SKI30_ARATH
ID SKI30_ARATH Reviewed; 352 AA.
AC Q9M1W7; Q3EAF6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=F-box/kelch-repeat protein SKIP30;
DE AltName: Full=SKP1-interacting partner 30;
GN Name=SKIP30; OrderedLocusNames=At3g63220; ORFNames=F16M2.70;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH SKP1A/ASK1.
RX PubMed=12795696; DOI=10.1046/j.1365-313x.2003.01768.x;
RA Risseeuw E.P., Daskalchuk T.E., Banks T.W., Liu E., Cotelesage J.,
RA Hellmann H., Estelle M., Somers D.E., Crosby W.L.;
RT "Protein interaction analysis of SCF ubiquitin E3 ligase subunits from
RT Arabidopsis.";
RL Plant J. 34:753-767(2003).
CC -!- FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase
CC complexes, which may mediate the ubiquitination and subsequent
CC proteasomal degradation of target proteins. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (ASK-cullin-F-box) protein ligase complex (By
CC similarity). Interacts with SKP1A/ASK1. {ECO:0000250,
CC ECO:0000269|PubMed:12795696}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M1W7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M1W7-2; Sequence=VSP_024315;
CC -!- DOMAIN: The F-box is necessary for the interaction with ASK proteins.
CC {ECO:0000250}.
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DR EMBL; AL138648; CAB86423.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80449.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80450.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64823.1; -; Genomic_DNA.
DR EMBL; AK229127; BAF01002.1; -; mRNA.
DR EMBL; AY087726; AAM65263.1; -; mRNA.
DR PIR; T48111; T48111.
DR RefSeq; NP_001326828.1; NM_001340193.1. [Q9M1W7-1]
DR RefSeq; NP_191881.1; NM_116187.4. [Q9M1W7-2]
DR RefSeq; NP_974481.1; NM_202752.2. [Q9M1W7-1]
DR AlphaFoldDB; Q9M1W7; -.
DR SMR; Q9M1W7; -.
DR BioGRID; 10811; 1.
DR IntAct; Q9M1W7; 2.
DR STRING; 3702.AT3G63220.2; -.
DR PaxDb; Q9M1W7; -.
DR PRIDE; Q9M1W7; -.
DR ProteomicsDB; 232657; -. [Q9M1W7-1]
DR EnsemblPlants; AT3G63220.1; AT3G63220.1; AT3G63220. [Q9M1W7-2]
DR EnsemblPlants; AT3G63220.2; AT3G63220.2; AT3G63220. [Q9M1W7-1]
DR EnsemblPlants; AT3G63220.3; AT3G63220.3; AT3G63220. [Q9M1W7-1]
DR GeneID; 825497; -.
DR Gramene; AT3G63220.1; AT3G63220.1; AT3G63220. [Q9M1W7-2]
DR Gramene; AT3G63220.2; AT3G63220.2; AT3G63220. [Q9M1W7-1]
DR Gramene; AT3G63220.3; AT3G63220.3; AT3G63220. [Q9M1W7-1]
DR KEGG; ath:AT3G63220; -.
DR Araport; AT3G63220; -.
DR TAIR; locus:2077299; AT3G63220.
DR eggNOG; KOG1072; Eukaryota.
DR InParanoid; Q9M1W7; -.
DR OMA; EKNVWDP; -.
DR OrthoDB; 754508at2759; -.
DR PhylomeDB; Q9M1W7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9M1W7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1W7; baseline and differential.
DR Genevisible; Q9M1W7; AT.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.120.10.80; -; 1.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR Pfam; PF01344; Kelch_1; 2.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00612; Kelch; 2.
DR SUPFAM; SSF117281; SSF117281; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Kelch repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..352
FT /note="F-box/kelch-repeat protein SKIP30"
FT /id="PRO_0000283238"
FT DOMAIN 9..55
FT /note="F-box"
FT REPEAT 57..109
FT /note="Kelch 1"
FT REPEAT 110..167
FT /note="Kelch 2"
FT REPEAT 168..215
FT /note="Kelch 3"
FT REPEAT 243..293
FT /note="Kelch 4"
FT REPEAT 296..351
FT /note="Kelch 5"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT /id="VSP_024315"
SQ SEQUENCE 352 AA; 38980 MW; A3CE224DADBAF66C CRC64;
MCYRQETMSG LLDGIPEAVA LRCLAHVPLH LHPNLELVSR SWRAAIRSHE LFRVRKELRS
SEHLLCVCAF DPENIWQVYS PNCDRWLTLP LLPSRIRHLA HFGAVTTAGM LFVLGGGSDA
VSPVTGDHDG TFATDQVWSY DFVQRQWTPR ASMLVPRAMF ACCVLQGKIV VAGGFTTCRK
SISGAEMYDP ENDVWTSIPD LHQTHNSACS GLVVNGKVHV LHKGLSTVQV LESVKLGWDV
KDYGWPQGPM VVVEDVLYVM SHGLVFKQEG DTWKMVASAS EFKRRIGMAM TSLSDEVLIV
GGVIGPDRLN WDIKPLSDVD ALTVGNDRPA WRSVAPMTRC RGTILGCTQL TI
