COIL_MOUSE
ID COIL_MOUSE Reviewed; 570 AA.
AC Q5SU73; Q3TK39; Q8K0K5; Q8VIQ2; Q9QXI1;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Coilin;
DE AltName: Full=p80-coilin;
GN Name=Coil; Synonyms=CLN80;
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 [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=10806077; DOI=10.1006/jsbi.2000.4234;
RA Tucker K.E., Massello L.K., Gao L., Barber T.J., Hebert M.D., Chan E.K.L.,
RA Matera A.G.;
RT "Structure and characterization of the murine p80 coilin gene, Coil.";
RL J. Struct. Biol. 129:269-277(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-491.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Lung, and Ovary;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122; SER-171; SER-245;
RP SER-247 AND SER-253, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of nuclear coiled bodies, also known as Cajal
CC bodies or CBs, which are involved in the modification and assembly of
CC nucleoplasmic snRNPs. {ECO:0000250|UniProtKB:P38432}.
CC -!- SUBUNIT: Interacts with ANKS1B. Interacts with SMN1 (via Tudor domain).
CC Interacts (via C-terminus) with AK6. Interacts with WRAP53/TCAB1.
CC Interacts with HMBOX1. Interacts with PSME3; the interaction is
CC inhibited by PSME3IP1. {ECO:0000250|UniProtKB:P38432}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10806077}. Nucleus,
CC Cajal body {ECO:0000250|UniProtKB:P38432}.
CC -!- TISSUE SPECIFICITY: Detectable in all tissues analyzed, with the
CC highest levels in brain and testis. {ECO:0000269|PubMed:10806077}.
CC -!- DOMAIN: The atypical Tudor domain at the C-terminus contains two large
CC unstructured loops, and does not bind methylated residues.
CC {ECO:0000250}.
CC -!- PTM: Symmetrical dimethylation of arginine residues within the RG
CC repeat region enhances affinity for SMN, and thus localization of SMN
CC complexes to CBs. {ECO:0000250}.
CC -!- PTM: Phosphorylation during mitosis is associated with disassembly of
CC CBs. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the coilin family. {ECO:0000305}.
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DR EMBL; AF208663; AAF19644.1; -; mRNA.
DR EMBL; AY047705; AAL32280.1; -; Genomic_DNA.
DR EMBL; AY047703; AAL32280.1; JOINED; Genomic_DNA.
DR EMBL; AY047704; AAL32280.1; JOINED; Genomic_DNA.
DR EMBL; AL646096; CAI24263.1; -; Genomic_DNA.
DR EMBL; CU407331; CAQ52167.1; -; Genomic_DNA.
DR EMBL; CH466556; EDL15867.1; -; Genomic_DNA.
DR EMBL; BC031167; AAH31167.1; -; mRNA.
DR EMBL; AK167167; BAE39306.1; -; mRNA.
DR AlphaFoldDB; Q5SU73; -.
DR IntAct; Q5SU73; 2.
DR MINT; Q5SU73; -.
DR STRING; 10090.ENSMUSP00000103530; -.
DR iPTMnet; Q5SU73; -.
DR PhosphoSitePlus; Q5SU73; -.
DR EPD; Q5SU73; -.
DR jPOST; Q5SU73; -.
DR MaxQB; Q5SU73; -.
DR PaxDb; Q5SU73; -.
DR PRIDE; Q5SU73; -.
DR ProteomicsDB; 285242; -.
DR Antibodypedia; 4307; 330 antibodies from 37 providers.
DR Ensembl; ENSMUST00000107898; ENSMUSP00000103530; ENSMUSG00000033983.
DR MGI; MGI:104842; Coil.
DR VEuPathDB; HostDB:ENSMUSG00000033983; -.
DR eggNOG; ENOG502QVWV; Eukaryota.
DR GeneTree; ENSGT00390000004832; -.
DR HOGENOM; CLU_034553_0_0_1; -.
DR InParanoid; Q5SU73; -.
DR PhylomeDB; Q5SU73; -.
DR ChiTaRS; Coil; mouse.
DR PRO; PR:Q5SU73; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SU73; protein.
DR Bgee; ENSMUSG00000033983; Expressed in spermatid and 248 other tissues.
DR ExpressionAtlas; Q5SU73; baseline and differential.
DR Genevisible; Q5SU73; MM.
DR GO; GO:0015030; C:Cajal body; IDA:MGI.
DR GO; GO:0001674; C:female germ cell nucleus; IDA:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
DR InterPro; IPR024822; Coilin.
DR InterPro; IPR031722; Coilin_N.
DR PANTHER; PTHR15197; PTHR15197; 1.
DR Pfam; PF15862; Coilin_N; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..570
FT /note="Coilin"
FT /id="PRO_0000416045"
FT REPEAT 390..391
FT /note="1"
FT REPEAT 394..395
FT /note="2"
FT REPEAT 405..406
FT /note="3"
FT REPEAT 407..408
FT /note="4"
FT REPEAT 410..411
FT /note="5"
FT REPEAT 412..413
FT /note="6"
FT REPEAT 414..415
FT /note="7"
FT REPEAT 416
FT /note="8"
FT DOMAIN 457..556
FT /note="Tudor; atypical"
FT REGION 119..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..417
FT /note="Required for interaction with SMN"
FT /evidence="ECO:0000250"
FT REGION 390..416
FT /note="8 X 2 AA tandem repeats of R-G"
FT COMPBIAS 119..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 184
FT /note="Phosphoserine; by VRK1 and VRK2"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT CROSSLNK 493
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P38432"
FT CONFLICT 87
FT /note="D -> G (in Ref. 1; AAF19644)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="N -> D (in Ref. 1; AAF19644/AAL32280)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="L -> S (in Ref. 1; AAF19644/AAL32280, 2; CAQ52167,
FT 3; EDL15867 and 4; AAH31167)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="K -> E (in Ref. 1; AAF19644)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="D -> G (in Ref. 1; AAF19644)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="Missing (in Ref. 1; AAF19644/AAL32280, 2; CAQ52167,
FT 3; EDL15867 and 4; AAH31167)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="G -> D (in Ref. 1; AAF19644)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 61917 MW; E9A775185D1556C1 CRC64;
MAASETVRLR LQFDYPPPAT PHCTVFWLLV DLNRCRVVTD LISLIRQRFG FSSGALLGLY
LEGGLLPPAE SARLVRDNDS LRVKLEDQGL PENLIVSNGG DSSFPCRKAK KRAFKLMEDE
ETDQGYKSLK KHCKRQEDSG QNEKASDLET KLLPDETGRT KSKKKSKVTG SPAEEDEEET
KKKSSKRKEK CEPKKQTRAS KSSKQQTPKE GASQNCSFPR ASPRSLGKAR RRSSTGLKGS
SGHLSESESC PESVSDGHCS VMMQEVTFSE KLSAELLKDA PATKTAAANR QASKPGFTFS
SGKGKASRTS SSSSDSSSES EDQFLVSKNM LEGASAGFLK PTGLFAGQGG SGPGLSLETP
GIMGWKSSDS NRGRQAPGPP STPVPTSLGR GWGRGEDLLF GKGLRGRGVR GRGRGRGQAV
SCVFNRSSES QKQRQLNDIL TNSSVVIQNP VEPPKKDYSL LPLLAAAPQV GEKIAFKLLE
LTSDYSPDVS DYKEGKILSH DPETQQVDIE VLSSLPALKE PGKFDLVYHN ENGTEVVEYA
VTQEKRITVL WRELIDPRLI IDSSGSISST
