlas:E7FE97};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT DOMAIN 286..371
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 227..280
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 17..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1269 AA; 145616 MW; 6C83501AE2BE97E1 CRC64;
MIAAPELQTE FHYPQDTDTR FSSDTDFDDP DGRNAIIGKG KAKKGKKGPG EKGKGMGKGV
GRMNGHHQEN GMENVMLFEV VRLGKSAMQS VVDDWIESYK HDRDVALLDL INFFIQCSGC
KGVVSGEMFR NMQNSEIIRK MTEEFDEDSG DYPLTMTGPQ WKKFKSSFCE FIGVLVRQCQ
YSIIYDEYMM DTVISLLTGL SDSQVRAFRH TSTLAAMKLM TALVNVALNL SINMDNTQRQ
YEAERNKMIG KRANDRLELL LQKRKELQEN QDEIENMMNA IFKGVFVHRY RDAIAEIRAI
CIEEIGVWMK MYSDAFLNDS YLKYVGWTMH DKQGEVRLKC LTALQGLYHN RELNAKLELF
TSRFKDRIVS MTLDKEYDVA VQAIKLLTLV LHSSDEVLTA EDCESVYHLV YSAHRPVAVA
AGEFLFKKLF SHRDPEDDSM PKRRGRQSVN ANLIKTTVFF FLESELHEHA AYLVDSMWDC
AAELLKDWEC MISLLLDEPL PGEEALTDRQ ETALIEILLC TIRQAAECHP PVGRGTGKRV
LTAKEKKTQL DDRTRMTELF AIALPALLAK YSVDAEKVTN LLQLPQFFDL EIYTTGRLEK
HLDSLLRQIR EIVEKHTDTD VLEACSKTYH SLCNEEFTIF NRVDIARSQL LDEQVDKFNK
LLEDFLQEGE DPDEDDAYQV LSTLKRISAF YNAHDLSKWD LFTSNYKLLN TGIENGDMPE
QIVVHALQCT HYVILWSLAK VSEGCYKKED MLTLRKQMRA FCLMCQRYLT SVNTAVKEQA
FTILCDLLLI FSHQIISGGR EALEPLVYTP EASLQSELLN FILDHVFIDQ DEDSNSTDGQ
QDDEAGKIEA LHKRRNLLAA YCKLIIYNVV EMSTGADIFK QYMRYYNDYG DIIKETMSKT
RQIDKIQCAK TLILSLQQLF NEMLSELGPS FDRSSSAFCG IKELARRFSL TFGLDQLKTR
EAIAMLHKDG IEFAFKEANP QGDGHPPLNL AFLDILSEFS SKLMRQDKRT VHMYLERFMT
FQMALQREDC WLPLISYRNS LQAGGDDDTM SVVSGISSRG SSVRSKKAKP ATAKRKLPEE
ESSSSSEVWM SREQSMQTPV MMPSPHLTST IMREPKRLRP EESYMGVYTM TPDQQQQHTH
PHTPQPQHHQ TPMDYNTQVT WMLAQRQQQE EVARQQQERA MNYAKLRSNL QHAIRRGTGL
MEDDEEPIVE DVMMSSEGRI EDLNEGMDFD TMDIDLPPSK NRRERSELKP DFFDPASIMD
ESVLGVPMF
//
