GEMI2_SCHPO
ID GEMI2_SCHPO Reviewed; 235 AA.
AC P0CU08; Q9P347;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=SMN complex subunit yip11/gem2 {ECO:0000312|PomBase:SPAC19B12.12c};
DE AltName: Full=Gem-associated protein 2 {ECO:0000305};
DE AltName: Full=Survival of motor neuron protein-interacting protein yip11 {ECO:0000305};
DE Short=SMN-interacting protein yip11 {ECO:0000305};
DE AltName: Full=Yab8-interacting protein 1-a;
GN Name=yip11;
GN Synonyms=gem2 {ECO:0000312|PomBase:SPAC19B12.12c},
GN gemin2 {ECO:0000303|PubMed:26092730}, yip1 {ECO:0000303|PubMed:10749973},
GN yip1-a; ORFNames=SPAC19B12.12c {ECO:0000312|PomBase:SPAC19B12.12c};
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 [MRNA], INTERACTION WITH SMN1, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10749973; DOI=10.1093/hmg/9.5.663;
RA Hannus S., Buehler D., Romano M., Seraphin B., Fischer U.;
RT "The Schizosaccharomyces pombe protein Yab8p and a novel factor, Yip1p,
RT share structural and functional similarity with the spinal muscular
RT atrophy-associated proteins SMN and SIP1.";
RL Hum. Mol. Genet. 9:663-674(2000).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-118, AND
RP IDENTIFICATION BY MASS 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).
RN [4]
RP INTERACTION WITH SMN1.
RX PubMed=26092730; DOI=10.1074/jbc.m115.667279;
RA Gupta K., Martin R., Sharp R., Sarachan K.L., Ninan N.S., Van Duyne G.D.;
RT "Oligomeric Properties of Survival Motor Neuron.Gemin2 Complexes.";
RL J. Biol. Chem. 290:20185-20199(2015).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE CORE SMN COMPLEX, AND INTERACTION WITH
RP SMN1.
RX PubMed=33754639; DOI=10.1093/nar/gkab158;
RA Veepaschit J., Viswanathan A., Bordonne R., Grimm C., Fischer U.;
RT "Identification and structural analysis of the Schizosaccharomyces pombe
RT SMN complex.";
RL Nucleic Acids Res. 49:gkab158-gkab158(2021).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs (PubMed:33754639). Most spliceosomal snRNPs contain a common set
CC of Sm proteins smb1, smd1, smd2, smd3, sme1, smf1 and smg1 that
CC assemble in a heptameric protein ring on the Sm site of the small
CC nuclear RNA to form the core snRNP (By similarity). In the cytosol, the
CC Sm proteins smd1, smd2, sme1, smf1 and smg1 (5Sm) are trapped in an
CC inactive 6S pICln-Sm complex by the chaperone saf5 (By similarity). To
CC complete assembly of core snRNPs, the SMN complex accepts 5Sm from saf5
CC (By similarity). Binding of snRNA inside 5Sm ultimately triggers
CC eviction of the SMN complex, thereby allowing binding of smd3 and smb1
CC to complete assembly of the core snRNP (By similarity). Within the SMN
CC complex, yip11/gem2 constrains the conformation of 5Sm, thereby
CC promoting 5Sm binding to snRNA containing the snRNP code (a nonameric
CC Sm site and a 3'-adjacent stem-loop), thus preventing progression of
CC assembly until a cognate substrate is bound (PubMed:33754639).
CC {ECO:0000250|UniProtKB:O14893, ECO:0000269|PubMed:33754639}.
CC -!- SUBUNIT: Part of the core SMN complex at least composed of smn1,
CC yip11/gem2, gem6, gem7 and gem8 (PubMed:33754639). Interacts with smn1;
CC the interaction is direct (PubMed:26092730, PubMed:10749973,
CC PubMed:33754639). {ECO:0000269|PubMed:10749973,
CC ECO:0000269|PubMed:26092730, ECO:0000269|PubMed:33754639}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10749973}.
CC -!- SIMILARITY: Belongs to the gemin-2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ252269; CAB88094.1; -; mRNA.
DR EMBL; CU329670; CAC00560.1; -; Genomic_DNA.
DR RefSeq; NP_001018218.1; NM_001018698.2.
DR RefSeq; NP_594775.1; NM_001020202.2.
DR AlphaFoldDB; P0CU08; -.
DR SASBDB; P0CU08; -.
DR SMR; P0CU08; -.
DR STRING; 4896.SPAC19B12.12c.1; -.
DR iPTMnet; P0CU08; -.
DR EnsemblFungi; SPAC19B12.12c.1; SPAC19B12.12c.1:pep; SPAC19B12.12c.
DR EnsemblFungi; SPAPB17E12.02.1; SPAPB17E12.02.1:pep; SPAPB17E12.02.
DR GeneID; 2542486; -.
DR GeneID; 3361408; -.
DR KEGG; spo:SPAC19B12.12c; -.
DR KEGG; spo:SPAPB17E12.02; -.
DR PomBase; SPAC19B12.12c; yip11.
DR VEuPathDB; FungiDB:SPAC19B12.12c; -.
DR VEuPathDB; FungiDB:SPAPB17E12.02; -.
DR eggNOG; ENOG502SCAA; Eukaryota.
DR OMA; DIFENCA; -.
DR PRO; PR:P0CU08; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032797; C:SMN complex; IDA:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:PomBase.
DR InterPro; IPR035426; Gemin2/Brr1.
DR Pfam; PF04938; SIP1; 1.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..235
FT /note="SMN complex subunit yip11/gem2"
FT /id="PRO_0000237700"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 235 AA; 26994 MW; 2EC8D23A80FEAA8C CRC64;
MPSKRKRNPL QYQTSGSLDE ETNQRSAFPQ IDNNSASESL EYDIPLDGLD YLATVREEAR
KLVPFVAARR EPETRETIPL RKLEIEAGKK SFDPFLRYLL NIIDKEGERL EQYMESSSLD
ASILPKNLQQ WRVYIEHKAP CWAILAVVDL ATVLEILESL SSWLEKDAID LQSQWIFCFC
YKLPELLNGE DISTLRSVLK SLRSTHTSFP ALQMSASALQ AVLVYRYGQK DLFQT
