SUN3_ARATH
ID SUN3_ARATH Reviewed; 660 AA.
AC F4I316; O23133; Q8GX04; Q8H7G6;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=SUN domain-containing protein 3 {ECO:0000305};
DE Short=AtSUN3 {ECO:0000303|PubMed:25217773};
GN Name=SUN3 {ECO:0000303|PubMed:25217773};
GN OrderedLocusNames=At1g22882 {ECO:0000312|Araport:AT1G22882};
GN ORFNames=F19G10.15 {ECO:0000312|EMBL:AAB72170.1};
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;
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 [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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-153.
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH SUN1; SUN2; SUN4; SUN5; TIK
RP AND WIP1, AND DISRUPTION PHENOTYPE.
RX PubMed=25217773; DOI=10.1093/jxb/eru368;
RA Graumann K., Vanrobays E., Tutois S., Probst A.V., Evans D.E., Tatout C.;
RT "Characterization of two distinct subfamilies of SUN-domain proteins in
RT Arabidopsis and their interactions with the novel KASH-domain protein
RT AtTIK.";
RL J. Exp. Bot. 65:6499-6512(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: Encodes a member of the mid-SUN subfamily of SUN-domain
CC proteins that is localized to both the nuclear envelope and the ER. It
CC is involved in early seed development and nuclear morphology. [TAIR].
CC -!- SUBUNIT: Forms homomers and heteromers with SUN4. Interacts with SUN1,
CC SUN2, SUN5, TIK and WIP1. {ECO:0000269|PubMed:25217773}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:25217773};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Embryo lethal when
CC associated with disruption mutants SUN4 and SUN5.
CC {ECO:0000269|PubMed:25217773}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB72170.1; Type=Erroneous gene model prediction; Evidence={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; AF000657; AAB72170.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30301.1; -; Genomic_DNA.
DR EMBL; AK118518; BAC43121.1; -; mRNA.
DR EMBL; BT005937; AAO64872.1; -; mRNA.
DR EMBL; AF083686; AAN60245.1; -; mRNA.
DR PIR; H86362; H86362.
DR RefSeq; NP_683323.2; NM_148482.5.
DR AlphaFoldDB; F4I316; -.
DR SMR; F4I316; -.
DR STRING; 3702.AT1G22882.1; -.
DR PaxDb; F4I316; -.
DR PRIDE; F4I316; -.
DR ProteomicsDB; 228434; -.
DR EnsemblPlants; AT1G22882.1; AT1G22882.1; AT1G22882.
DR GeneID; 838894; -.
DR Gramene; AT1G22882.1; AT1G22882.1; AT1G22882.
DR KEGG; ath:AT1G22882; -.
DR Araport; AT1G22882; -.
DR TAIR; locus:504956296; AT1G22882.
DR eggNOG; KOG1396; Eukaryota.
DR HOGENOM; CLU_022850_2_0_1; -.
DR InParanoid; F4I316; -.
DR OMA; HAQNFTF; -.
DR OrthoDB; 1550835at2759; -.
DR PRO; PR:F4I316; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I316; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IDA:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR045120; Suco/Slp1-like.
DR InterPro; IPR012919; SUN_dom.
DR PANTHER; PTHR12953; PTHR12953; 2.
DR Pfam; PF07738; Sad1_UNC; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR PROSITE; PS51469; SUN; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..660
FT /note="SUN domain-containing protein 3"
FT /id="PRO_0000441678"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 238..402
FT /note="SUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT REGION 50..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 563..608
FT /evidence="ECO:0000255"
FT COMPBIAS 141..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 53
FT /note="E -> A (in Ref. 5; AAN60245)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="N -> D (in Ref. 3; BAC43121 and 4; AAO64872)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="M -> I (in Ref. 5; AAN60245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 74184 MW; 662735FC07BF50A5 CRC64;
MQRSCRTRRR VSVNKFNGRN SFYKVSLSLV FLLWVLLFFS TLLISHGDGA KDEPLNDSMG
MADPDDGQSD EKVVPFDGPL SLASASVDVT SDLSRNDDVN LSEESEDKEQ EAEISSTVSG
NDIESKDTYL LKQSEINKKD TGIDAGSKYD DFPKKSEINN TGTWNDTEGK DDNNFLKQSQ
LNKTGTGNDT ESSDNEFLEQ NQMNKTVLGN GTEINVSKVD QPSRAVPLGL DEFKSRASNS
RNKSLSDQVS GVIHRMEPGG KEYNYASASK GAKVLSSNKE AKGAASILSR DNDKYLRNPC
STEGKFVVVE LSEETLVNTI KIANFEHYSS NLKEFELQGT LVYPTDTWVH MGNFTASNVK
HEQNFTLLEP KWVRYLKLNF ISHYGSEFYC TLSLIEVYGV DAVERMLEDL ISVQDNKNAY
KPREGDSEHK EKPMQQIESL EGDDGADKST HREKEKEAPP ENMLAKTEAS MAKSSNKLSE
PVEEMRHHQP GSRMPGDTVL KILMQKLRSL DLNLSILERY LEELNLRYGN IFKEMDREAG
VREKAIVALR LDLEGMKERQ EGMVSEAEEM KEWRKRVEAE MEKAEKEKEN IRQSLEQVSK
RLEWMEKKCL TVFTVCLGFG IIAVIAVVIG MGTGLAEKTG SGAWLLLLIS STFIMFVLSL
