SKS2_ARATH
ID SKS2_ARATH Reviewed; 592 AA.
AC Q9FHN6;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Monocopper oxidase-like protein SKS2;
DE Flags: Precursor;
GN Name=SKS2; OrderedLocusNames=At5g51480; ORFNames=K17N15.3;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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=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}.
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DR EMBL; AB018109; BAB08664.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96089.1; -; Genomic_DNA.
DR EMBL; BT004990; AAO50523.1; -; mRNA.
DR EMBL; BT004129; AAO42151.1; -; mRNA.
DR RefSeq; NP_199961.1; NM_124527.5.
DR AlphaFoldDB; Q9FHN6; -.
DR SMR; Q9FHN6; -.
DR BioGRID; 20467; 1.
DR IntAct; Q9FHN6; 2.
DR MINT; Q9FHN6; -.
DR STRING; 3702.AT5G51480.1; -.
DR PaxDb; Q9FHN6; -.
DR PRIDE; Q9FHN6; -.
DR ProteomicsDB; 232636; -.
DR EnsemblPlants; AT5G51480.1; AT5G51480.1; AT5G51480.
DR GeneID; 835222; -.
DR Gramene; AT5G51480.1; AT5G51480.1; AT5G51480.
DR KEGG; ath:AT5G51480; -.
DR Araport; AT5G51480; -.
DR TAIR; locus:2153107; AT5G51480.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_022744_2_1_1; -.
DR InParanoid; Q9FHN6; -.
DR OMA; GSWNLRA; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; Q9FHN6; -.
DR PRO; PR:Q9FHN6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHN6; baseline and differential.
DR Genevisible; Q9FHN6; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; 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 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 2: Evidence at transcript level;
KW Cell membrane; Copper; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Metal-binding; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..564
FT /note="Monocopper oxidase-like protein SKS2"
FT /id="PRO_0000251281"
FT PROPEP 565..592
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000251282"
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 564
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
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"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 592 AA; 66407 MW; 7F833E2E7CEEF602 CRC64;
MAATDFFFAF VFSFALIFGF SFAGDPYVSY DFTLSYITAS PLGVPQQVIA VNGKFPGPVI
NATTNYNVHV NVLNHLDEPL LLTWPGVQMR RNSWQDGVLG TNCPIPPNWN FTYDFQLKDQ
IGSYFYSPSL NFQRASGGFG ALIINNRDLV PIPFTEPDGE IIFIIGDWYT QNHTALRRIL
DSGKELGMPD GVLINGKGPF KYNSSVPDGI EHETVNVDPG KTYRIRVHNV GISTSLNFRI
QNHKLLLIET EGRYTSQMNF TDFDVHVGQS YSFLVTMDQN ATSDYYIVAS ARFVNETVWQ
RVTGVGILHY SNSKGPASGP LPVSATDVNH PWSAMNQPRA IKQNTSASGA RPNPQGSFHY
GQINITRTYI LRSLPPTKIN GKLRATLNGI SFVNPSTPMR LADDHKVKGD YMLDFPDRPL
DEKLPRLSSS IINATYKGFI QVIFQNNDTK IQSFHIDGYA FYVVAMDFGI WSEDRNSSYN
NWDAVARSTV EVYPGAWTAV LISLDNVGVW NIRVENLDRW YLGQETYMRI INPEENGSTE
MDPPENVMYC GALQAMQKEQ HHSSATKSMT NGQLILIFSM MMVLLSSFSS FC
