US107_SCHPO
ID US107_SCHPO Reviewed; 695 AA.
AC Q8WZK0; Q9UTX7;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=U1 snRNP-associated protein usp107;
GN Name=usp107; Synonyms=snu71; ORFNames=SPBC839.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 502-620, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP IDENTIFICATION IN THE U1 SNRNP COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND FUNCTION.
RX PubMed=17264129; DOI=10.1093/nar/gkl1144;
RA Newo A.N.S., Luetzelberger M., Bottner C.A., Wehland J., Wissing J.,
RA Jaensch L., Kaeufer N.F.;
RT "Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals
RT three essential organism-specific proteins.";
RL Nucleic Acids Res. 35:1391-1401(2007).
RN [5]
RP INTERACTION WITH PRP5 AND USP102.
RX PubMed=22064476; DOI=10.1128/mcb.06234-11;
RA Shao W., Kim H.S., Cao Y., Xu Y.Z., Query C.C.;
RT "A U1-U2 snRNP interaction network during intron definition.";
RL Mol. Cell. Biol. 32:470-478(2012).
CC -!- FUNCTION: Component of the U1 snRNP particle, which recognizes and
CC binds the 5'-splice site of pre-mRNA. Together with other non-snRNP
CC factors, U1 snRNP forms the spliceosomal commitment complex, that
CC targets pre-mRNA to the splicing pathway.
CC {ECO:0000269|PubMed:17264129}.
CC -!- SUBUNIT: Component of the U1 snRNP particle, a subcomplex of the
CC spliceosome. Interacts with prp5 and usp102.
CC {ECO:0000269|PubMed:17264129, ECO:0000269|PubMed:22064476}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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DR EMBL; CU329671; CAB46703.1; -; Genomic_DNA.
DR EMBL; AB027940; BAA87244.1; -; Genomic_DNA.
DR PIR; T40717; T40717.
DR RefSeq; NP_595250.1; NM_001021156.2.
DR AlphaFoldDB; Q8WZK0; -.
DR SMR; Q8WZK0; -.
DR BioGRID; 277725; 14.
DR IntAct; Q8WZK0; 1.
DR STRING; 4896.SPBC839.10.1; -.
DR iPTMnet; Q8WZK0; -.
DR MaxQB; Q8WZK0; -.
DR PaxDb; Q8WZK0; -.
DR PRIDE; Q8WZK0; -.
DR EnsemblFungi; SPBC839.10.1; SPBC839.10.1:pep; SPBC839.10.
DR GeneID; 2541211; -.
DR KEGG; spo:SPBC839.10; -.
DR PomBase; SPBC839.10; usp107.
DR VEuPathDB; FungiDB:SPBC839.10; -.
DR eggNOG; KOG2253; Eukaryota.
DR HOGENOM; CLU_413975_0_0_1; -.
DR InParanoid; Q8WZK0; -.
DR OMA; DYKEQEC; -.
DR PhylomeDB; Q8WZK0; -.
DR PRO; PR:Q8WZK0; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005685; C:U1 snRNP; IDA:PomBase.
DR GO; GO:0071004; C:U2-type prespliceosome; ISO:PomBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IC:PomBase.
DR CDD; cd12446; RRM_RBM25; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034268; RBM25_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF01480; PWI; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00311; PWI; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51025; PWI; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..695
FT /note="U1 snRNP-associated protein usp107"
FT /id="PRO_0000082027"
FT DOMAIN 139..221
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 605..695
FT /note="PWI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00627"
FT REGION 85..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 265..369
FT /evidence="ECO:0000255"
FT COMPBIAS 86..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 81044 MW; 5B56816D3CEE47BA CRC64;
MQRQNTQAAG MPMMPQVPMV GNGVPYVVPI QPVFAPLPPD YRSLYKKLYG QGAFLVDNPV
EASSPYDFSQ PILKFGKLPI KQVLRDNESQ QKDRKNLPRN QKSNEIQEKQ TFQTPSSEKS
TTERESRPFV PPNSQQMRRM LFIGNIPKEL DDFWMDKILR LSGKLASWRR VADADNSMTS
FGFAEFESNE QFSRALEALN DFVVPPLYEG GPSTRLSLIT DVENEGLYRE WQTSRYARNK
QKEINILQQI RFNLERICQD IGNFDVRSRI ERAARQAREK NEKLLQNVKT SEIPINAADL
EGINPELLPV IEEEIRSFRD QSAMKKREKQ RSKDEYASLY KEYTRKEQEK LRKQNDDLQN
LLSKHRISRI PMSTVNAFLR AEDSIPESFS DEQAYYEEKR RKDQLEAEEY YARERRWMNR
EKARTAALER EAAREEEERV NNTSFGTYLS EKLASFDDDE EARVSRDEYF VDRAAWIRHR
AVARAREEDA DALDRKEEER ELRTRGEGAT VETENYVENG KLVTSEMPQH ENGPFKIKIQ
TKKPAVPSER REFGLPERLL LEEEDEEPQG YSPNPQKPKP AMEENDAEKT KRLRSLIEKI
PVEAESLWAL PIDWSKVTED LLKEEMQAFV TKKIIEYIGI QEDSLITFTI DHIRQHKGAE
QLVSELDLAL AEDAPEFVSK VYRYLHVLLI LRSEA
