PDS5B_RAT
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 25-MAY-2022, entry version 95.
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
RC Wistar {ECO:0000312|EMBL:AAW69306.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAW69306.1}, and
RC Testis {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; Q6TRW4; -.
DR PeptideAtlas; Q6TRW4; -.
DR PRIDE; Q6TRW4; -.
DR UCSC; RGD:1310838; rat. [Q6TRW4-1]
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:0006281; P:DNA repair; IBA:GO_Central.
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:0097402; P:neuroblast migration; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039776; Pds5.
DR PANTHER; PTHR12663; PTHR12663; 1.
DR SUPFAM; SSF48371; SSF48371; 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
