RFPL3_HUMAN
ID RFPL3_HUMAN Reviewed; 317 AA.
AC O75679; A2A279; Q6IC03; Q6IC04; Q6NSX3; Q8N5R4;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Ret finger protein-like 3;
GN Name=RFPL3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10508838; DOI=10.1101/gr.9.9.803;
RA Seroussi E., Kedra D., Pan H.-Q., Peyrad M., Schwartz C., Scambler P.,
RA Donnai D., Roe B.A., Dumanski J.P.;
RT "Duplications on human chromosome 22 reveal a novel Ret finger protein-like
RT gene family with sense and endogenous antisense transcripts.";
RL Genome Res. 9:803-814(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP MET-110.
RC TISSUE=Brain;
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 TISSUE SPECIFICITY.
RX PubMed=18656177; DOI=10.1016/j.ajhg.2008.07.007;
RA Bonnefont J., Nikolaev S.I., Perrier A.L., Guo S., Cartier L., Sorce S.,
RA Laforge T., Aubry L., Khaitovich P., Peschanski M., Antonarakis S.E.,
RA Krause K.H.;
RT "Evolutionary forces shape the human RFPL1,2,3 genes toward a role in
RT neocortex development.";
RL Am. J. Hum. Genet. 83:208-218(2008).
RN [6]
RP FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=25107902; DOI=10.1074/jbc.m114.561662;
RA Tan B.H., Suzuki Y., Takahashi H., Ying P.H., Takahashi C., Han Q.,
RA Chin W.X., Chao S.H., Sawasaki T., Yamamoto N., Suzuki Y.;
RT "Identification of RFPL3 protein as a novel E3 ubiquitin ligase modulating
RT the integration activity of human immunodeficiency virus, type 1
RT preintegration complex using a microtiter plate-based assay.";
RL J. Biol. Chem. 289:26368-26382(2014).
CC -!- FUNCTION: (Microbial infection) Stimulates the activity of Human
CC Immunodeficiency Virus 1/HIV-1 pre-integration complex.
CC {ECO:0000269|PubMed:25107902}.
CC -!- INTERACTION:
CC O75679; Q6ZUJ4: C3orf62; NbExp=3; IntAct=EBI-10188956, EBI-2837036;
CC O75679; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-10188956, EBI-742054;
CC O75679; P47813: EIF1AX; NbExp=3; IntAct=EBI-10188956, EBI-1045377;
CC O75679; Q16082: HSPB2; NbExp=4; IntAct=EBI-10188956, EBI-739395;
CC O75679; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10188956, EBI-739832;
CC O75679; Q9NQP4: PFDN4; NbExp=3; IntAct=EBI-10188956, EBI-357021;
CC O75679; Q8WVV4-1: POF1B; NbExp=3; IntAct=EBI-10188956, EBI-11986735;
CC O75679; Q92546: RGP1; NbExp=3; IntAct=EBI-10188956, EBI-2823702;
CC O75679; Q8ND83: SLAIN1; NbExp=5; IntAct=EBI-10188956, EBI-10269374;
CC O75679; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-10188956, EBI-10180829;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25107902}. Nucleus
CC {ECO:0000269|PubMed:25107902}. Note=A higher concentration of RFPL3 is
CC observed in the cytoplasm compared to the nucleus.
CC {ECO:0000269|PubMed:25107902}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75679-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75679-2; Sequence=VSP_045651;
CC -!- TISSUE SPECIFICITY: Expressed during neurogenesis in differentiating
CC human embryonic stem cells and in the developing human neocortex.
CC {ECO:0000269|PubMed:18656177}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA09046.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ010232; CAA09046.1; ALT_INIT; mRNA.
DR EMBL; CR456564; CAG30450.1; -; mRNA.
DR EMBL; AL021937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031689; AAH31689.1; -; mRNA.
DR EMBL; BC069753; AAH69753.2; -; mRNA.
DR CCDS; CCDS13904.1; -. [O75679-2]
DR CCDS; CCDS43011.1; -. [O75679-1]
DR RefSeq; NP_001092005.1; NM_001098535.1. [O75679-1]
DR RefSeq; NP_006595.1; NM_006604.2. [O75679-2]
DR AlphaFoldDB; O75679; -.
DR SMR; O75679; -.
DR BioGRID; 115961; 19.
DR IntAct; O75679; 15.
DR STRING; 9606.ENSP00000249007; -.
DR iPTMnet; O75679; -.
DR PhosphoSitePlus; O75679; -.
DR BioMuta; RFPL3; -.
DR MassIVE; O75679; -.
DR PaxDb; O75679; -.
DR PeptideAtlas; O75679; -.
DR PRIDE; O75679; -.
DR Antibodypedia; 11237; 186 antibodies from 22 providers.
DR DNASU; 10738; -.
DR Ensembl; ENST00000249007.4; ENSP00000249007.4; ENSG00000128276.10. [O75679-1]
DR Ensembl; ENST00000397468.5; ENSP00000380609.1; ENSG00000128276.10. [O75679-2]
DR GeneID; 10738; -.
DR KEGG; hsa:10738; -.
DR MANE-Select; ENST00000249007.4; ENSP00000249007.4; NM_001098535.1; NP_001092005.1.
DR UCSC; uc003amj.3; human. [O75679-1]
DR CTD; 10738; -.
DR DisGeNET; 10738; -.
DR GeneCards; RFPL3; -.
DR HGNC; HGNC:9980; RFPL3.
DR HPA; ENSG00000128276; Tissue enriched (testis).
DR MIM; 605970; gene.
DR neXtProt; NX_O75679; -.
DR OpenTargets; ENSG00000128276; -.
DR PharmGKB; PA34349; -.
DR VEuPathDB; HostDB:ENSG00000128276; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000163408; -.
DR HOGENOM; CLU_013137_7_1_1; -.
DR InParanoid; O75679; -.
DR OMA; RSGCIRH; -.
DR OrthoDB; 1139938at2759; -.
DR PhylomeDB; O75679; -.
DR TreeFam; TF317532; -.
DR PathwayCommons; O75679; -.
DR SignaLink; O75679; -.
DR BioGRID-ORCS; 10738; 5 hits in 1031 CRISPR screens.
DR GenomeRNAi; 10738; -.
DR Pharos; O75679; Tbio.
DR PRO; PR:O75679; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O75679; protein.
DR Bgee; ENSG00000128276; Expressed in buccal mucosa cell and 59 other tissues.
DR Genevisible; O75679; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd15821; SPRY_PRY_RFPL; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 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; IPR038908; 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; PTHR25462:SF279; PTHR25462:SF279; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF11002; RDM; 1.
DR Pfam; PF00622; SPRY; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Host-virus interaction; Metal-binding;
KW Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..317
FT /note="Ret finger protein-like 3"
FT /id="PRO_0000056032"
FT DOMAIN 107..301
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 40..82
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045651"
FT VARIANT 83
FT /note="M -> T (in dbSNP:rs16987625)"
FT /id="VAR_052091"
FT VARIANT 110
FT /note="L -> M (in dbSNP:rs9621427)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052092"
FT VARIANT 126
FT /note="D -> N (in dbSNP:rs9619258)"
FT /id="VAR_052093"
FT VARIANT 181
FT /note="Y -> C (in dbSNP:rs5749408)"
FT /id="VAR_059814"
SQ SEQUENCE 317 AA; 35386 MW; 6C27D4829924D2FB CRC64;
MKRLSLVTTN RLSPQGNFLP LCTFPLAVDM AALFQEASSC PVCSDYLEKP MSLECGCTVC
LKCINSLQKE PHGEDLLCCC CSMVSQRNKI RPNRQLERLV SHIKELEPKL KKILQMNPRM
RKFQVDMTLD ADTANNFLLI SDDLRSVRSG LITQNRQDLA ERFDVSVCIL GSPRFTCGRH
YWEVDVGTST EWDLGVCRES VHCKGKIQLT TELGFWTVSL RDGSRLSAST VPLTFLLVDR
KLQRVGIFLD MGMQNVSFFD AESGSHVYTF RSVSAEEPLR PFLAPSIPPN GDQGVLSICP
LMNSGTTDAP VRPGEAK
