SIN2_ARATH
ID SIN2_ARATH Reviewed; 386 AA.
AC Q8L607; O22228;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Short integuments 2, mitochondrial {ECO:0000303|PubMed:10835408};
DE AltName: Full=DAR GTPase 1 {ECO:0000303|PubMed:16849600};
DE Flags: Precursor;
GN Name=SIN2 {ECO:0000303|PubMed:10835408};
GN Synonyms=DGP1 {ECO:0000303|PubMed:16849600};
GN OrderedLocusNames=At2g41670 {ECO:0000312|Araport:AT2G41670};
GN ORFNames=T32G6.19 {ECO:0000312|EMBL:AAB84349.1};
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 {ECO:0000312|EMBL:AAM20589.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MUTAGENESIS OF SER-150, DISRUPTION PHENOTYPE, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=16849600; DOI=10.1534/genetics.106.060657;
RA Hill T.A., Broadhvest J., Kuzoff R.K., Gasser C.S.;
RT "Arabidopsis SHORT INTEGUMENTS 2 is a mitochondrial DAR GTPase.";
RL Genetics 174:707-718(2006).
RN [2]
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 [3]
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 [4]
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 [5]
RP DOMAIN, AND GENE FAMILY.
RX PubMed=9573393; DOI=10.1016/s0378-1119(98)00088-2;
RA Fu G., Melville S., Brewster S., Warner J., Barker D.C.;
RT "Analysis of the genomic organisation of a small chromosome of Leishmania
RT braziliensis M2903 reveals two genes encoding GTP-binding proteins, one of
RT which belongs to a new G-protein family and is an antigen.";
RL Gene 210:325-333(1998).
RN [6]
RP FUNCTION.
RX PubMed=10835408; DOI=10.1093/genetics/155.2.899;
RA Broadhvest J., Baker S.C., Gasser C.S.;
RT "SHORT INTEGUMENTS 2 promotes growth during Arabidopsis reproductive
RT development.";
RL Genetics 155:899-907(2000).
CC -!- FUNCTION: GTPase that may function in mitochondrial ribosome assembly
CC (Probable). Involved in a variety of growth processes during vegetative
CC development and promotes growth and cell division in the developing
CC integuments (PubMed:10835408, PubMed:16849600).
CC {ECO:0000269|PubMed:10835408, ECO:0000269|PubMed:16849600}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16849600}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, stems,
CC inflorescences and siliques. {ECO:0000269|PubMed:16849600}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern. {ECO:0000305}.
CC -!- DOMAIN: The DARXP motif is also sometime designated as G6 region.
CC {ECO:0000305|PubMed:9573393}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when heterozygous, but
CC completely female sterile when homozygous.
CC {ECO:0000269|PubMed:16849600}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB84349.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY254472; AAP41843.1; -; mRNA.
DR EMBL; AC002510; AAB84349.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10014.1; -; Genomic_DNA.
DR EMBL; AY099738; AAM20589.1; -; mRNA.
DR EMBL; BT000379; AAN15698.1; -; mRNA.
DR PIR; T00823; T00823.
DR RefSeq; NP_850353.1; NM_180022.2.
DR AlphaFoldDB; Q8L607; -.
DR SMR; Q8L607; -.
DR STRING; 3702.AT2G41670.1; -.
DR PaxDb; Q8L607; -.
DR PRIDE; Q8L607; -.
DR ProteomicsDB; 232538; -.
DR EnsemblPlants; AT2G41670.1; AT2G41670.1; AT2G41670.
DR GeneID; 818765; -.
DR Gramene; AT2G41670.1; AT2G41670.1; AT2G41670.
DR KEGG; ath:AT2G41670; -.
DR Araport; AT2G41670; -.
DR TAIR; locus:2062657; AT2G41670.
DR eggNOG; KOG2485; Eukaryota.
DR HOGENOM; CLU_011106_0_3_1; -.
DR InParanoid; Q8L607; -.
DR OMA; DCIPINA; -.
DR OrthoDB; 583045at2759; -.
DR PhylomeDB; Q8L607; -.
DR PRO; PR:Q8L607; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L607; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0048481; P:plant ovule development; IMP:TAIR.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..386
FT /note="Short integuments 2, mitochondrial"
FT /id="PRO_0000432553"
FT DOMAIN 37..207
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 81..84
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 109..111
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 143..150
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 180..184
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 200..203
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT MOTIF 55..59
FT /note="DARXP motif"
FT BINDING 81..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 109..110
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 146..151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT BINDING 203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O31743"
FT MUTAGEN 150
FT /note="S->F: In sin2-1; loss of function."
FT /evidence="ECO:0000269|PubMed:16849600"
SQ SEQUENCE 386 AA; 42984 MW; 8E14E12CE24A922F CRC64;
MVMMLKKTVK KGLIGGMSFA KDAGKINWFP GHMAAATRAI RNRLKLSDLV IEVRDARIPL
SSANEDLQSQ MSAKRRIIAL NKKDLANPNV LNKWTRHFES SKQDCIAINA HSRSSVMKLL
DLVELKLKEV IAREPTLLVM VVGVPNVGKS ALINSIHQIA AARFPVQERL KRATVGPLPG
VTQDIAGFKI AHRPSIYVLD SPGVLVPSIP DIETGLKLAL SGSVKDSVVG EERIAQYFLA
ILNIRGTPLH WKYLVEGINE GPHADCIDKP SYNLKDLRHQ RTKQPDSSAL HYVGDMISEV
QRSLYITLSE FDGDTEDEND LECLIEQQFE VLQKALKIPH KASEARLMVS KKFLTLFRTG
RLGPFILDDV PETETDHPNS KRVVVL
