PD5BA_XENLA
ID PD5BA_XENLA Reviewed; 1448 AA.
AC Q498H0; Q4QXM2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Sister chromatid cohesion protein PDS5 homolog B-A;
DE AltName: Full=Androgen-induced proliferation inhibitor A;
GN Name=pds5b-a; Synonyms=aprin-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAI00221.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte {ECO:0000312|EMBL:AAI00221.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAV84284.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 484-1448, FUNCTION, AND PHOSPHORYLATION.
RX PubMed=15855230; DOI=10.1242/jcs.02355;
RA Losada A., Yokochi T., Hirano T.;
RT "Functional contribution of Pds5 to cohesin-mediated cohesion in human
RT cells and Xenopus egg extracts.";
RL J. Cell Sci. 118:2133-2141(2005).
CC -!- FUNCTION: Plays a role in androgen-induced proliferative arrest (By
CC similarity). Required for maintenance of sister chromatid cohesion
CC during mitosis. {ECO:0000250|UniProtKB:Q9NTI5,
CC ECO:0000269|PubMed:15855230}.
CC -!- SUBUNIT: Interacts with the cohesin complex.
CC {ECO:0000250|UniProtKB:Q9NTI5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6TRW4}.
CC -!- PTM: Phosphorylated in mitotic cells. {ECO:0000269|PubMed:15855230}.
CC -!- SIMILARITY: Belongs to the PDS5 family. {ECO:0000305}.
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DR EMBL; BC100220; AAI00221.1; -; mRNA.
DR EMBL; AY695732; AAV84284.1; -; mRNA.
DR RefSeq; NP_001089658.1; NM_001096189.1.
DR AlphaFoldDB; Q498H0; -.
DR SMR; Q498H0; -.
DR BioGRID; 592499; 5.
DR IntAct; Q498H0; 5.
DR PRIDE; Q498H0; -.
DR DNASU; 734718; -.
DR GeneID; 734718; -.
DR KEGG; xla:734718; -.
DR CTD; 734718; -.
DR Xenbase; XB-GENE-6255297; pds5b.L.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 734718; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR039776; Pds5.
DR PANTHER; PTHR12663; PTHR12663; 1.
DR SMART; SM00384; AT_hook; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1448
FT /note="Sister chromatid cohesion protein PDS5 homolog B-A"
FT /id="PRO_0000287427"
FT REPEAT 383..419
FT /note="HEAT"
FT /evidence="ECO:0000255"
FT DNA_BIND 1286..1298
FT /note="A.T hook 1"
FT /evidence="ECO:0000255"
FT DNA_BIND 1374..1386
FT /note="A.T hook 2"
FT /evidence="ECO:0000255"
FT DNA_BIND 1390..1402
FT /note="A.T hook 3"
FT /evidence="ECO:0000255"
FT REGION 1141..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 704
FT /note="P -> H (in Ref. 2; AAV84284)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="L -> W (in Ref. 2; AAV84284)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="A -> V (in Ref. 2; AAV84284)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="P -> L (in Ref. 2; AAV84284)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="L -> V (in Ref. 2; AAV84284)"
FT /evidence="ECO:0000305"
FT CONFLICT 1169
FT /note="K -> R (in Ref. 2; AAV84284)"
FT /evidence="ECO:0000305"
FT CONFLICT 1176..1177
FT /note="SM -> TT (in Ref. 2; AAV84284)"
FT /evidence="ECO:0000305"
FT CONFLICT 1211
FT /note="L -> V (in Ref. 2; AAV84284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1448 AA; 164709 MW; B276CA9EFD129AF8 CRC64;
MAHSKAKGND GKITYPPGVK EISDKISKEE MVRRLKMVVK TFMDMDQDSE EEKEQYLNLA
LHLASDFFLK HPDKDVRLLV ACCLADIFRI YAPEAPYTSP DKLKDIFMFI SRQLKGLEDT
KSPQFNRYFY LLENIAWVKS YNICFELEDS NEIFTQLYRT LFSVINNGHN QKVHMHMVDL
MSSIVCEGDT VSQELLDSVL VNLVPAHKNL NKQAYDLAKA LLKRTAQAIE PYITNFFNQV
LMLGKTSISD LSEHVFDLIL ELYNIDSHLL LSVLPQLEFK LKSNDNEERL QVVKLLAKMF
GAKDSELASQ NKTLWQCYLG RFNDIHVPVR LECVKFASHS LVNHPDLAKD LTDYLKVRSH
DPEEAIRHDV IVSIVTAAKK DLLLVNDQLL NFVRERTLDK RWRVRKEAMM GLAQIYKKYS
LQAEAGKESA KQISWIKDKL LHIYYQNSID DRLLVERIFA QYMVPHNLET TERMKCLYYL
YATLDTNAVK ALNEMWKCQN MLRHHVKDLL DLIKKPKTEA GSKAIFSKVM VITRNLPDPG
KGQDFLKKFT QVLEDDEKIR GQLEKLVSPT CSCKQAEVCV RDITKKLGNP KQPTNPFLEM
IKFLLERIAP VHIDTESISA LIKLVNKSID GTADDEDEGV TTDQAIRAGL ELLKVLSFTH
PISFHSAETF ESLLACLKMD DEKVAEAALQ IFKNTGSKIE EDFPHIRSAL LPVLQQKAKK
GPPRQAKYSI HCIQAIFSSK ETQFAQIFEP LHKSLDPGNP EQLITSLVSI GHIAQLAPDQ
FTAPLKSMVA TFVVKDLLMT DRLPGKKTTK LWVSDDEVST ETKVKIQAIK MMVRWLLGMK
NNLSKSGNST LRLLMAILHT DGDLTEHGKL SKPDMSRLRL AAASAIVKLA QEPCYHEIIT
LEQYQLCALV INDECYQVRQ LFAQKIHKGL SRLRLPLEYM AICALCAKDP VKERRAHARQ
CLVKNINVRR EYLKQHAAVS EKLFSLLPEY VVPYTVHLLA HDPDYVKVQD IEQLKDIKEC
LWFVLEILMS KNENNSHAFI RKMVEYIKQT KDGQNPDDQK MNEKMYTVCD VAMNIIISKS
TTYSLESPKD PVLPARFFTQ PDKNFSNTKN YLPAELKSFF TPGKPKSTNV LGAVNKPLSS
AGKQMLSKSS RMETVSNASS GSNPSSPGKI KGRLDSMELD QSENEDYTMS SPLSGKKSDK
RDDSDLLKSE LEKPRRGKKQ SLIDQDDSLS MDELSKPAQE PKSRTGQRGR KRAAAASDSE
EQTWQEKRLK EDLLENEDEQ NSPPKKGRRG RPPKSAKMAI SKEEPTVTTP KRGRKKAVPV
ESPPTDEDDH LEISEEQDFE NIDQKRKGRG SSRRTPQKSD STDSLLDTSR PTPQKRRGRP
PKTPTVQQKK SHVGRPRKVV SKEPESEEEM EMSQNSPALS EHLSNEDESA EEVVVAPSTG
RLRSAKKR
