PD5BB_XENLA
ID PD5BB_XENLA Reviewed; 1464 AA.
AC Q5U241;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Sister chromatid cohesion protein PDS5 homolog B-B;
DE AltName: Full=Androgen-induced proliferation inhibitor B;
GN Name=pds5b-b; Synonyms=aprin-b;
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:AAH86289.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye {ECO:0000312|EMBL:AAH86289.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in androgen-induced proliferative arrest.
CC Required for maintenance of sister chromatid cohesion during mitosis
CC (By similarity). {ECO:0000250|UniProtKB:Q9NTI5}.
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:0000250|UniProtKB:Q498H0}.
CC -!- SIMILARITY: Belongs to the PDS5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH86289.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC086289; AAH86289.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001088643.2; NM_001095174.2.
DR AlphaFoldDB; Q5U241; -.
DR SMR; Q5U241; -.
DR IntAct; Q5U241; 1.
DR GeneID; 495695; -.
DR KEGG; xla:495695; -.
DR CTD; 495695; -.
DR Xenbase; XB-GENE-6041384; pds5b.S.
DR OrthoDB; 69768at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 495695; 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; ISS: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 2: Evidence at transcript level;
KW Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1464
FT /note="Sister chromatid cohesion protein PDS5 homolog B-B"
FT /id="PRO_0000287428"
FT REPEAT 383..419
FT /note="HEAT"
FT /evidence="ECO:0000255"
FT DNA_BIND 1287..1299
FT /note="A.T hook 1"
FT /evidence="ECO:0000255"
FT DNA_BIND 1375..1387
FT /note="A.T hook 2"
FT /evidence="ECO:0000255"
FT DNA_BIND 1391..1403
FT /note="A.T hook 3"
FT /evidence="ECO:0000255"
FT REGION 1126..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1464 AA; 166925 MW; 2D1AA6281B01AA72 CRC64;
MALSKAKGND GKITYPPGVK EISDKISKEE MVRRLKMVVK TFMDMDQDSE EEKEQYLNLA
LHLASDFFLK HPDKDVRLLV ACCLADIFRI YAPEAPYTSP DKLKDIFMFI TRQLKGLEDT
KSPQFNRYFY LLENIAWVKS YNICFELEDC NEIFTQLYRT LFSVINNGHN QKVHMHMVDL
MSSIVCEGDT VSQELLDSVL VNLVPAHKNL NKQAYDLAKA LLKRTAQAIE PYITNFFNQV
LMLGKTSISD LSEHVFDLIL ELYNIDSHLL LSVLPQLEFK LKSNDNEERL QVVKLLAKMF
GAKDSELASQ NKPLWQCYLG RFNDIHVPIR LECVKFASHS LMNHPDLAKD LTEYLKVRSH
DPEEAIRHDV IVSIVTAAKK DLLLVNDQLL NFVRERTLDK RWRVRKEAMM GLAQIYKKYS
LQVEAGKESA KQISWIKDKL LHIYYQNSID DRLLVERIFA QYMVPHNLET TERMKCLYYL
YATLDTNAVK ALNEMWKCQN MLRHHVKDLL DLIKKPKTEA GSKAIFSKVM VITKNLPDPG
KGQDFLKKFT QVLEDDEKIR GQLEKLVSPT CSYKQAEVCV RDITKKLGNP KQPTNPFLEM
IKFLLERIAP VHIDTESISS LIKLVNKSID GTADDEDEGV PTDQAIRAGL ELLKVLSFTH
PISFHSAETF ESLLACLKMD DEKVAEAALQ IFKNTGNKIE EDFPHIRSAL LPVLQQKAKK
GSPRQAKYSI HCIHAIFSSK ETQFAQIFEP LHKSLDPGNP EQLITSLVTI GHIAQLAPDQ
FTAPLKSMVA TFVVKDLLMS DQLPGKKTTK LWVPDDEVSQ ETMVKIQAIK MMVRWLLGMK
NNLSKSGNST LRLLTAILHT DGDLTEHGKL SKPDMSRLRL AAGSAIVKLA QEPCYHEIIT
LEQYQLCALV INDECYQVRQ LFAQKLHKGL SRLRLPLEYM AICALCAKDP VKERRAHARQ
CLVKNINVRR EYLKQHAAVS EKLFSLLPEY VVPYTVHLLT HDPDYVKVQD IEQLKDIKEC
LWFVLEILMS KNENNSHAFI RKMVEYIKQT KDAQNPDDQK MNEKMYTVCD VAMNIIISKS
TTYSLESPKD PVLPARFFTQ PDKNFSNTKH YLPAELKSFF TPGKPKSTNV LGAVNKPLSS
AGKQMQSKSS RMETVSNASS GSNPSSPGRI KGRLDSTELD QIEYEDYTMI SSPLSGKKSD
KRDDSDLLKS EVEKPRRGRK QPLIDPDDSF SMDELSKPAQ EPKSRTSQRG RKRAAAASES
EEQAWQEKRL KEDLLENEDE QNSPPKKGRR GRPPKSAKMA ISKEEPPVTT PKRGRKNVVP
IESPPTDEED HLEISEEQDS ENIDQKRKGR GSSKKTPQKS DSTDSALDTS RPTPQKRRGR
PPKTPTVQQK KSHVGRPRKV VSKEPESEEE MEISQNSPAL SENISNEEET ADEEVVAPST
GRRRTAKKRR WIQRMKSELE GPLL