ID   NUFP1_RAT               Reviewed;         486 AA.
AC   Q641W3;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=FMR1-interacting protein NUFIP1 {ECO:0000250|UniProtKB:Q9UHK0};
DE   AltName: Full=Nuclear FMRP-interacting protein 1;
GN   Name=Nufip1 {ECO:0000312|RGD:1359440};
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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Binds RNA. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with FMR1 (By similarity). Interacts with ZNHIT3 (By
CC       similarity). {ECO:0000250|UniProtKB:Q9UHK0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Distributed in the
CC       nucleus in a dot-like pattern. {ECO:0000250}.
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DR   EMBL; BC082111; AAH82111.1; -; mRNA.
DR   RefSeq; NP_001007759.1; NM_001007758.1.
DR   AlphaFoldDB; Q641W3; -.
DR   STRING; 10116.ENSRNOP00000001366; -.
DR   iPTMnet; Q641W3; -.
DR   PhosphoSitePlus; Q641W3; -.
DR   PaxDb; Q641W3; -.
DR   PRIDE; Q641W3; -.
DR   Ensembl; ENSRNOT00000001366; ENSRNOP00000001366; ENSRNOG00000001033.
DR   GeneID; 364430; -.
DR   KEGG; rno:364430; -.
DR   UCSC; RGD:1359440; rat.
DR   CTD; 26747; -.
DR   RGD; 1359440; Nufip1.
DR   eggNOG; ENOG502QPTB; Eukaryota.
DR   GeneTree; ENSGT00390000003758; -.
DR   HOGENOM; CLU_038059_0_0_1; -.
DR   InParanoid; Q641W3; -.
DR   OMA; KNHKWKN; -.
DR   OrthoDB; 1394860at2759; -.
DR   PhylomeDB; Q641W3; -.
DR   TreeFam; TF329804; -.
DR   PRO; PR:Q641W3; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000001033; Expressed in Ammon's horn and 20 other tissues.
DR   Genevisible; Q641W3; RN.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005726; C:perichromatin fibrils; ISO:RGD.
DR   GO; GO:0070761; C:pre-snoRNP complex; ISO:RGD.
DR   GO; GO:0048786; C:presynaptic active zone; IDA:HGNC-UCL.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0045202; C:synapse; ISO:RGD.
DR   GO; GO:0008023; C:transcription elongation factor complex; ISO:RGD.
DR   GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR   GO; GO:0003723; F:RNA binding; ISO:RGD.
DR   GO; GO:0030515; F:snoRNA binding; IEA:Ensembl.
DR   GO; GO:0000492; P:box C/D snoRNP assembly; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   InterPro; IPR039136; NUFIP1-like.
DR   InterPro; IPR019496; NUFIP1_cons_dom.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR13309:SF1; PTHR13309:SF1; 1.
DR   Pfam; PF10453; NUFIP1; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..486
FT                   /note="FMR1-interacting protein NUFIP1"
FT                   /id="PRO_0000245520"
FT   ZN_FING         167..189
FT                   /note="C2H2-type"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           236..252
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        10..24
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..49
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         331
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHK0"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHK0"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHK0"
FT   MOD_RES         396
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UHK0"
SQ   SEQUENCE   486 AA;  55090 MW;  59C76B6BDAD06D5B CRC64;
     MAEPTPAGWP SAPELTPAPG TPSEAAPPQD NWVYWAMLPP PPPPLSSPVA GTEPCQKEQP
     HVEPQPTSGA FPPFDAQILP AAQPPFDAQA PPDGQSQFND QQAWNFQAST PWYWGLSPNG
     FPTYNTSFHS PATHSYFPQS YANYNDFNLP QNRKQKKKKR KEPVFHFFCD TCDRGFKNQE
     KYDIHMSEHK KCPEVDCSFS AHEKIVQFHW RNMHAPGMKK IKLDTPEDIA RWREERRKNY
     PTLANIERKK LLQLEKEKRG EVLTTTQYGK MKGMSRHSQM AKIRSPGKHY KWKSGGARQR
     AVLGLGNRAR DLKPEIPTKV NVDPLGVLIH SDSESDKDEK SQRAIVPKEV TPALCSLMSS
     YGNVSGSESE PEEAPIKTEA EVLAENRVLP SSPPKSPRHN VRTTARTVLR AKWKAQRSGL
     RKITLKQKKS PCHPLFEPRT RHPHLLEMLL APDIRHERNV ILQCVRYIIK KDFFGLTAGS
     VKTEDV