SURF6_MOUSE
ID SURF6_MOUSE Reviewed; 355 AA.
AC P70279; Q8BPI4; Q8BRL7; Q8R0Q7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Surfeit locus protein 6;
GN Name=Surf6; Synonyms=Surf-6;
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 SUBCELLULAR LOCATION.
RX PubMed=8639267; DOI=10.1089/dna.1996.15.305;
RA Magoulas C., Fried M.;
RT "The Surf-6 gene of the mouse surfeit locus encodes a novel nucleolar
RT protein.";
RL DNA Cell Biol. 15:305-316(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 235-355.
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and 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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9548374; DOI=10.1016/s0171-9335(98)80059-9;
RA Magoulas C., Zatsepina O.V., Jordan P.W., Jordan E.G., Fried M.;
RT "The SURF-6 protein is a component of the nucleolar matrix and has a high
RT binding capacity for nucleic acids in vitro.";
RL Eur. J. Cell Biol. 75:174-183(1998).
RN [5]
RP CITRULLINATION AT ARG-106.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
CC -!- FUNCTION: Binds to both DNA and RNA in vitro, with a stronger binding
CC capacity for RNA. May represent a nucleolar constitutive protein
CC involved in ribosomal biosynthesis or assembly.
CC {ECO:0000269|PubMed:9548374}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:8639267,
CC ECO:0000269|PubMed:9548374}. Note=Granular component of the nucleolus.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including heart,
CC brain, spleen, lung, liver, muscle, kidney and testis.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the SURF6 family. {ECO:0000305}.
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DR EMBL; X92842; CAA63428.1; -; mRNA.
DR EMBL; BC026514; AAH26514.1; -; mRNA.
DR EMBL; BC037634; AAH37634.1; -; mRNA.
DR EMBL; AK043984; BAC31725.1; -; mRNA.
DR EMBL; AK075636; BAC35872.1; -; mRNA.
DR CCDS; CCDS15812.1; -.
DR RefSeq; NP_033324.1; NM_009298.4.
DR AlphaFoldDB; P70279; -.
DR SMR; P70279; -.
DR BioGRID; 203584; 26.
DR STRING; 10090.ENSMUSP00000048457; -.
DR iPTMnet; P70279; -.
DR PhosphoSitePlus; P70279; -.
DR EPD; P70279; -.
DR jPOST; P70279; -.
DR PaxDb; P70279; -.
DR PeptideAtlas; P70279; -.
DR PRIDE; P70279; -.
DR ProteomicsDB; 258781; -.
DR Antibodypedia; 18324; 114 antibodies from 18 providers.
DR DNASU; 20935; -.
DR Ensembl; ENSMUST00000047632; ENSMUSP00000048457; ENSMUSG00000036160.
DR GeneID; 20935; -.
DR KEGG; mmu:20935; -.
DR UCSC; uc008iwc.1; mouse.
DR CTD; 6838; -.
DR MGI; MGI:98447; Surf6.
DR VEuPathDB; HostDB:ENSMUSG00000036160; -.
DR eggNOG; KOG2885; Eukaryota.
DR GeneTree; ENSGT00390000006980; -.
DR HOGENOM; CLU_067122_0_0_1; -.
DR InParanoid; P70279; -.
DR OMA; QKKRTDN; -.
DR OrthoDB; 1153190at2759; -.
DR PhylomeDB; P70279; -.
DR TreeFam; TF321608; -.
DR BioGRID-ORCS; 20935; 19 hits in 72 CRISPR screens.
DR ChiTaRS; Surf6; mouse.
DR PRO; PR:P70279; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P70279; protein.
DR Bgee; ENSMUSG00000036160; Expressed in epiblast (generic) and 260 other tissues.
DR ExpressionAtlas; P70279; baseline and differential.
DR Genevisible; P70279; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0001652; C:granular component; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IBA:GO_Central.
DR GO; GO:0042255; P:ribosome assembly; NAS:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IMP:MGI.
DR InterPro; IPR029190; Rrp14/SURF6_C.
DR InterPro; IPR007019; SURF6.
DR PANTHER; PTHR14369; PTHR14369; 1.
DR Pfam; PF04935; SURF6; 1.
PE 1: Evidence at protein level;
KW Citrullination; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..355
FT /note="Surfeit locus protein 6"
FT /id="PRO_0000220970"
FT REGION 18..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..49
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 152..156
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 53..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..340
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75683"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75683"
SQ SEQUENCE 355 AA; 41235 MW; 8C55841EDD8259B8 CRC64;
MASLLAKDTY LQDLAKKICA QPGPERQRST WGVRTKGSEA AGAPKKKRKK TQKKSPEQEQ
KAMDHKTKAL GKKPPTSSRP KNPMVSKQEK GLSSLGSPKD SQGTARESVF ALDFLRQRLH
EKIQLARGQG STKELSAATL EKRQRRKQER ERKKRKRKER QAKQQVAEAE KKEEPVEVTP
KMACKELQES GLIFNKVEVT EEEPASKAQR KKEKRQKVKG NLTPLTGRNY RQLLDRLQAR
QGRLDELRDQ DAAKAQELEA KMKWTNLLYK AEGVKIRDDE RLLQEALKRK EKRRAQRQRK
WEKRSEHVVE KMQQRQDKRR QNLRKKKAAR AERRLQKAHK KGRVLPQDLE RAGLS
