ID   RIP_MOUSE               Reviewed;         219 AA.
AC   Q9CWY9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=RPA-interacting protein;
GN   Name=Rpain; Synonyms=Rip;
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].
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
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   [4]
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).
CC   -!- FUNCTION: Mediates the import of RPA complex into the nucleus, possibly
CC       via some interaction with importin beta. Sumoylation mediates the
CC       localization of RPA complex into the PML body of the nucleus, thereby
CC       participating in RPA function in DNA metabolism (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the RPA1 subunit of RPA complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- PTM: Sumoylated; required for localization in the nuclear PML body and
CC       transport of RPA complex in PML body. Upon UV irradiation and during S
CC       phase, it is desumoylated, releasing RPA complex that is translocated
CC       to sites of DNA damage. Sumoylation takes place at different Lys
CC       residues (By similarity). {ECO:0000250}.
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DR   EMBL; AK010289; BAB26825.1; -; mRNA.
DR   EMBL; AL596136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC047996; AAH47996.1; -; mRNA.
DR   CCDS; CCDS24969.1; -.
DR   RefSeq; NP_001239342.1; NM_001252413.1.
DR   RefSeq; NP_001239343.1; NM_001252414.1.
DR   RefSeq; NP_001239344.1; NM_001252415.1.
DR   RefSeq; NP_081462.1; NM_027186.2.
DR   AlphaFoldDB; Q9CWY9; -.
DR   STRING; 10090.ENSMUSP00000018593; -.
DR   iPTMnet; Q9CWY9; -.
DR   PhosphoSitePlus; Q9CWY9; -.
DR   MaxQB; Q9CWY9; -.
DR   PaxDb; Q9CWY9; -.
DR   PRIDE; Q9CWY9; -.
DR   ProteomicsDB; 253323; -.
DR   Antibodypedia; 23662; 198 antibodies from 27 providers.
DR   DNASU; 69723; -.
DR   Ensembl; ENSMUST00000018593; ENSMUSP00000018593; ENSMUSG00000018449.
DR   GeneID; 69723; -.
DR   KEGG; mmu:69723; -.
DR   UCSC; uc007jxa.2; mouse.
DR   CTD; 84268; -.
DR   MGI; MGI:1916973; Rpain.
DR   VEuPathDB; HostDB:ENSMUSG00000018449; -.
DR   eggNOG; ENOG502R0QT; Eukaryota.
DR   GeneTree; ENSGT00390000006416; -.
DR   HOGENOM; CLU_086690_0_0_1; -.
DR   InParanoid; Q9CWY9; -.
DR   OMA; EHSTHCP; -.
DR   OrthoDB; 1518754at2759; -.
DR   PhylomeDB; Q9CWY9; -.
DR   TreeFam; TF326215; -.
DR   BioGRID-ORCS; 69723; 20 hits in 107 CRISPR screens.
DR   ChiTaRS; Rpain; mouse.
DR   PRO; PR:Q9CWY9; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9CWY9; protein.
DR   Bgee; ENSMUSG00000018449; Expressed in spermatid and 230 other tissues.
DR   ExpressionAtlas; Q9CWY9; baseline and differential.
DR   Genevisible; Q9CWY9; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016605; C:PML body; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0006310; P:DNA recombination; ISO:MGI.
DR   GO; GO:0006281; P:DNA repair; ISO:MGI.
DR   GO; GO:0006261; P:DNA-templated DNA replication; ISO:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR   GO; GO:0009411; P:response to UV; ISO:MGI.
DR   InterPro; IPR028156; RIP.
DR   InterPro; IPR028159; RPA_interact_C_dom.
DR   InterPro; IPR028155; RPA_interact_central.
DR   InterPro; IPR028158; RPA_interact_N_dom.
DR   PANTHER; PTHR31742; PTHR31742; 1.
DR   Pfam; PF14768; RPA_interact_C; 1.
DR   Pfam; PF14767; RPA_interact_M; 1.
DR   Pfam; PF14766; RPA_interact_N; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..219
FT                   /note="RPA-interacting protein"
FT                   /id="PRO_0000076300"
FT   ZN_FING         137..212
FT                   /note="RIP-type"
FT   REGION          164..180
FT                   /note="Mediates nuclear export"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86UA6"
SQ   SEQUENCE   219 AA;  24897 MW;  6802C83809EB3EAF CRC64;
     MAESSGSPHR LLYKQVGSPH WKETFRQGCL ERMRNSRHRL LNKYRQAAGS TPGTASDRLL
     VQEVMEEEWA SLQSVENCPE ALLQLELPLD LAVLQDIEQE LCNEEKSIIS EYEEDLEFDE
     SCLRRMLAEW EANSLICPVC IKYNLRIMNS VVTCPCGLHI PVHSTDLTEQ KLRACLEENV
     NEHSVHCPHT PVFSVTGGTE EKPSLLMNCL TCDTWAVIL