SKU5_ARATH
ID SKU5_ARATH Reviewed; 587 AA.
AC Q9SU40; Q0WM56; Q8H7C9;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Monocopper oxidase-like protein SKU5;
DE AltName: Full=Skewed roots;
DE Flags: Precursor;
GN Name=SKU5; OrderedLocusNames=At4g12420; ORFNames=T1P17.10;
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], PROTEIN SEQUENCE OF 21-35, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND GPI-ANCHOR.
RC STRAIN=cv. Columbia;
RX PubMed=12119380; DOI=10.1105/tpc.002360;
RA Sedbrook J.C., Carroll K.L., Hung K.F., Masson P.H., Somerville C.R.;
RT "The Arabidopsis SKU5 gene encodes an extracellular glycosyl
RT phosphatidylinositol-anchored glycoprotein involved in directional root
RT growth.";
RL Plant Cell 14:1635-1648(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] OF 1-157.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 257-587.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
CC -!- FUNCTION: May be a monocopper oxidase of unknown specificity. Involved
CC in directional growth processes, possibly by participating in cell wall
CC expansion.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:12119380}. Cell membrane
CC {ECO:0000269|PubMed:12119380, ECO:0000269|PubMed:15060130}; Lipid-
CC anchor, GPI-anchor {ECO:0000269|PubMed:12119380}; Extracellular side
CC {ECO:0000269|PubMed:12119380}. Note=Partially soluble and located in
CC the cell wall.
CC -!- TISSUE SPECIFICITY: Expressed in roots, hypocotyls, cotyledons, leaves,
CC stems and flowers. {ECO:0000269|PubMed:12119380}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AF439406; AAL62306.1; -; mRNA.
DR EMBL; AL049730; CAB41712.1; -; Genomic_DNA.
DR EMBL; AL161534; CAB78285.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83128.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83129.1; -; Genomic_DNA.
DR EMBL; AF083740; AAN60298.1; -; mRNA.
DR EMBL; AK229975; BAF01800.1; -; mRNA.
DR PIR; T07634; T07634.
DR RefSeq; NP_001190704.1; NM_001203775.2.
DR RefSeq; NP_192979.1; NM_117312.4.
DR AlphaFoldDB; Q9SU40; -.
DR SMR; Q9SU40; -.
DR BioGRID; 12149; 3.
DR STRING; 3702.AT4G12420.2; -.
DR iPTMnet; Q9SU40; -.
DR PaxDb; Q9SU40; -.
DR PRIDE; Q9SU40; -.
DR ProteomicsDB; 232592; -.
DR EnsemblPlants; AT4G12420.1; AT4G12420.1; AT4G12420.
DR EnsemblPlants; AT4G12420.2; AT4G12420.2; AT4G12420.
DR GeneID; 826851; -.
DR Gramene; AT4G12420.1; AT4G12420.1; AT4G12420.
DR Gramene; AT4G12420.2; AT4G12420.2; AT4G12420.
DR KEGG; ath:AT4G12420; -.
DR Araport; AT4G12420; -.
DR TAIR; locus:2135535; AT4G12420.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_022744_2_1_1; -.
DR InParanoid; Q9SU40; -.
DR OMA; YIKVVNP; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; Q9SU40; -.
DR PRO; PR:Q9SU40; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU40; baseline and differential.
DR Genevisible; Q9SU40; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:TAIR.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009932; P:cell tip growth; IMP:TAIR.
DR CDD; cd13846; CuRO_1_AAO_like_1; 1.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034273; CuRO_1_AAO-like.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Copper; Direct protein sequencing; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:12119380"
FT CHAIN 21..562
FT /note="Monocopper oxidase-like protein SKU5"
FT /id="PRO_0000002961"
FT PROPEP 563..587
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002962"
FT BINDING 80
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT LIPID 562
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 46..48
FT /note="IAI -> MAM (in Ref. 4; AAN60298)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="F -> V (in Ref. 4; AAN60298)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 587 AA; 65638 MW; 86232D755A5CA219 CRC64;
MDLFKILLLV FFVNISFCFA ADPYSFYNFE VSYITASPLG VPQQVIAING KFPGPTINVT
TNENLVVNVR NKLDEGLLLH WNGIQQRRVS WQDGVLGTNC PIPPKWNWTY EFQVKDQIGS
FFYFPSLHFQ RASGGFGSFV VNPRAIIPVP FSTPDGDITV TIGDWYIRNH TALRKALDDG
KDLGMPDGVL INGKGPYRYN DTLVADGIDF ETITVHPGKT YRLRVSNVGI STSLNFRIQG
HNLVLAESEG SYTVQQNYTS LDIHVGQSYS FLVTMDQNAS SDYYIVASAR VVNETIWRRV
TGVGILKYTN SKGKAKGQLP PGPQDEFDKT FSMNQARSIR WNVSASGARP NPQGSFKYGS
INVTDVYVLR NMPPVTISGK RRTTLNGISF KNPSTPIRLA DKLKVKDVYK LDFPKRPLTG
PAKVATSIIN GTYRGFMEVV LQNNDTKMQS YHMSGYAFFV VGMDYGEWTE NSRGTYNKWD
GIARSTIQVY PGAWSAILIS LDNPGAWNLR TENLDSWYLG QETYVRVVNP DENNKTEFGH
PDNVLYCGAL SKLQKPQKVS SSASKSIGFT SLSMVVMALV MMMMLQH
