ID   FCF1_MOUSE              Reviewed;         198 AA.
AC   Q9CTH6; Q505C6; Q8K261;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-SEP-2003, sequence version 2.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=rRNA-processing protein FCF1 homolog;
GN   Name=Fcf1;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-198.
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).
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:0000250|UniProtKB:Q9Y324}.
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:0000250|UniProtKB:Q9Y324}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9Y324}.
CC   -!- SIMILARITY: Belongs to the UTP23/FCF1 family. FCF1 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH33045.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC033045; AAH33045.1; ALT_TERM; mRNA.
DR   EMBL; BC094619; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK003561; BAB22857.1; -; mRNA.
DR   CCDS; CCDS49113.1; -.
DR   RefSeq; NP_082908.2; NM_028632.2.
DR   AlphaFoldDB; Q9CTH6; -.
DR   SMR; Q9CTH6; -.
DR   BioGRID; 216221; 1.
DR   STRING; 10090.ENSMUSP00000021669; -.
DR   PhosphoSitePlus; Q9CTH6; -.
DR   EPD; Q9CTH6; -.
DR   jPOST; Q9CTH6; -.
DR   MaxQB; Q9CTH6; -.
DR   PaxDb; 10090-ENSMUSP00000021669; -.
DR   ProteomicsDB; 271888; -.
DR   Pumba; Q9CTH6; -.
DR   DNASU; 73736; -.
DR   Ensembl; ENSMUST00000021669.15; ENSMUSP00000021669.9; ENSMUSG00000021243.15.
DR   GeneID; 73736; -.
DR   KEGG; mmu:73736; -.
DR   UCSC; uc007ogc.2; mouse.
DR   AGR; MGI:1920986; -.
DR   CTD; 51077; -.
DR   MGI; MGI:1920986; Fcf1.
DR   VEuPathDB; HostDB:ENSMUSG00000021243; -.
DR   eggNOG; KOG3165; Eukaryota.
DR   GeneTree; ENSGT00940000153117; -.
DR   InParanoid; Q9CTH6; -.
DR   OMA; GMMDCLL; -.
DR   OrthoDB; 5472282at2759; -.
DR   PhylomeDB; Q9CTH6; -.
DR   TreeFam; TF314992; -.
DR   Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   BioGRID-ORCS; 73736; 28 hits in 78 CRISPR screens.
DR   ChiTaRS; Fcf1; mouse.
DR   PRO; PR:Q9CTH6; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q9CTH6; Protein.
DR   Bgee; ENSMUSG00000021243; Expressed in primary oocyte and 69 other cell types or tissues.
DR   ExpressionAtlas; Q9CTH6; baseline and differential.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:MGI.
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); IMP:MGI.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS: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; Q9CTH6; MM.
PE   2: Evidence at transcript level;
KW   Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..198
FT                   /note="rRNA-processing protein FCF1 homolog"
FT                   /id="PRO_0000089921"
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;  23341 MW;  FBEC2ABABC12C109 CRC64;
     MGKQKKTRKY ATMKRMLSLR DERLKEKDRL KPKKKEKKDP SALKEREVPQ HPSCLFFQYN
     TQLGPPYHIL VDTNFINFSI KAKLDLVQSM MDCLYAKCIP CITDCVMAEI EKLGQKFRVA
     LRIAKDPRFD RLPCTHKGTY ADDCLVQRVT QHKCYIVATV DRDLKRRIRK IPGVPIMYLS
     NHRYNIERMP DDYGAPRF
//