ID RFPLA_MOUSE Reviewed; 287 AA.
AC Q8VH31; Q6IS67;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 24-JAN-2024, entry version 139.
DE RecName: Full=Ret finger protein-like 4A;
GN Name=Rfpl4a; Synonyms=Rfpl4;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11850190; DOI=10.1016/s0925-4773(01)00635-9;
RA Rajkovic A., Lee J.H., Yan C., Matzuk M.M.;
RT "The ret finger protein-like 4 gene, Rfpl4, encodes a putative E3
RT ubiquitin-protein ligase expressed in adult germ cells.";
RL Mech. Dev. 112:173-177(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Oocyte;
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 [5]
RP INTERACTION WITH PSMB1; UBE2A AND CCNB1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12525704; DOI=10.1073/pnas.0234474100;
RA Suzumori N., Burns K.H., Yan W., Matzuk M.M.;
RT "RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome
RT degradation pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:550-555(2003).
CC -!- SUBUNIT: Interacts with PSMB1, UBE2A and CCNB1.
CC {ECO:0000269|PubMed:12525704}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12525704}. Nucleus
CC {ECO:0000269|PubMed:12525704}.
CC -!- TISSUE SPECIFICITY: Expressed in the ovaries and oocytes (at protein
CC level) (PubMed:12525704, PubMed:11850190). Expression restricted to
CC gonads. In testis, present at later stages of spermatogeneis and
CC abundant in elongating spermatids. {ECO:0000269|PubMed:11850190,
CC ECO:0000269|PubMed:12525704}.
CC -!- DEVELOPMENTAL STAGE: Expressed in growing oocytes and early embryos.
CC {ECO:0000269|PubMed:12525704}.
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DR EMBL; AY070253; AAL55432.1; -; mRNA.
DR EMBL; AK136022; BAE22777.1; -; mRNA.
DR EMBL; CH466627; EDL31289.1; -; Genomic_DNA.
DR EMBL; CH466627; EDL31290.1; -; Genomic_DNA.
DR EMBL; BC069834; AAH69834.1; -; mRNA.
DR CCDS; CCDS20759.1; -.
DR RefSeq; NP_001138485.1; NM_001145013.1.
DR RefSeq; NP_620404.1; NM_138954.3.
DR AlphaFoldDB; Q8VH31; -.
DR SMR; Q8VH31; -.
DR BioGRID; 228699; 3.
DR STRING; 10090.ENSMUSP00000039519; -.
DR REPRODUCTION-2DPAGE; Q8VH31; -.
DR PaxDb; 10090-ENSMUSP00000039519; -.
DR DNASU; 192658; -.
DR Ensembl; ENSMUST00000045215.9; ENSMUSP00000039519.8; ENSMUSG00000035191.16.
DR Ensembl; ENSMUST00000179971.8; ENSMUSP00000136497.2; ENSMUSG00000035191.16.
DR GeneID; 192658; -.
DR KEGG; mmu:192658; -.
DR UCSC; uc009faa.2; mouse.
DR AGR; MGI:2149590; -.
DR CTD; 192658; -.
DR MGI; MGI:2149590; Rfpl4.
DR VEuPathDB; HostDB:ENSMUSG00000035191; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000163220; -.
DR HOGENOM; CLU_013137_7_1_1; -.
DR InParanoid; Q8VH31; -.
DR OMA; RPFFSHK; -.
DR OrthoDB; 4508030at2759; -.
DR PhylomeDB; Q8VH31; -.
DR TreeFam; TF317532; -.
DR BioGRID-ORCS; 192658; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Rfpl4; mouse.
DR PRO; PR:Q8VH31; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8VH31; Protein.
DR Bgee; ENSMUSG00000035191; Expressed in animal zygote and 12 other cell types or tissues.
DR ExpressionAtlas; Q8VH31; baseline and differential.
DR Genevisible; Q8VH31; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0001674; C:female germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR CDD; cd15821; SPRY_PRY_RFPL; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR022723; RDM_domain_RFPL.
DR InterPro; IPR037960; SPRY/PRY_RFPL.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF666; RET FINGER PROTEIN-LIKE 4A-RELATED; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF11002; RDM; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF15227; zf-C3HC4_4; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..287
FT /note="Ret finger protein-like 4A"
FT /id="PRO_0000394967"
FT DOMAIN 78..278
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 11..53
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 184
FT /note="N -> S (in Ref. 4; AAH69834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 32358 MW; 7197FABEEF3D8629 CRC64;
MAHLFKEKSN CYFCFRCLES PVYLNCGYIC CLKCLDSLEK SPEGDGVLCP TCSVVSLKED
IIHAKQLGAL VTKIKNLEPQ LNFILTMDQG MKIFQVTMTL DVDTAQNHLI ISDDLLSVYY
TPQKQARKKC AERFHPSPCV LGSSRFTSGR HYWEVVVGTS KEWDIGICKE SINRKKAIHL
SEKNGFWTVG VRAKKVYSAS TDPLTVLRVN PRLRRVGIFL DMLEKSVSFW DLSDGSHIYT
FLEIPDTDPF RPFFSPASSY PDGDQEQVLS ICPVTNPGIF GIPVNPQ
//
