ID W5N691_LEPOC Unreviewed; 1258 AA.
AC W5N691;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016150.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000016150.1}
RP IDENTIFICATION.
RG Ensembl;
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; AHAT01024677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01024678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015195780.1; XM_015340294.1.
DR RefSeq; XP_015195781.1; XM_015340295.1.
DR RefSeq; XP_015195782.1; XM_015340296.1.
DR RefSeq; XP_015195783.1; XM_015340297.1.
DR AlphaFoldDB; W5N691; -.
DR STRING; 7918.ENSLOCP00000016150; -.
DR Ensembl; ENSLOCT00000016180.1; ENSLOCP00000016150.1; ENSLOCG00000013098.1.
DR GeneID; 102689854; -.
DR KEGG; loc:102689854; -.
DR CTD; 10734; -.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR InParanoid; W5N691; -.
DR OMA; LEMYSST; -.
DR OrthoDB; 5354237at2759; -.
DR Proteomes; UP000018468; Linkage group LG2.
DR Bgee; ENSLOCG00000013098; Expressed in testis and 13 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: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:SF10; COHESIN SUBUNIT SA; 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 326..411
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 290..320
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1231
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 142291 MW; 60D6EB6186F3C956 CRC64;
MDQSKTMEPT SSPRPHARGP ASSNKNQPGS KAQQIKDVFD SVEEWSEPSD SGSDFEPPAK
RRSRKRTAHS EPARSPVARQ ADRETVHKRA QRNTAQAHRT PPRASETRSQ QVTAAHLYEA
VRGGRTAMRS LIDDFLEGYK QDKEAELLEL INFIVMCSGC KGVVNRKMFA NMQNAQIISR
LTREFDEDSG SYPLCSPGVQ WKKFRVNLCE FFSMLVHRCQ NSLLYDETLF SSLIALLTGM
SDSQVRAFRH TSTLIVLKLM TALVEVSLGV GYQRETCQRL YEAELGKELQ RQAPAKLEEL
RDKLAELQEQ QEEMNSMINS IFKGVFVHRY RDILPEIRAL CMEEIGLWMK IHSESFLNDG
YLKYLGWTLH DKQGAVRLKC LKALQGLYSE KDFIGRLELF TNRFKERILS MVLDKEVEAA
VEAVHLLVLI QQNTEDVLTQ EDCDNVYLLV FSSHRGLASA AGTFLYNRLC SKVEGDSERM
EVDNRRMAII KLLLSFYIQT ELHEHGAYLV DSLWDSASAE LKDWQTMTEL LLGRPGEEEG
LGDEEESALI ELMVCAVKQA AEGQPPIGRV SGKRVQTAKE KKTRAQDRIR LTGHFIIVLP
QLLAKYSADV EKVTCLLQTP LHFNMDIYCT GRLEKYLELL LDQVSMIAEK HTNDGVLDAC
ARVFSELCSD CYTFAGRSNV ALSQLVEGLV DRFTTTVEDL LQGTLDEDEQ YGAVANLKRI
AALYNAKDLT RWELFDPCYQ ILNHGVQSGH TVMEVMVPAL KSAFLHVMWE LVRVVNSQPS
KAQLSQLKQH TKGLIAVFQS CLSMIKKEIR DQAFLLLCDF LIILSPKLAK GRDDLQTVVF
LPPDALRLEM ASFVMDYVFV EEEVDDKEED LEKMEDLHRR RNQLAGYCKL IVYNVLDLSA
ATDVFKHFVK FYKDFGDIIK ETLSRAKLIN RVQCAKTVCL SLQQLFTELV QDHGVASMSV
SPEFGAMRDL AHRLAMTFGI ELHSVREALV ALHKDGIRFA FRDLGVGDRP PENLHFLEIL
SEFSFKLIKQ DRALLANFLQ RMTSSTSTSS RFWPPMVMYQ RSLQTGEKEA GGWDKRSSVS
RTSPRTPASR PRRKRATAAS SPSVKETAWL DQSSSFHSKL QTPPLTSTVL KKAPQAPSDR
ESEVYRTLPD RDRASSERGS EADFTNSPPV RSVSRKQAAF PTPTKTRALP NPTPTPTSGR
SRDLDSQLHL LSLIEEDEDD NQEELEIDDD EGSGGTSPLH LPSTRYQHSG GFLEDLFD
//
