ID CDCA5_MOUSE Reviewed; 264 AA. AC Q9CPY3; Q78HI6; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 24-JAN-2024, entry version 151. DE RecName: Full=Sororin; DE AltName: Full=Cell division cycle-associated protein 5; GN Name=Cdca5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [4] RP FUNCTION, INTERACTION WITH PDS5A AND PDS5B, AND SUBCELLULAR LOCATION. RX PubMed=21111234; DOI=10.1016/j.cell.2010.10.031; RA Nishiyama T., Ladurner R., Schmitz J., Kreidl E., Schleiffer A., RA Bhaskara V., Bando M., Shirahige K., Hyman A.A., Mechtler K., Peters J.M.; RT "Sororin mediates sister chromatid cohesion by antagonizing wapl."; RL Cell 143:737-749(2010). CC -!- FUNCTION: Regulator of sister chromatid cohesion in mitosis stabilizing CC cohesin complex association with chromatin. May antagonize the action CC of WAPL which stimulates cohesin dissociation from chromatin. Cohesion CC ensures that chromosome partitioning is accurate in both meiotic and CC mitotic cells and plays an important role in DNA repair. Required for CC efficient DNA double-stranded break repair. CC {ECO:0000269|PubMed:21111234}. CC -!- SUBUNIT: Interacts with the APC/C complex (By similarity). Interacts CC with the chromatin-bound cohesin complex; the interaction is indirect, CC occurs after DNA replication and requires acetylation of the cohesin CC component SMC3. Interacts (via the FGF motif) with PDS5A and PDS5B; the CC interaction is direct and prevents the interaction of PDS5A with WAPL. CC {ECO:0000250, ECO:0000269|PubMed:21111234}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21111234}. Chromosome CC {ECO:0000269|PubMed:21111234}. Cytoplasm {ECO:0000269|PubMed:21111234}. CC Note=Associates with nuclear chromatin from S phase until metaphase and CC is released in the cytoplasm upon nuclear envelope breakdown. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9CPY3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9CPY3-2; Sequence=VSP_014402; CC -!- DOMAIN: The KEN box is required for the association with the APC/C CC complex. {ECO:0000250}. CC -!- PTM: Phosphorylated. Phosphorylation, as cells enter mitosis, disrupts CC the interaction with PDS5A and relieves the inhibition of WAPL by CDCA5 CC (By similarity). {ECO:0000250}. CC -!- PTM: Ubiquitinated by the APC/C complex in G1, leading to its CC degradation. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the sororin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK010540; BAB27016.1; -; mRNA. DR EMBL; AK011701; BAB27788.1; -; mRNA. DR EMBL; BC029626; AAH29626.1; -; mRNA. DR EMBL; BC052904; AAH52904.1; -; mRNA. DR CCDS; CCDS29493.1; -. [Q9CPY3-1] DR RefSeq; NP_080686.1; NM_026410.3. [Q9CPY3-1] DR AlphaFoldDB; Q9CPY3; -. DR SMR; Q9CPY3; -. DR BioGRID; 212479; 21. DR IntAct; Q9CPY3; 20. DR STRING; 10090.ENSMUSP00000025704; -. DR iPTMnet; Q9CPY3; -. DR PhosphoSitePlus; Q9CPY3; -. DR EPD; Q9CPY3; -. DR jPOST; Q9CPY3; -. DR MaxQB; Q9CPY3; -. DR PaxDb; 10090-ENSMUSP00000025704; -. DR PeptideAtlas; Q9CPY3; -. DR ProteomicsDB; 281277; -. [Q9CPY3-1] DR ProteomicsDB; 281278; -. [Q9CPY3-2] DR Pumba; Q9CPY3; -. DR Antibodypedia; 15765; 152 antibodies from 20 providers. DR Ensembl; ENSMUST00000025704.3; ENSMUSP00000025704.3; ENSMUSG00000024791.11. [Q9CPY3-1] DR GeneID; 67849; -. DR KEGG; mmu:67849; -. DR UCSC; uc008ghh.1; mouse. [Q9CPY3-1] DR UCSC; uc008ghi.1; mouse. [Q9CPY3-2] DR AGR; MGI:1915099; -. DR CTD; 113130; -. DR MGI; MGI:1915099; Cdca5. DR VEuPathDB; HostDB:ENSMUSG00000024791; -. DR eggNOG; ENOG502S4XG; Eukaryota. DR GeneTree; ENSGT00390000010028; -. DR HOGENOM; CLU_088614_0_0_1; -. DR InParanoid; Q9CPY3; -. DR OMA; KKVQQID; -. DR OrthoDB; 4642808at2759; -. DR PhylomeDB; Q9CPY3; -. DR TreeFam; TF101070; -. DR Reactome; R-MMU-2467813; Separation of Sister Chromatids. DR Reactome; R-MMU-2468052; Establishment of Sister Chromatid Cohesion. DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion. DR BioGRID-ORCS; 67849; 30 hits in 114 CRISPR screens. DR PRO; PR:Q9CPY3; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; Q9CPY3; Protein. DR Bgee; ENSMUSG00000024791; Expressed in primary oocyte and 193 other cell types or tissues. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB. DR GO; GO:0007076; P:mitotic chromosome condensation; ISS:UniProtKB. DR GO; GO:0007080; P:mitotic metaphase chromosome alignment; ISS:UniProtKB. DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IGI:UniProtKB. DR GO; GO:0031536; P:positive regulation of exit from mitosis; ISO:MGI. DR InterPro; IPR018605; Sororin. DR PANTHER; PTHR31092; SORORIN; 1. DR PANTHER; PTHR31092:SF2; SORORIN; 1. DR Pfam; PF09666; Sororin; 1. DR Genevisible; Q9CPY3; MM. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Cell division; Chromosome; Cytoplasm; KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..264 FT /note="Sororin" FT /id="PRO_0000089450" FT REGION 1..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 87..89 FT /note="KEN box" FT MOTIF 166..168 FT /note="FGF motif" FT COMPBIAS 12..45 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96FF9" FT MOD_RES 32 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96FF9" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96FF9" FT MOD_RES 78 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96FF9" FT MOD_RES 82 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96FF9" FT MOD_RES 97 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q96FF9" FT MOD_RES 106 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96FF9" FT MOD_RES 110 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q96FF9" FT MOD_RES 114 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q96FF9" FT MOD_RES 159 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q96FF9" FT MOD_RES 222 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96FF9" FT VAR_SEQ 1..137 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014402" SQ SEQUENCE 264 AA; 28991 MW; E8543BBE3593B212 CRC64; MAERRTRSGG AAQRSGPRTS LTKPSKSSKR KSGSDLPNSF SEIWPRTTPA VPVRKAIVLK KIVAHAVEVP DVHTVRRSPR ISFILEKENN PPLKVPTKED LFKTCSVPGT PSSTPVLYTQ NVEPDSGEAE LDSRDLEMSQ KVRRSYSRLQ SLGCASTSTP GRRSFFGFEG PDDLPGVSPV VCSKLIETPK VPAKDLVPAR TKDLVPDSTK DLVPARTLPG ISPPVVKEKR KKKVPEILKS ELDKWAVAMN AEFEAAEQFE LLIE //