SCD1_ARATH
ID SCD1_ARATH Reviewed; 1187 AA.
AC Q8RXA7; Q9M9A6; Q9M9A7;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=DENN domain and WD repeat-containing protein SCD1 {ECO:0000305};
DE AltName: Full=Protein STOMATAL CYTOKINESIS DEFECTIVE 1 {ECO:0000303|PubMed:12874123};
GN Name=SCD1 {ECO:0000303|PubMed:12874123};
GN OrderedLocusNames=At1g49040 {ECO:0000312|Araport:AT1G49040};
GN ORFNames=F27J15.16/F27J15.17 {ECO:0000312|EMBL:AAF69702.1,
GN ECO:0000312|EMBL:AAF69703.1};
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP SER-131, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=12874123; DOI=10.1242/dev.00619;
RA Falbel T.G., Koch L.M., Nadeau J.A., Segui-Simarro J.M., Sack F.D.,
RA Bednarek S.Y.;
RT "SCD1 is required for cytokinesis and polarized cell expansion in
RT Arabidopsis thaliana [corrected.";
RL Development 130:4011-4024(2003).
RN [2]
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 [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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH FLS2.
RX PubMed=20472560; DOI=10.1074/jbc.m109.090787;
RA Korasick D.A., McMichael C., Walker K.A., Anderson J.C., Bednarek S.Y.,
RA Heese A.;
RT "Novel functions of Stomatal Cytokinesis-Defective 1 (SCD1) in innate
RT immune responses against bacteria.";
RL J. Biol. Chem. 285:23342-23350(2010).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24179130; DOI=10.1105/tpc.113.115162;
RA McMichael C.M., Reynolds G.D., Koch L.M., Wang C., Jiang N., Nadeau J.,
RA Sack F.D., Gelderman M.B., Pan J., Bednarek S.Y.;
RT "Mediation of clathrin-dependent trafficking during cytokinesis and cell
RT expansion by Arabidopsis stomatal cytokinesis defective proteins.";
RL Plant Cell 25:3910-3925(2013).
CC -!- FUNCTION: Involved in growth and development through its role in
CC cytokinesis and polarized cell expansion (PubMed:12874123). Required
CC for plasma membrane internalization. May function in clathrin-mediated
CC membrane trafficking, including plasma membrane endocytosis, essential
CC to both cytokinesis and cell expansion (PubMed:24179130). Acts as a
CC negative regulator of basal resistance against bacteria
CC (PubMed:20472560). {ECO:0000269|PubMed:12874123,
CC ECO:0000269|PubMed:20472560, ECO:0000269|PubMed:24179130}.
CC -!- SUBUNIT: Interacts with FLS2. {ECO:0000269|PubMed:20472560}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24179130};
CC Peripheral membrane protein {ECO:0000269|PubMed:24179130}. Cytoplasmic
CC vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:24179130}.
CC Note=Colocalized with clathrin at the plasma membrane.
CC {ECO:0000269|PubMed:24179130}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are reduced. According to EST sequences.
CC {ECO:0000305};
CC Name=1;
CC IsoId=Q8RXA7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette and cauline leaves,
CC buds and flowers. {ECO:0000269|PubMed:12874123}.
CC -!- DISRUPTION PHENOTYPE: Defects in seedling development, root elongation,
CC leaf expansion, flower morphogenesis and fertility due to defective
CC cytokinesis in epidermal cells. {ECO:0000269|PubMed:12874123}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF69702.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; Evidence={ECO:0000305};
CC Sequence=AAF69703.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes.; 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; AY082605; AAL92456.1; -; mRNA.
DR EMBL; AC016041; AAF69702.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC016041; AAF69703.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32385.1; -; Genomic_DNA.
DR PIR; H96527; H96527.
DR RefSeq; NP_850959.1; NM_180628.4. [Q8RXA7-1]
DR AlphaFoldDB; Q8RXA7; -.
DR SMR; Q8RXA7; -.
DR STRING; 3702.AT1G49040.1; -.
DR iPTMnet; Q8RXA7; -.
DR PaxDb; Q8RXA7; -.
DR PRIDE; Q8RXA7; -.
DR ProteomicsDB; 232938; -. [Q8RXA7-1]
DR EnsemblPlants; AT1G49040.1; AT1G49040.1; AT1G49040. [Q8RXA7-1]
DR GeneID; 841327; -.
DR Gramene; AT1G49040.1; AT1G49040.1; AT1G49040. [Q8RXA7-1]
DR KEGG; ath:AT1G49040; -.
DR Araport; AT1G49040; -.
DR TAIR; locus:2028481; AT1G49040.
DR eggNOG; KOG2127; Eukaryota.
DR HOGENOM; CLU_007834_0_0_1; -.
DR InParanoid; Q8RXA7; -.
DR PhylomeDB; Q8RXA7; -.
DR PRO; PR:Q8RXA7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RXA7; baseline and differential.
DR Genevisible; Q8RXA7; AT.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0010235; P:guard mother cell cytokinesis; IMP:TAIR.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0045824; P:negative regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0032483; P:regulation of Rab protein signal transduction; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF03456; uDENN; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00800; uDENN; 1.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell membrane;
KW Cytoplasmic vesicle; Growth regulation; Membrane; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..1187
FT /note="DENN domain and WD repeat-containing protein SCD1"
FT /id="PRO_0000431668"
FT DOMAIN 19..179
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 199..330
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 332..437
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT REPEAT 841..892
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 897..934
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 937..975
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 978..1017
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 1020..1057
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 1060..1099
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 1104..1141
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 1152..1187
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REGION 508..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 131
FT /note="S->F: In scd1-1; temperature sensitive mutant with
FT normal growth at the permissive temperature of 16 degrees
FT Celsius and growth defects and sterility due to defective
FT cytokinesis in guard cells and leaf epidermal cells at 22
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:12874123"
SQ SEQUENCE 1187 AA; 131593 MW; D63B27E7D77AED16 CRC64;
MGRIFEYFVV CGLGPEMRTV DGDLGFHGMQ TFYLPALLDQ FPPTDQSPYP APPPQLPTCV
LPAGVEFHSS GFVSSDPASF PRSYPIVLTE GDGSKIFVSC IAFRDRVCED IIEAYRLPPN
TYADKCICLV SHAPNFRVLR NSLEEIFVLC FSSEGSCKPL WDIIAYMVSN VPLPTPGKDR
VLFAVENCLL SVEAPPEDSL PQADISLQPL VQCLDVDNLI KLFTSVLVER RILIRSNKYS
LLTLVSESIC HLIYPFRWLQ VYIPLLFFSG VDYIDAPTPY MMGLHSDVDT SNLAMDGVVV
VDLDINQITT SEEIPQIPEP EFSTLRNDIL KLLHPNVVAI DQLKGFGNSV EQCPKSLSKP
WGEDHDLQLR VIFLKCFASI LGGYRNFIEN KVFSTDAFLK RRSRSTNQPP EPMLVQFLGS
FAFLDYLERR LSSDEKSTNL LEKLQDAVGR GQDAMSILPK SSMEPEIITI AEPEVEESAT
RYTYDRFPAS VRSEEQEEKR KQILAAASGA LESNGRHPPS SPPGKNTKED NFSSMERAAE
RERMVLDIQV KLQGLWLRLL KLGSDEDPLS SFEYGTILAL IESDAEGIGG SGFIECIREH
LYSGWHGQLS EEQFIAVKEL LKMAVGRAAS RSDLSTVRDA LEVSAEMFKK DANNVSDYVQ
RHLISIPIWE ELRFWEGYFE YLMEQPANES VNYATLVTAR LIIVASHMAG LGLPDTEAWN
MIETIAEKQK LGYKLLIKLR GFLSHVQQLR VGYWGASSFK QQAISAGLPS PRPKDVSVSD
ETQQPSEASG RSWVQSMFSR DTASRANSFS RVRKWVSDNA SSDITAAAQK KIQTNVRVLK
GHGGAVTALH SVTRREVCDL VGDREDAGFF ISGSTDCLVK IWDPSLRGSE LRATLKGHTG
TVRAISSDRG KIVSGSDDLS VIVWDKQTTQ LLEELKGHDS QVSCVKMLSG ERVLTAAHDG
TVKMWDVRTD MCVATVGRCS SAILSLEYDD STGILAAAGR DTVANIWDIR SGKQMHKLKG
HTKWIRSIRM VEDTLITGSD DWTARVWSVS RGSCDAVLAC HAGPVQSVEY SPFDKGIITG
SADGLLRFWE NDEGGIKCVK NITLHSSSIL SINAGENWLG IGAADNSMSL FHRPSNAGTK
VSGWQLYRVP QRTAAVVRCV ASDLERKRIC SGGRNGVLRL WDATINI