ID A0A091P4N5_9PASS Unreviewed; 973 AA.
AC A0A091P4N5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
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};
DE Flags: Fragment;
GN ORFNames=N310_02124 {ECO:0000313|EMBL:KFP86525.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP86525.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP86525.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP86525.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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; KK844672; KFP86525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091P4N5; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:UniProtKB-UniRule.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199:SF2; SCD DOMAIN-CONTAINING PROTEIN; 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:UP000053537}.
FT DOMAIN 215..300
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT COILED 179..209
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP86525.1"
FT NON_TER 973
FT /evidence="ECO:0000313|EMBL:KFP86525.1"
SQ SEQUENCE 973 AA; 112365 MW; 9D0401E608C4620C CRC64;
VEAVTLFEVV SIGKQAMQSV VDDWVEAYKQ DRDVALLDLI NFFIQCSGCQ GMVTAEMFQS
LHKKDVMQKM TETFDEDNED YPLIRTGPYW KKFKANFCEF IAVLVQQCQC SILYDNYFMD
TIISLLTGLA DSMVRAFRHT STLAAMKLLT AVVSVHLNLD VNRHNAQRLY ELKKQGLSGK
RTNYRLDQLE RKKKEYEHKL LEIQNMMNTI FKGTFLTRYC DVIPEIRATC MEEIGSWIKT
CPDAFLNDSY LKYVGWMLYD KQAEVRLKCL LGLQGIYSKK ELVSRMDLFN SRFKDRIVSM
PLDKDHEVAV QAMKLLMLMS QNCQDVLSAE DCEMLHQFVY TTHRPLAAAA GEFLYKRLLS
CEGDEEVQPK GEGKLGASAD QLKRLIHFFL ESELHKHVPY LIDSLWDWAG KFLKDWECMT
TLLLKNAEED GEALNDAQES ALIEIILATV REAAEGHPPV GRGAAKKILS VKEKKIQLED
CTKITEHFIV VLPQLLAKYS TDAQKVANLL QIPQYYDLDV YSTGHLEKHL DALLREIKDI
VAKHSDMSVL EASSRTYYTF CSEEIAIYSQ VDHARTQLID ELMEQLNQLL DCFWQKEGGF
CTDAGEISRM HSALRRIAAF HNAHDLTKWN LYDKTLRFLE FEMEHGSLPV MIILPALQCT
YFSLLWQLAA VSENSPKETL FPLRRELRRF SQICTCFLHH KDKDVREKAF MILCDWLLIL
SHQNSNNNEE AVRLLGYLPN ASLQEKLFLF IQEHVFVDEE ESKDLREEEE EKNESCKLDD
LHKKRRLLAA YCKLIVYNVV EMTAAAEIYK YYVKSYNDFG DIIKETLSKM RHNNKIQSAK
TLILCLQQLF KTHVESQDSS SGVDFSSASF TNIKELARRF SLTFGLDQVK SRESVAMIHK
EGIEFAFQGA TRVDGKSLPP NLSFLVIISE FSNKLLKPDK RLVYAYLQRY IAEPLPCREE
WQPLVCYRSS LLA
//
