ID   A0A091TIA2_PHALP        Unreviewed;       972 AA.
AC   A0A091TIA2;
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=N335_14012 {ECO:0000313|EMBL:KFQ75539.1};
OS   Phaethon lepturus (White-tailed tropicbird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC   Phaethontidae; Phaethon.
OX   NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ75539.1, ECO:0000313|Proteomes:UP000053638};
RN   [1] {ECO:0000313|EMBL:KFQ75539.1, ECO:0000313|Proteomes:UP000053638}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ75539.1};
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}.
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DR   EMBL; KK454509; KFQ75539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091TIA2; -.
DR   PhylomeDB; A0A091TIA2; -.
DR   Proteomes; UP000053638; 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   Nucleus {ECO:0000256|RuleBase:RU369063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053638}.
FT   DOMAIN          215..300
FT                   /note="SCD"
FT                   /evidence="ECO:0000259|PROSITE:PS51425"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ75539.1"
FT   NON_TER         972
FT                   /evidence="ECO:0000313|EMBL:KFQ75539.1"
SQ   SEQUENCE   972 AA;  112317 MW;  01D52F54AFDB3160 CRC64;
     VEAVTLFEVV SMGKQAMQSV VDDWVEAYKQ DRNVALLDLI NFFIQCSGCQ GMVTAEMFQS
     LHKKDVMRKM TETFDEDNED YPLIRTGPYW KKFKANFCEF IAVLVQQCQC SILYDSYLMD
     AIISLLTGLA DSMVRAFRHT STLAAMKLLA AVVSVHMNLD VNKHNTQRLY EVEKKKVSGK
     RTNYRLDQLE GKGEEYEQKL VEIQNMMNAI FKGTFLNRYR DVIPEIRATC IEEIGSCIKT
     YPDAFLKDSY LKYIGWMLYD KQAEVRLKSL LGLQGIYSRK ELVSRMDLFT SRFKDRIVSM
     PLDKDHEVAV QAMKLLMLMS QNCEDVLSAE DCETLYQFVY TTHRPLAVAA GEFLYKRLLS
     HEGDEEFQPK GGGKFGASTD QLKRLIRFFL ERELHKHVAY LIDSLWDWAG KFLKDWECMT
     TLLLKNNGEA LSDAHESALI EIILATVREA AEGHPPVGRG AAKKILSVKE KKIQLEDCTK
     ITEHFIMVLP QLLAKYSTDV QKVANLLQIP QYYDLDVYST RHLEKHLDAL LREVKDIVTK
     HSDMSVLEAS SRTYYILCSE KIAIYNQVDC ARTQLIDELM GQLNQVLEGF WQKEEGFCMD
     AGEISRMHSA LRRVAAFHNA HDLTKWNLYD KTSRLLVFEM EHGSLPVLII LPALQCTYFS
     LLWQLAAVSE NSPKQTLFAL RRELRRFSQI CMHFLHHKEK DVREKVFMIL CDWLLILSHQ
     DSNNNEEAVG LLDFLPNTSL QEKLLLFIQE HVFMEEEEES KDLTEEEERK DESCKFDDLH
     KKRSLLAAYC KLIVYNVVEM TAAAEIYKYY VKTYNDFGDI IKEMLSRTRH SNKIQSAKTL
     ILCLQQLFQT HAESQDSSSG VDFSSSSFTN MKELARRFSL TFGWDQVKFR ESVAMIHKEG
     IEFAFQGATG VDGKCLPPNL SFLVIISEFS NKLLKPDKRL VYTYLQRYIA EPLPCRGDGW
     QPLVWYRNSL LA
//