ID H2QZ32_PANTR Unreviewed; 1254 AA.
AC H2QZ32;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 69.
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=STAG1 {ECO:0000313|Ensembl:ENSPTRP00000038306.4,
GN ECO:0000313|VGNC:VGNC:2595};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000038306.4, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000038306.4, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000038306.4}
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; AACZ04048203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04048204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04048205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04048206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04048207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04048208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H2QZ32; -.
DR Ensembl; ENSPTRT00000041473.4; ENSPTRP00000038306.4; ENSPTRG00000015432.6.
DR VGNC; VGNC:2595; STAG1.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR HOGENOM; CLU_005067_1_0_1; -.
DR TreeFam; TF314604; -.
DR Proteomes; UP000002277; Chromosome 3.
DR Bgee; ENSPTRG00000015432; Expressed in thymus and 21 other cell types or tissues.
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:SF6; COHESIN SUBUNIT SA-1; 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:UP000002277}.
FT DOMAIN 292..377
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..286
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1254 AA; 144027 MW; 4E3FCEBDA1FBC960 CRC64;
LLVVQMDSTN ETTAHSDAGS ELEETEVKGK RKRGRPGRPP STNKKPRKSP GEKSRIEAGI
RGVGRGRANG HPQQNGEGEP VTLFEVVKLG KSAMQSVVDD WIESYKQDRD IALLDLINFF
IQCSGCRGTV RIEMFRNMQN AEIIRKMTEE FDEDSGDYPL TMPGPQWKKF RSNFCEFIGV
LIRQCQYSII YDEYMMDTVI SLLTGLSDSQ VRAFRHTSTL AAMKLMTALV NVALNLSIHQ
DNTQRQYEAE RNKMIGKRAN ERLELLLQKR KELQENQDEI ENMMNSIFKG IFVHRYRDAI
AEIRAICIEE IGVWMKMYSD AFLNDSYLKY VGWTLHDRQG EVRLKCLKAL QSLYTNRELF
PKLELFTNRF KDRIVSMTLD KEYDVAVEAI RLVTLILHGS EEALSNEDCE NVYHLVYSAH
RPVAVAAGEF LHKKLFSRHD PQAEEALAKR RGRNSPNGNL IRMLVLFFLE SELHEHAAYL
VDSLWESSQE LLKDWECMTE LLLEEPVQGE EAMSDRQESA LIELMVCTIR QAAEAHPPVG
RGTGKRVLTA KERKTQIDDR NKLTEHFIIT LPMLLSKYSA DAEKVANLLQ IPQYFDLEIY
STGRMEKHLD ALLKQIKFVV EKHVESDVLE ACSKTYSILC SEEYTIQNRV DIARSQLIDE
FVDRFNHSVE DLLQEGEEAD DDDIYNVLST LKRLTSFHNA HDLTKWDLFG NCYRLLKTGI
EHGAMPEQIV VQALQCSHYS ILWQLVKITD GSPSKEDLLV LRKTVKSFLA VCQQCLSNVN
TPVKEQAFML LCDLLMIFSH QLMTGGREGL QPLVFNPDTG LQSELLSFVM DHVFIDQDEE
NQSMEGDEED EANKIEALHK RRNLLAAFSK LIIYDIVDMH AAADIFKHYM KYYNDYGDII
KETLSKTRQI DKIQCAKTLI LSLQQLFNEL VQEQGPNLDR TSAHVSGIKE LARRFALTFG
LDQIKTREAV ATLHKDGIEF AFKYQNQKGQ EYPPPNLAFL EVLSEFSSKL LRQDKKTVHS
YLEKFLTEQM MERREDVWLP LISYRNSLVT GGEDDRMSVN SGSSSSKTSS VRNKKGRPPL
HKKRVEDESL DNTWLNRTDT MIQTPGPLPA PQLTSTVLRE NSRPMGDQIQ EPESEHGSEP
DFLHNPQMQI SWLGQPKLED LNRKDRTGMN YMKVRTGVRH AVRGLMEEDA EPIFEDVMMS
SRSQLEDMNE EFEDTMVIDL PPSRNRRERA ELRPDFFDSA AIIEDDSGFG MPMF
//
