ID A0A1V4JB62_PATFA Unreviewed; 1194 AA.
AC A0A1V4JB62;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ORFNames=AV530_012546 {ECO:0000313|EMBL:OPJ69513.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ69513.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ69513.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ69513.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ69513.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ69513.1}.
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DR EMBL; LSYS01008075; OPJ69513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4JB62; -.
DR STRING; 372326.A0A1V4JB62; -.
DR Proteomes; UP000190648; 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:UP000190648}.
FT DOMAIN 310..395
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 274..304
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 136988 MW; 42EDD207B6D30539 CRC64;
MIAEPNTSPS QKENAVHDEP VPESTVQNGS CVRNSNLKTP REKRKVREQC ENIRRNSSSS
RRVSQLQNGE VVEAVTLFEV VSMGKQAMQS VVDDWVEAYK QDRNVALLDL INFFIQCSGC
QGMVTAEMFQ SLRKKDVMRK MTETFDEETG LQYKKFMAYP WILTVTWPVD MDNEDYPLIR
TGPYWKKFKT NFCEFIAVLV QQCQCSILYD SYLMDTIISL LTGLADSMVR AFRHTSTLAA
MKLLTAVVSV HLNLDVNKHN AQRLYEVEKK RISGKRTTYR LDQLERKRKE YEQKLLEVQN
MMNAIFKGTF LNRYRDVIPE IRATCIEEIG SWIKTYPDAF LNDSYLKYIG WMLYDKQPEV
RLKCLLGLQG IYSRKELVSR MDLFTSRFKD RIVSMPLDKD HEVAVQAMKL LMLMSQNCED
VLSAEDCEAL YLFVYTTHRP LAVAAGEFLY KRLLSREGDE EVQPKGGGKF GASSDQLKRL
IRFSLESELH KHVAYLIDSL WDWAGKFLKD WECMTTLLLR NGEEDGEALS DAHENVLIEI
ILATVREAAE GHPPVGRGAT KKIVSLKEKK IQLEDCTKIT EHFIVVLPRL LAKYSTDAQK
VANLLQIPQY YDLDVYRTGH LEKHLDALLR EVKDIVAKHS DLSVLEASSR TYYILCSEEI
AIYSQVDRAR TQLIDELMGQ LNQLLDGFWQ KEEGFCMDAG EISQMNSALT RVAAFHNAHD
LTKWNLYDKT LRLLVFEMEH GSLPVLMILP ALQCTYFSLL WQLAAVSENS PKETLFALRR
QLRRFSQICT WFLHHKEKDV REKAFMILCD WLLILSHQDS NDNEEAVGLL YYLPSTSLQE
KLLLFIQKHV FMEEEEESKD LTEEEERKDE SCKLDDLHKK RSLLAAYCKL IVHNVVEMTA
AAEIYKYYVK TYSDFGDIIK EMLSKTRHNN KIQSAKTLIL CLQQLFQAHA ESQDRSSDVD
FSSASFTNIK ELARRFSLTF GWDQVKCRES VAMIHKEGIE FAFQGAAGVD GKCLPPNLNF
LLIISEFSNK LLKPDKRLVY TYLQRYIAEP LPCRGDDWQP LIFYRNSLLA NEDEEGFVLG
SPGESSSVGT SKTSSFKRKL SNGSLPETSQ TEAASKAPDL RCATRLASVA GKSRKRLKSR
EVCLQEHLPF LCPGGLQRRY CKAEIKTEDV SKEGQAEDSI EDVDVDVVGA DQDS
//
