SINE1_ARATH
ID SINE1_ARATH Reviewed; 560 AA.
AC Q5XVI1; Q1KS90; Q9SLJ5;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein SINE1 {ECO:0000303|PubMed:24891605};
GN Name=SINE1 {ECO:0000303|PubMed:24891605};
GN OrderedLocusNames=At1g54385 {ECO:0000312|Araport:AT1G54385};
GN ORFNames=F20D21.21 {ECO:0000312|EMBL:AAD25634.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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;
RA Xiao Y.-L., Underwood B.A., Moskal W.A. Jr., Wang W., Redman J.C., Wu H.C.,
RA Utterback T., Town C.D.;
RT "Reconstruction of cDNA sequences for hypothetical genes in Arabidopsis
RT thaliana from 5' and 3' RACE products.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [6]
RP GENE FAMILY, NOMENCLATURE, SUBCELLULAR LOCATION, INTERACTION WITH SINE1 AND
RP SINE2, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=24891605; DOI=10.1083/jcb.201401138;
RA Zhou X., Graumann K., Wirthmueller L., Jones J.D., Meier I.;
RT "Identification of unique SUN-interacting nuclear envelope proteins with
RT diverse functions in plants.";
RL J. Cell Biol. 205:677-692(2014).
RN [7]
RP REVIEW.
RX PubMed=25740919; DOI=10.1093/jxb/erv082;
RA Zhou X., Graumann K., Meier I.;
RT "The plant nuclear envelope as a multifunctional platform LINCed by SUN and
RT KASH.";
RL J. Exp. Bot. 66:1649-1659(2015).
CC -!- FUNCTION: Plays a role in nucleus positioning in guard cells.
CC {ECO:0000269|PubMed:24891605}.
CC -!- SUBUNIT: Interacts with SUN1 and SUN2. Binds to F-actin.
CC {ECO:0000269|PubMed:24891605}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:24891605};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in guards cells, but also
CC detected in root cells. {ECO:0000269|PubMed:24891605}.
CC -!- DOMAIN: The KASH domain, which contains a transmembrane domain,
CC mediates the nuclear envelope targeting and is involved in the binding
CC to the SUN proteins. {ECO:0000305|PubMed:24891605}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Affected nucleus
CC positioning in guard cells. {ECO:0000269|PubMed:24891605}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25634.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005287; AAD25634.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33091.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33092.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59946.1; -; Genomic_DNA.
DR EMBL; AY735540; AAU44410.1; -; mRNA.
DR EMBL; AY735541; AAU44411.1; -; mRNA.
DR EMBL; DQ459171; ABE97170.1; -; mRNA.
DR PIR; F96585; F96585.
DR RefSeq; NP_001031189.1; NM_001036112.3.
DR RefSeq; NP_001322263.1; NM_001333644.1.
DR RefSeq; NP_683432.1; NM_148591.3.
DR AlphaFoldDB; Q5XVI1; -.
DR SMR; Q5XVI1; -.
DR STRING; 3702.AT1G54385.2; -.
DR iPTMnet; Q5XVI1; -.
DR PaxDb; Q5XVI1; -.
DR PRIDE; Q5XVI1; -.
DR ProteomicsDB; 234470; -.
DR EnsemblPlants; AT1G54385.1; AT1G54385.1; AT1G54385.
DR EnsemblPlants; AT1G54385.2; AT1G54385.2; AT1G54385.
DR EnsemblPlants; AT1G54385.3; AT1G54385.3; AT1G54385.
DR GeneID; 841880; -.
DR Gramene; AT1G54385.1; AT1G54385.1; AT1G54385.
DR Gramene; AT1G54385.2; AT1G54385.2; AT1G54385.
DR Gramene; AT1G54385.3; AT1G54385.3; AT1G54385.
DR KEGG; ath:AT1G54385; -.
DR Araport; AT1G54385; -.
DR TAIR; locus:504956282; AT1G54385.
DR eggNOG; ENOG502QQPA; Eukaryota.
DR HOGENOM; CLU_028938_0_0_1; -.
DR InParanoid; Q5XVI1; -.
DR OMA; YDDYVGL; -.
DR OrthoDB; 385794at2759; -.
DR PhylomeDB; Q5XVI1; -.
DR PRO; PR:Q5XVI1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5XVI1; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032797; C:SMN complex; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:TAIR.
DR GO; GO:0007097; P:nuclear migration; IMP:TAIR.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..560
FT /note="Protein SINE1"
FT /id="PRO_0000441681"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 517..560
FT /note="KASH"
FT /evidence="ECO:0000305|PubMed:24891605"
FT REGION 7..287
FT /note="ARMADILLO-type fold"
FT /evidence="ECO:0000255"
FT MOTIF 557..560
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000269|PubMed:24891605"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 166
FT /note="W -> C (in Ref. 4; ABE97170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 62153 MW; 375B2961F16CB5ED CRC64;
MGLNLNPILR QELANLDKDT ESRKSAMKAL KSYVKDLDSK AIPGFLAQVF ETKETNSLSG
EYTISLYEIL ARVHGPNIVP QIDTIMSTIV KTLASSAGSF PLQQACSKVI PAIARYGIDP
TTTEDKKRVI IHSLCKPLTD SLLASQESLT SGAALCLKAL VDSDNWRFAS DEMVNRVCQN
VVVALDSNSN QTHLQMGLVM SLAKHNPLIV EAYARLLIHT GLRILGFGVS EGNSQKRLSA
VQMLNFLMKC LDPRSIYSEV ELIIKEMERC QSDQMAYVRG AAYEAMMTSK RIAAELESKM
EKGCRSVTGS NFSRRNCSSI VPDYSLSPES QTLGSFSGYD SPVESSPISH TSCNSEFDRR
SVNRKLWRRD ENGGVVDISL KDGLFSRVTK GSTTVSDSPL VPYDTCENGD EFEGFLMESL
RNTTPSPQRQ RSRRINAEDF NIFSTPRKLI SSLQYPDDVD LDHSDIQSPI LRGEREKTIG
SRKNPKLRKQ FPTMVETMSS TITVSEDTAQ TQMITGKKKK KKMSYAKLVI AISFVVVALF
ATVILMVNQD DDVGYYTVPT
