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Database: UniProt
Entry: SMD1_SCHPO
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ID   SMD1_SCHPO              Reviewed;         117 AA.
AC   O42661;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Small nuclear ribonucleoprotein Sm D1;
DE            Short=Sm-D1;
DE   AltName: Full=snRNP core protein D1;
GN   Name=smd1; ORFNames=SPAC27D7.07c;
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   IDENTIFICATION IN THE CWF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA   Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT   "Proteomics analysis reveals stable multiprotein complexes in both fission
RT   and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT   splicing factors, and snRNAs.";
RL   Mol. Cell. Biol. 22:2011-2024(2002).
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   INTERACTION WITH SAF5.
RX   PubMed=24298023; DOI=10.1128/mcb.01407-13;
RA   Barbarossa A., Antoine E., Neel H., Gostan T., Soret J., Bordonne R.;
RT   "Characterization and in vivo functional analysis of the
RT   Schizosaccharomyces pombe ICLN gene.";
RL   Mol. Cell. Biol. 34:595-605(2014).
CC   -!- FUNCTION: Plays a role in pre-mRNA splicing as a core component of the
CC       spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins
CC       (snRNPs), the building blocks of the spliceosome (By similarity).
CC       {ECO:0000250|UniProtKB:P62314}.
CC   -!- SUBUNIT: Belongs to the 40S cdc5-associated complex (or cwf complex), a
CC       spliceosome sub-complex reminiscent of a late-stage spliceosome
CC       composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5,
CC       cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27,
CC       cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16,
CC       cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26,
CC       cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10,
CC       prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1,
CC       smd1, smd3, smf1, smg1 and syf2 (PubMed:11884590). Interacts with saf5;
CC       the interaction is direct (PubMed:24298023).
CC       {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:24298023}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372,
CC       ECO:0000269|PubMed:24298023}. Cytoplasm {ECO:0000269|PubMed:16823372,
CC       ECO:0000269|PubMed:24298023}. Note=Localizes to the nucleus
CC       predominantly. {ECO:0000269|PubMed:24298023}.
CC   -!- SIMILARITY: Belongs to the snRNP core protein family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA15826.1; -; Genomic_DNA.
DR   PIR; T38440; T38440.
DR   RefSeq; NP_594613.1; NM_001020041.2.
DR   PDB; 3JB9; EM; 3.60 A; F/f=1-117.
DR   PDBsum; 3JB9; -.
DR   AlphaFoldDB; O42661; -.
DR   SMR; O42661; -.
DR   BioGRID; 279143; 25.
DR   IntAct; O42661; 7.
DR   STRING; 284812.O42661; -.
DR   MaxQB; O42661; -.
DR   PaxDb; 4896-SPAC27D7-07c-1; -.
DR   EnsemblFungi; SPAC27D7.07c.1; SPAC27D7.07c.1:pep; SPAC27D7.07c.
DR   GeneID; 2542690; -.
DR   KEGG; spo:SPAC27D7.07c; -.
DR   PomBase; SPAC27D7.07c; smd1.
DR   VEuPathDB; FungiDB:SPAC27D7.07c; -.
DR   eggNOG; KOG3428; Eukaryota.
DR   HOGENOM; CLU_123956_3_0_1; -.
DR   InParanoid; O42661; -.
DR   OMA; TFLMKLT; -.
DR   PhylomeDB; O42661; -.
DR   PRO; PR:O42661; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0000243; C:commitment complex; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0034715; C:pICln-Sm protein complex; IBA:GO_Central.
DR   GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR   GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR   GO; GO:0034719; C:SMN-Sm protein complex; IBA:GO_Central.
DR   GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR   GO; GO:0005685; C:U1 snRNP; IDA:PomBase.
DR   GO; GO:0005686; C:U2 snRNP; IDA:PomBase.
DR   GO; GO:0071004; C:U2-type prespliceosome; ISO:PomBase.
DR   GO; GO:0005687; C:U4 snRNP; IBA:GO_Central.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISS:PomBase.
DR   GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; ISS:PomBase.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000395; P:mRNA 5'-splice site recognition; IC:PomBase.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
DR   CDD; cd01724; Sm_D1; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR027141; LSm4/Sm_D1/D3.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR047575; Sm.
DR   InterPro; IPR034102; Sm_D1.
DR   InterPro; IPR001163; Sm_dom_euk/arc.
DR   PANTHER; PTHR23338; SMALL NUCLEAR RIBONUCLEOPROTEIN SM; 1.
DR   PANTHER; PTHR23338:SF18; SMALL NUCLEAR RIBONUCLEOPROTEIN SM D1; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS52002; SM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Ribonucleoprotein; Spliceosome.
FT   CHAIN           1..117
FT                   /note="Small nuclear ribonucleoprotein Sm D1"
FT                   /id="PRO_0000122205"
FT   DOMAIN          2..74
FT                   /note="Sm"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
FT   REGION          81..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..109
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   117 AA;  13089 MW;  B568575B62600C64 CRC64;
     MKLVRFLMKL TNETVSIELK NGTIVHGTIT SVDMQMNTHL KAVKMTVKGR EPVPVETLSI
     RGNNIRYYIL PDSLPLDTLL IDDSTKPKQK KKEVVRGRGR GRGRGTRGRG RGASRGF
//
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