RIP_RAT
ID RIP_RAT Reviewed; 219 AA.
AC Q4G2Y1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=RPA-interacting protein;
GN Name=Rpain; Synonyms=Rip;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=16008515; DOI=10.1089/dna.2005.24.464;
RA Chen J.-Z., Huang S.-D., Ji C.-N., Pang R.-Y., Xie Y., Xue J.-L.;
RT "Identification, expression pattern, and subcellular location of human RIP
RT isoforms.";
RL DNA Cell Biol. 24:464-469(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-219 (ISOFORM 1).
RX PubMed=15277470; DOI=10.1167/iovs.03-1391;
RA Farkas R.H., Qian J., Goldberg J.L., Quigley H.A., Zack D.J.;
RT "Gene expression profiling of purified rat retinal ganglion cells.";
RL Invest. Ophthalmol. Vis. Sci. 45:2503-2513(2004).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4G2Y1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4G2Y1-2; Sequence=VSP_016411;
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; AY775322; AAX14376.1; -; mRNA.
DR EMBL; AABR03073214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CF978727; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001028232.1; NM_001033060.1. [Q4G2Y1-1]
DR RefSeq; XP_006246730.1; XM_006246668.3. [Q4G2Y1-1]
DR AlphaFoldDB; Q4G2Y1; -.
DR STRING; 10116.ENSRNOP00000009082; -.
DR iPTMnet; Q4G2Y1; -.
DR PhosphoSitePlus; Q4G2Y1; -.
DR PaxDb; Q4G2Y1; -.
DR Ensembl; ENSRNOT00000009082; ENSRNOP00000009082; ENSRNOG00000006913. [Q4G2Y1-1]
DR Ensembl; ENSRNOT00000044363; ENSRNOP00000040269; ENSRNOG00000006913. [Q4G2Y1-2]
DR GeneID; 287463; -.
DR KEGG; rno:287463; -.
DR UCSC; RGD:1308492; rat. [Q4G2Y1-1]
DR CTD; 84268; -.
DR RGD; 1308492; Rpain.
DR eggNOG; ENOG502R0QT; Eukaryota.
DR GeneTree; ENSGT00390000006416; -.
DR HOGENOM; CLU_086690_0_0_1; -.
DR InParanoid; Q4G2Y1; -.
DR OMA; EHSTHCP; -.
DR OrthoDB; 1518754at2759; -.
DR PhylomeDB; Q4G2Y1; -.
DR TreeFam; TF326215; -.
DR PRO; PR:Q4G2Y1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000006913; Expressed in skeletal muscle tissue and 19 other tissues.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0006310; P:DNA recombination; ISO:RGD.
DR GO; GO:0006281; P:DNA repair; ISO:RGD.
DR GO; GO:0006261; P:DNA-templated DNA replication; ISO:RGD.
DR GO; GO:0006606; P:protein import into nucleus; ISO:RGD.
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 2: Evidence at transcript level;
KW Alternative splicing; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..219
FT /note="RPA-interacting protein"
FT /id="PRO_0000076301"
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"
FT VAR_SEQ 212..219
FT /note="CDTWAVIL -> YKLHC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16008515"
FT /id="VSP_016411"
FT CONFLICT 43
FT /note="R -> T (in Ref. 3; CF978727)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="R -> G (in Ref. 3; CF978727)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 24710 MW; E24EAF7CABEA2A8D CRC64;
MAESSGSPHR LLYKQVGSPP WKETFRQGCL ERMRNSRHKL LNRYRQAAGS TLGTASDRLL
VQEVMEEEWN SLQSVENCPE ALLQLELPLN LAVLQDIEQE LWNEEKSIIS EYEKGLQFDE
SCLNSMLAEW EANPLICPVC IKYNLRIMNS VVTCPCGLHI PSHSTDLTEQ KLRACLEGNV
NEHSAHCPHI PEFSVTGGTE EKPSLLMSCL ACDTWAVIL