SRP2_SCHPO
ID SRP2_SCHPO Reviewed; 365 AA.
AC P78814;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Pre-mRNA-splicing factor srp2;
GN Name=srp2; ORFNames=SPAC16.02c;
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 [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=9421507; DOI=10.1093/nar/26.2.505;
RA Gross T., Richert K., Mierke C., Luetzelberger M., Kaeufer N.F.;
RT "Identification and characterization of srp1, a gene of fission yeast
RT encoding a RNA binding domain and a RS domain typical of SR splicing
RT factors.";
RL Nucleic Acids Res. 26:505-511(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-365.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-188; SER-276;
RP SER-294; SER-296; SER-298 AND SER-308, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in pre-mRNA splicing where it is involved in
CC spliceosome assembly. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AF012278; AAC39357.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB57400.1; -; Genomic_DNA.
DR EMBL; D89163; BAA13825.1; -; mRNA.
DR PIR; T37730; T37730.
DR PIR; T42525; T42525.
DR RefSeq; NP_594570.1; NM_001019999.2.
DR AlphaFoldDB; P78814; -.
DR SMR; P78814; -.
DR BioGRID; 279221; 23.
DR STRING; 4896.SPAC16.02c.1; -.
DR iPTMnet; P78814; -.
DR MaxQB; P78814; -.
DR PaxDb; P78814; -.
DR PRIDE; P78814; -.
DR EnsemblFungi; SPAC16.02c.1; SPAC16.02c.1:pep; SPAC16.02c.
DR GeneID; 2542772; -.
DR KEGG; spo:SPAC16.02c; -.
DR PomBase; SPAC16.02c; srp2.
DR VEuPathDB; FungiDB:SPAC16.02c; -.
DR eggNOG; KOG0106; Eukaryota.
DR HOGENOM; CLU_012062_34_5_1; -.
DR InParanoid; P78814; -.
DR OMA; HRMQISG; -.
DR PRO; PR:P78814; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003729; F:mRNA binding; IPI:PomBase.
DR GO; GO:0008143; F:poly(A) binding; ISO:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISO:PomBase.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..365
FT /note="Pre-mRNA-splicing factor srp2"
FT /id="PRO_0000081963"
FT DOMAIN 6..69
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 100..166
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 166..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 365 AA; 42566 MW; 67E988573A736691 CRC64;
MSETRLFVGR IPPQATREDM MDFFKGYGQI LDCKLMNGFG FVEVEDARDA RDIVNDFQGK
EFMGSRIVVE PARGERRRRE NFRESAASKY PRPRRTGFRL IVENLSEDVS WQDLKDVMRK
AGEPTFTDAH RENPGAGVVE FSTEEDMRNA LTSLNGEVIK GQAVTLREDP DAANEPLPEV
PSRFRSRSPP ARRRYRDDYR RGGDYRRDAY RPGRDDERRY APRGEYRRNN RDEYRRGGRD
EYRRNSRSDY RRPHDDEYRR PRGDEYRPGR DEYRRSRDDG RPSHDDEYRR DAYSRSPSPR
RDREENRSPA YEGSKSYSAA PEASMESSAP TESYDKPAAS EEQQPLQNHS DVGNGSAEGQ
VAAEW
