ID   PDS5B_RAT               Reviewed;        1447 AA.
AC   Q6TRW4; Q5G5U1; Q5G6V7; Q5G6V8; Q5PY35; Q5PY36;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-NOV-2023, entry version 100.
DE   RecName: Full=Sister chromatid cohesion protein PDS5 homolog B;
DE   AltName: Full=Androgen-induced proliferation inhibitor;
DE   AltName: Full=Androgen-induced prostate proliferative shutoff-associated protein AS3;
GN   Name=Pds5b; Synonyms=Aprin, As3 {ECO:0000303|PubMed:12072405};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAQ91374.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 42-283, NUCLEOTIDE SEQUENCE [MRNA] OF
RP   1110-1378 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1110-1264 (ISOFORM 3),
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1327-1381 (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 1334-1420 (ISOFORM 2).
RC   STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAQ91374.1}, and Wistar
RC   {ECO:0000312|EMBL:AAW69306.1};
RC   TISSUE=Liver {ECO:0000312|EMBL:AAW69306.1}, and Testis
RC   {ECO:0000312|EMBL:AAQ91374.1};
RA   Weiler E., Farbman A.I.;
RT   "Aprin expression in rat olfactory epithelium.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=9459187; DOI=10.1016/s0960-0760(97)00122-2;
RA   Geck P., Szelei J., Jimenez J., Lin T.-M., Sonnenschein C., Soto A.M.;
RT   "Expression of novel genes linked to the androgen-induced, proliferative
RT   shutoff in prostate cancer cells.";
RL   J. Steroid Biochem. Mol. Biol. 63:211-218(1997).
RN   [4] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12072405; DOI=10.1210/endo.143.7.8899;
RA   Maffini M.V., Geck P., Powell C.E., Sonnenschein C., Soto A.M.;
RT   "Mechanism of androgen action on cell proliferation: AS3 protein as a
RT   mediator of proliferative arrest in the rat prostate.";
RL   Endocrinology 143:2708-2714(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1162; SER-1166; SER-1221;
RP   SER-1257; SER-1283; SER-1357 AND THR-1369, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Regulator of sister chromatid cohesion in mitosis which may
CC       stabilize cohesin complex association with chromatin. May couple sister
CC       chromatid cohesion during mitosis to DNA replication. Cohesion ensures
CC       that chromosome partitioning is accurate in both meiotic and mitotic
CC       cells and plays an important role in DNA repair. Plays a role in
CC       androgen-induced proliferative arrest in prostate cells.
CC       {ECO:0000269|PubMed:12072405}.
CC   -!- SUBUNIT: Interacts with the cohesin complex. Interacts with RAD21; the
CC       interaction is direct. Interacts with WAPL (via FGF motifs) or CDCA5
CC       (via the FGF motif); the interaction is direct, cohesin-dependent and
CC       competitive (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12072405}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:15057822};
CC         IsoId=Q6TRW4-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|Ref.2};
CC         IsoId=Q6TRW4-2; Sequence=VSP_052408;
CC       Name=3 {ECO:0000269|Ref.2};
CC         IsoId=Q6TRW4-3; Sequence=VSP_052407;
CC   -!- TISSUE SPECIFICITY: Highly expressed in intact prostate with levels
CC       decreasing after castration. Expressed exclusively in prostate cells
CC       inhibited from proliferating by long-term androgen exposure.
CC       {ECO:0000269|PubMed:9459187}.
CC   -!- SIMILARITY: Belongs to the PDS5 family. {ECO:0000305}.
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DR   EMBL; AABR03082233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03082545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY388627; AAQ91374.1; -; mRNA.
DR   EMBL; AY820182; AAV68352.1; -; mRNA.
DR   EMBL; AY820183; AAV68353.1; -; mRNA.
DR   EMBL; AY831451; AAW69306.1; -; Genomic_DNA.
DR   EMBL; AY831452; AAW69307.1; -; mRNA.
DR   EMBL; AY836673; AAW69308.1; -; mRNA.
DR   AlphaFoldDB; Q6TRW4; -.
DR   SMR; Q6TRW4; -.
DR   STRING; 10116.ENSRNOP00000063199; -.
DR   iPTMnet; Q6TRW4; -.
DR   PhosphoSitePlus; Q6TRW4; -.
DR   PaxDb; 10116-ENSRNOP00000063199; -.
DR   PeptideAtlas; Q6TRW4; -.
DR   UCSC; RGD:1310838; rat. [Q6TRW4-1]
DR   AGR; RGD:1310838; -.
DR   RGD; 1310838; Pds5b.
DR   eggNOG; KOG1525; Eukaryota.
DR   InParanoid; Q6TRW4; -.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-2468052; Establishment of Sister Chromatid Cohesion.
DR   Reactome; R-RNO-2470946; Cohesin Loading onto Chromatin.
DR   Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR   PRO; PR:Q6TRW4; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR   CDD; cd19953; PDS5; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR039776; Pds5.
DR   PANTHER; PTHR12663; ANDROGEN INDUCED INHIBITOR OF PROLIFERATION AS3 / PDS5-RELATED; 1.
DR   PANTHER; PTHR12663:SF1; SISTER CHROMATID COHESION PROTEIN PDS5 HOMOLOG B; 1.
DR   Pfam; PF20168; PDS5; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division; Mitosis;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1447
FT                   /note="Sister chromatid cohesion protein PDS5 homolog B"
FT                   /id="PRO_0000287426"
FT   REPEAT          383..419
FT                   /note="HEAT"
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        1247..1259
FT                   /note="A.T hook 1"
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        1287..1299
FT                   /note="A.T hook 2"
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        1371..1383
FT                   /note="A.T hook 3"
FT                   /evidence="ECO:0000255"
FT   REGION          1137..1447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1138..1170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1195..1287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1305..1324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1354..1391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1136
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT   MOD_RES         1140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT   MOD_RES         1162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT   MOD_RES         1182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT   MOD_RES         1191
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT   MOD_RES         1221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1257
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT   MOD_RES         1283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1357
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1365
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4VA53"
FT   MOD_RES         1366
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT   MOD_RES         1368
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4VA53"
FT   MOD_RES         1369
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         1380
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT   MOD_RES         1382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NTI5"
FT   MOD_RES         1416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4VA53"
FT   MOD_RES         1419
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4VA53"
FT   VAR_SEQ         1207..1208
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_052407"
FT   VAR_SEQ         1354..1390
FT                   /note="RAESPETSAVESTQSTPQKGRGRPSKTPSPSQPKKNI -> S (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_052408"
SQ   SEQUENCE   1447 AA;  164459 MW;  9EC8B4A03C320428 CRC64;
     MAHSKTRTND GKITYPPGVK EISDKISKEE MVRRLKMVVK TFMDMDQDSE EEKELYLNLA
     LHLASDFFLK HPDKDVRLLV ACCLADIFRI YAPEAPYTSP DKLKDIFMFI TRQLKGLEDT
     KSPQFNRYFY LLENIAWVKS YNICFELEDS NEIFTQLYRT LFSVINNGHN QKVHMHMVDL
     MSSIICEGDT VSQELLDTVL VNLVPAHKNL NKQAYDLAKA LLKRTAQAIE PYITNFFNQV
     LMLGKTSISD LSEHVFDLIL ELYNIDSHLL LSVLPQLEFK LKSNDNEERL QVVKLLAKMF
     GAKDSELASQ NKPLWQCYLG RFNDIHVPIR LECVKFASHC LMNHPDLAKD LTEYLKVRSH
     DPEEAIRHDV IVSIVTAAKK DILLVNDHLL NFVRERTLDK RWRVRKEAMM GLAQIYKKYA
     LQSAAGKDAA KQICWVKDKL LHIYYQNSID DRLLVERIFA QYMVPHNLET TERMKCLYYL
     YATLDLNAVK ALNEMWKCQN LLRHQVKDLL DLIKQPKTDA SVKAIFSKVM VITRNLPDPG
     KAQDFMKKFT QVLEDDEKIR KQLEALVSPT CSCKQAEGCV REITKKLGNP KQPTNPFLEM
     IKFLLERIAP VHIDTESISA LIKQVNKSID GTADDEDEGV PTDQAIRAGL ELLKVLSFTH
     PISFHSAETF ESLLACLKMD DEKVAEAALQ IFKNTGSKIE EDFPHIRSAL LPVLHHKSKK
     GPPRQAKYAI HCIHAIFSSK ETQFAQIFEP LHKSLDPSNL EHLITPLVTI GHIALLAPDQ
     FAAPLKSLVA TFIVKDLLMN DRLPGKKTTK LWVPDEEVSP ETMVKIQAIK MMVRWLLGMK
     NNHSKSGTST LRLLTTILHS DGDLTEQGKI SKPDMSRLRL AAGSAIVKLA QEPCYHEIIT
     LEQYQLCALA INDECYQVRQ VFAQKLHKGL SRLRLPLEYM AICALCAKDP VKERRAHARQ
     CLVKNITVRR EYLKQHAAVS EKLLSLLPEY VVPYTIHLLA HDPDYVKVQD IEQLKDVKEC
     LWFVLEILMA KNENNSHAFI RKMVENIKQT KDAQGPDDTK MNEKLYTVCD VAMNIIMSKS
     TTYSLESPKD PVLPARFFTQ PDKNFSNTKN YLPPEMKSFF TPGKPKTANV LGAVNKPLSS
     AGKQSQTKSS RMETVSNASS SSNPSSPGRI KGRLDSTEMD HSENEDYTMS SPLPGKKSDK
     REDSDLVRSE LEKPRSRKKA SVTDPEEKLG MDDLSKLVQE QKPKGSQRGR KRGHAASESE
     EQQWPEEKRH KEELLGNEDE QNSPPKKGKR GRPPKPLGGT SKEEPVVKTS KKGNKKKPAP
     PVVDEDEEEE RQMGNTEQKS KSKQQRTSKR AQQRAESPET SAVESTQSTP QKGRGRPSKT
     PSPSQPKKNI RVGRSKQVAT KENDSSEEMD VLQASSPVSD DTTQEGAEEE DISAGNVRRR
     SSKRERR
//