CDCA5_MOUSE
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 03-AUG-2022, entry version 144.
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}.
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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; Q9CPY3; -.
DR PeptideAtlas; Q9CPY3; -.
DR PRIDE; Q9CPY3; -.
DR ProteomicsDB; 281277; -. [Q9CPY3-1]
DR ProteomicsDB; 281278; -. [Q9CPY3-2]
DR Antibodypedia; 15765; 105 antibodies from 19 providers.
DR Ensembl; ENSMUST00000025704; ENSMUSP00000025704; ENSMUSG00000024791. [Q9CPY3-1]
DR GeneID; 67849; -.
DR KEGG; mmu:67849; -.
DR UCSC; uc008ghh.1; mouse. [Q9CPY3-1]
DR UCSC; uc008ghi.1; mouse. [Q9CPY3-2]
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; 1454872at2759; -.
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 109 CRISPR screens.
DR PRO; PR:Q9CPY3; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9CPY3; protein.
DR Bgee; ENSMUSG00000024791; Expressed in primary oocyte and 189 other tissues.
DR Genevisible; Q9CPY3; MM.
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 plate congression; 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 GO; GO:0071922; P:regulation of cohesin loading; ISS:UniProtKB.
DR InterPro; IPR018605; Sororin.
DR PANTHER; PTHR31092; PTHR31092; 1.
DR Pfam; PF09666; Sororin; 1.
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
