ID   FCF1_HUMAN              Reviewed;         198 AA.
AC   Q9Y324; Q86TW8; Q8TBL8;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=rRNA-processing protein FCF1 homolog;
GN   Name=FCF1 {ECO:0000312|HGNC:HGNC:20220}; Synonyms=C14orf111;
GN   ORFNames=CGI-35;
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 [LARGE SCALE MRNA].
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neuroblastoma;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [4] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=34516797; DOI=10.1126/science.abj5338;
RA   Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.;
RT   "Nucleolar maturation of the human small subunit processome.";
RL   Science 373:eabj5338-eabj5338(2021).
CC   -!- FUNCTION: Part of the small subunit (SSU) processome, first precursor
CC       of the small eukaryotic ribosomal subunit. During the assembly of the
CC       SSU processome in the nucleolus, many ribosome biogenesis factors, an
CC       RNA chaperone and ribosomal proteins associate with the nascent pre-
CC       rRNA and work in concert to generate RNA folding, modifications,
CC       rearrangements and cleavage as well as targeted degradation of pre-
CC       ribosomal RNA by the RNA exosome. {ECO:0000269|PubMed:34516797}.
CC   -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more
CC       than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3.
CC       {ECO:0000269|PubMed:34516797}.
CC   -!- INTERACTION:
CC       Q9Y324; Q9P287: BCCIP; NbExp=3; IntAct=EBI-5455734, EBI-711154;
CC       Q9Y324; Q5MJ68: SPDYC; NbExp=3; IntAct=EBI-5455734, EBI-12162209;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.
CC   -!- SIMILARITY: Belongs to the UTP23/FCF1 family. FCF1 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD62599.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF132969; AAD27744.1; -; mRNA.
DR   EMBL; BX248271; CAD62599.1; ALT_INIT; mRNA.
DR   EMBL; AC007956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS9832.1; -.
DR   RefSeq; NP_057046.1; NM_015962.4.
DR   PDB; 7MQ8; EM; 3.60 A; SL=1-198.
DR   PDB; 7MQ9; EM; 3.87 A; SL=1-198.
DR   PDB; 7MQA; EM; 2.70 A; SL=1-198.
DR   PDBsum; 7MQ8; -.
DR   PDBsum; 7MQ9; -.
DR   PDBsum; 7MQA; -.
DR   AlphaFoldDB; Q9Y324; -.
DR   EMDB; EMD-23936; -.
DR   EMDB; EMD-23937; -.
DR   EMDB; EMD-23938; -.
DR   SMR; Q9Y324; -.
DR   BioGRID; 119268; 100.
DR   ComplexPortal; CPX-2511; Small ribosomal subunit processome.
DR   IntAct; Q9Y324; 59.
DR   STRING; 9606.ENSP00000344393; -.
DR   iPTMnet; Q9Y324; -.
DR   PhosphoSitePlus; Q9Y324; -.
DR   SwissPalm; Q9Y324; -.
DR   BioMuta; FCF1; -.
DR   DMDM; 34582346; -.
DR   EPD; Q9Y324; -.
DR   jPOST; Q9Y324; -.
DR   MassIVE; Q9Y324; -.
DR   MaxQB; Q9Y324; -.
DR   PaxDb; 9606-ENSP00000344393; -.
DR   PeptideAtlas; Q9Y324; -.
DR   ProteomicsDB; 85964; -.
DR   Pumba; Q9Y324; -.
DR   Antibodypedia; 50547; 34 antibodies from 11 providers.
DR   DNASU; 51077; -.
DR   Ensembl; ENST00000341162.8; ENSP00000344393.4; ENSG00000119616.11.
DR   GeneID; 51077; -.
DR   KEGG; hsa:51077; -.
DR   MANE-Select; ENST00000341162.8; ENSP00000344393.4; NM_015962.5; NP_057046.1.
DR   UCSC; uc001xqh.4; human.
DR   AGR; HGNC:20220; -.
DR   CTD; 51077; -.
DR   DisGeNET; 51077; -.
DR   GeneCards; FCF1; -.
DR   HGNC; HGNC:20220; FCF1.
DR   HPA; ENSG00000119616; Low tissue specificity.
DR   neXtProt; NX_Q9Y324; -.
DR   OpenTargets; ENSG00000119616; -.
DR   PharmGKB; PA162388159; -.
DR   VEuPathDB; HostDB:ENSG00000119616; -.
DR   eggNOG; KOG3165; Eukaryota.
DR   GeneTree; ENSGT00940000153117; -.
DR   InParanoid; Q9Y324; -.
DR   OMA; GMMDCLL; -.
DR   OrthoDB; 5472282at2759; -.
DR   PhylomeDB; Q9Y324; -.
DR   TreeFam; TF314992; -.
DR   PathwayCommons; Q9Y324; -.
DR   Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR   Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   SignaLink; Q9Y324; -.
DR   BioGRID-ORCS; 51077; 756 hits in 1128 CRISPR screens.
DR   ChiTaRS; FCF1; human.
DR   GeneWiki; FCF1; -.
DR   GenomeRNAi; 51077; -.
DR   Pharos; Q9Y324; Tdark.
DR   PRO; PR:Q9Y324; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9Y324; Protein.
DR   Bgee; ENSG00000119616; Expressed in germinal epithelium of ovary and 205 other cell types or tissues.
DR   ExpressionAtlas; Q9Y324; baseline and differential.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:Ensembl.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:Ensembl.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR   CDD; cd09864; PIN_Fcf1-like; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   InterPro; IPR006984; Fcf1/Utp23.
DR   InterPro; IPR037503; Fcf1_PIN.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR002716; PIN_dom.
DR   PANTHER; PTHR12416:SF2; RRNA-PROCESSING PROTEIN FCF1 HOMOLOG; 1.
DR   PANTHER; PTHR12416; UNCHARACTERIZED; 1.
DR   Pfam; PF04900; Fcf1; 1.
DR   SMART; SM00670; PINc; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   Genevisible; Q9Y324; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Reference proteome; Ribosome biogenesis;
KW   rRNA processing.
FT   CHAIN           1..198
FT                   /note="rRNA-processing protein FCF1 homolog"
FT                   /id="PRO_0000089920"
FT   DOMAIN          67..166
FT                   /note="PINc"
FT   REGION          22..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   198 AA;  23370 MW;  A0C98414C21F16AE CRC64;
     MGKQKKTRKY ATMKRMLSLR DQRLKEKDRL KPKKKEKKDP SALKEREVPQ HPSCLFFQYN
     TQLGPPYHIL VDTNFINFSI KAKLDLVQSM MDCLYAKCIP CITDCVMAEI EKLGQKYRVA
     LRIAKDPRFE RLPCTHKGTY ADDCLVQRVT QHKCYIVATV DRDLKRRIRK IPGVPIMYIS
     NHRYNIERMP DDYGAPRF
//