U1135_ARATH
ID U1135_ARATH Reviewed; 333 AA.
AC Q8VY74; O22851; Q8GX59;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=U11/U12 small nuclear ribonucleoprotein 35 kDa protein;
DE Short=U11/U12 snRNP 35 kDa protein;
DE Short=U11/U12-35K;
GN Name=SNRNP35; OrderedLocusNames=At2g43370; ORFNames=T1O24.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, SUBUNIT, PHOSPHORYLATION, INTERACTION WITH SCL28; SCL30;
RP SCL30A; SCL33; SC35; SR30; SR34; RS31; RS40; RSZ21 AND RS2Z33, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15987817; DOI=10.1261/rna.2440305;
RA Lorkovic Z.J., Lehner R., Forstner C., Barta A.;
RT "Evolutionary conservation of minor U12-type spliceosome between plants and
RT humans.";
RL RNA 11:1095-1107(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-333 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=10373121; DOI=10.1126/science.284.5422.2003;
RA Will C.L., Schneider C., Reed R., Luehrmann R.;
RT "Identification of both shared and distinct proteins in the major and minor
RT spliceosomes.";
RL Science 284:2003-2005(1999).
RN [7]
RP INTERACTION WITH CYP95.
RX PubMed=15166240; DOI=10.1074/jbc.m400270200;
RA Lorkovic Z.J., Lopato S., Pexa M., Lehner R., Barta A.;
RT "Interactions of Arabidopsis RS domain containing cyclophilins with SR
RT proteins and U1 and U11 small nuclear ribonucleoprotein-specific proteins
RT suggest their involvement in pre-mRNA Splicing.";
RL J. Biol. Chem. 279:33890-33898(2004).
CC -!- FUNCTION: May facilitate 5' splice site recognition in the minor
CC spliceosome. May be involved in interactions with components of the
CC major spliceosome bound to the pyrimidine tract of an upstream U2-type
CC intron. {ECO:0000269|PubMed:10373121}.
CC -!- SUBUNIT: Part of the U11 snRNP, a component of the minor U12-type
CC spliceosome. U11 and U12 snRNPs exist not only as monoparticles but
CC also as a preformed U11/U12 di-snRNP complex. Interacts with CYP95,
CC SCL28, SCL30, SCL30A, SCL33, SC35, SR30, SR34, RS31, RS40, RSZ21 and
CC RS2Z33. {ECO:0000269|PubMed:15166240, ECO:0000269|PubMed:15987817}.
CC -!- INTERACTION:
CC Q8VY74; O23160: MYB73; NbExp=3; IntAct=EBI-927038, EBI-25506855;
CC Q8VY74; P92964: RS31; NbExp=4; IntAct=EBI-927038, EBI-927132;
CC Q8VY74; Q8L3X8: SCL30; NbExp=2; IntAct=EBI-927038, EBI-927061;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:15987817}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VY74-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VY74-2; Sequence=VSP_055300;
CC Name=3;
CC IsoId=Q8VY74-3; Sequence=VSP_055301, VSP_055302;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15987817}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15987817}.
CC -!- MISCELLANEOUS: [Isoform 2]: Has no effect on the assembly of the
CC protein into snRNP, but reduces the affinity for SR proteins.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64330.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC43032.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC002335; AAB64330.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10257.1; -; Genomic_DNA.
DR EMBL; AY072388; AAL62380.1; -; mRNA.
DR EMBL; AY114697; AAM48016.1; -; mRNA.
DR EMBL; AK118423; BAC43032.1; ALT_INIT; mRNA.
DR PIR; C84865; C84865.
DR RefSeq; NP_850395.1; NM_180064.3. [Q8VY74-1]
DR AlphaFoldDB; Q8VY74; -.
DR SMR; Q8VY74; -.
DR BioGRID; 4275; 30.
DR IntAct; Q8VY74; 32.
DR STRING; 3702.AT2G43370.1; -.
DR PaxDb; Q8VY74; -.
DR PRIDE; Q8VY74; -.
DR ProteomicsDB; 228670; -. [Q8VY74-1]
DR EnsemblPlants; AT2G43370.1; AT2G43370.1; AT2G43370. [Q8VY74-1]
DR GeneID; 818938; -.
DR Gramene; AT2G43370.1; AT2G43370.1; AT2G43370. [Q8VY74-1]
DR KEGG; ath:AT2G43370; -.
DR Araport; AT2G43370; -.
DR TAIR; locus:2058141; AT2G43370.
DR eggNOG; KOG0113; Eukaryota.
DR HOGENOM; CLU_035088_0_0_1; -.
DR InParanoid; Q8VY74; -.
DR OMA; HKRHKSH; -.
DR PhylomeDB; Q8VY74; -.
DR PRO; PR:Q8VY74; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VY74; baseline and differential.
DR Genevisible; Q8VY74; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0034693; C:U11/U12 snRNP; IDA:GO_Central.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0017069; F:snRNA binding; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12237; RRM_snRNP35; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034146; snRNP35_RRM.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Spliceosome.
FT CHAIN 1..333
FT /note="U11/U12 small nuclear ribonucleoprotein 35 kDa
FT protein"
FT /id="PRO_0000429830"
FT DOMAIN 64..142
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 154..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..325
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 123
FT /note="E -> EQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15987817"
FT /id="VSP_055300"
FT VAR_SEQ 180..187
FT /note="RPIPHEDL -> YGFALLFL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15987817"
FT /id="VSP_055301"
FT VAR_SEQ 188..333
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15987817"
FT /id="VSP_055302"
FT CONFLICT 214
FT /note="G -> R (in Ref. 5; BAC43032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 38375 MW; 11FE374575F6C137 CRC64;
MSGGGNNVVN KVFYATSYHP IQAGSIDGTD VAPHDNGVRR ALLCYNAGLY DPSGDSKAVG
DPYCTLFVGR LSHHTTEDTL REVMSKYGRI KNLRLVRHIV TGASRGYGFV EYETEKEMLR
AYEDAHHSLI DGREIIVDYN RQQLMPGWIP RRLGGGLGGR KESGQLRFGG RDRPFRAPLR
PIPHEDLKKL GIQLPPEGRY MSRTQIPSPP RRKGSVSDRE EEYYREKSSV EREEEFKERS
SLRSYHSHRS SAHTHSSHRR RSKDREECSR EESRSDRKER ARGMEDRYGD NKGEVSGSKR
SKRSEEDRSR KRHKHLPSHH HRRSYSQDHH SSD
