SKS1_ARATH
ID SKS1_ARATH Reviewed; 589 AA.
AC Q8VXX5; Q9SB39;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Monocopper oxidase-like protein SKS1;
DE Flags: Precursor;
GN Name=SKS1; OrderedLocusNames=At4g25240; ORFNames=F24A6.80;
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=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 [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=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).
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23065.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81335.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035396; CAA23065.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161563; CAB81335.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85030.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66973.1; -; Genomic_DNA.
DR EMBL; AY074379; AAL67075.1; -; mRNA.
DR EMBL; AY091230; AAM14169.1; -; mRNA.
DR PIR; T05545; T05545.
DR RefSeq; NP_001320060.1; NM_001341725.1.
DR RefSeq; NP_194254.2; NM_118656.5.
DR AlphaFoldDB; Q8VXX5; -.
DR SMR; Q8VXX5; -.
DR BioGRID; 13914; 4.
DR IntAct; Q8VXX5; 2.
DR STRING; 3702.AT4G25240.1; -.
DR PaxDb; Q8VXX5; -.
DR PRIDE; Q8VXX5; -.
DR ProteomicsDB; 232557; -.
DR EnsemblPlants; AT4G25240.1; AT4G25240.1; AT4G25240.
DR EnsemblPlants; AT4G25240.2; AT4G25240.2; AT4G25240.
DR GeneID; 828627; -.
DR Gramene; AT4G25240.1; AT4G25240.1; AT4G25240.
DR Gramene; AT4G25240.2; AT4G25240.2; AT4G25240.
DR KEGG; ath:AT4G25240; -.
DR Araport; AT4G25240; -.
DR TAIR; locus:2122689; AT4G25240.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_022744_2_1_1; -.
DR InParanoid; Q8VXX5; -.
DR OMA; HYTSQAN; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; Q8VXX5; -.
DR PRO; PR:Q8VXX5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VXX5; baseline and differential.
DR Genevisible; Q8VXX5; 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:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA: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 CDD; cd13846; CuRO_1_AAO_like_1; 1.
DR CDD; cd13872; CuRO_2_AAO_like_1; 1.
DR CDD; cd13894; CuRO_3_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 InterPro; IPR034271; CuRO_2_AO-like.
DR InterPro; IPR034275; CuRO_3_AO-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 2: Evidence at transcript level;
KW Cell membrane; Copper; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..563
FT /note="Monocopper oxidase-like protein SKS1"
FT /id="PRO_0000002963"
FT PROPEP 564..589
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002964"
FT REGION 322..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 455
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 563
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 589 AA; 65877 MW; D9EE6958D9CE8710 CRC64;
MAATCSLLAS FLLCFALLSA VSFAADPFVS YDFRVSYLTA SPLGVPQQVI AVNGQFPGPL
LNATTNYNVV VNVFNHLDEP LLLTWPGIQM RRNSWQDGVL GTNCPIPPRW NFTYQFQVKD
QIGSFFYSPS LNFQRASGGF GPIVINNRDI IPIPFPQPDG ELIFIIGDWY TQDHKALRRA
LDSGKELGMP DGVLINGKGP YKYNSSVPDG IDYLTFHVEP GKTYRIRVHN VGISTSLNFR
IQNHSLLLVE TEGHYTSQAN FTDFDVHVGQ SYSFLVTMDQ DATSDYYIVA SARFVNETVW
QRVTGVAILH YSNSKGPVSG PLPVPKTDVS SPWSAMSQPK TIRQNTSASG ARPNPQGSFH
YGQINITNTY ILRSLPPTII NGALRATLNG ISFVNPSTPV RLADRNKVKG AYKLDFPDRP
FNRPLRLDRS MINATYKGFI QVVFQNNDTK IQSFHVDGYS FFVVGMDFGI WSEDKKGSYN
NWDAISRSTI EVYPGGWTAV LISLDNVGVW NIRVENLDRW YLGEETYMRI TNPEEDGKTE
MDPPDNVLYC GALKNLQKEQ HHSAATSILN GHLKLMLLMV LLASVFRFC
