SCO11_ARATH
ID SCO11_ARATH Reviewed; 334 AA.
AC Q8VYP0; Q9SR94;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein SCO1 homolog 1, mitochondrial;
DE AltName: Full=Homolog of the copper chaperone SCO1 member 1;
DE Short=HCC1;
DE Flags: Precursor;
GN Name=HCC1; Synonyms=SCO1-1; OrderedLocusNames=At3g08950; ORFNames=T16O11.9;
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].
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=21041373; DOI=10.1093/jxb/erq269;
RA Steinebrunner I., Landschreiber M., Krause-Buchholz U., Teichmann J.,
RA Rodel G.;
RT "HCC1, the Arabidopsis homologue of the yeast mitochondrial copper
RT chaperone SCO1, is essential for embryonic development.";
RL J. Exp. Bot. 62:319-330(2011).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=21543521; DOI=10.1093/jxb/err138;
RA Attallah C.V., Welchen E., Martin A.P., Spinelli S.V., Bonnard G.,
RA Palatnik J.F., Gonzalez D.H.;
RT "Plants contain two SCO proteins that are differentially involved in
RT cytochrome c oxidase function and copper and redox homeostasis.";
RL J. Exp. Bot. 62:4281-4294(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 169-334 IN COMPLEX WITH COPPER
RP ION.
RX PubMed=31348612; DOI=10.1111/febs.15016;
RA Llases M.E., Lisa M.N., Morgada M.N., Giannini E., Alzari P.M., Vila A.J.;
RT "Arabidopsis thaliana Hcc1 is a Sco-like metallochaperone for CuA assembly
RT in cytochrome c oxidase.";
RL FEBS J. 287:749-762(2020).
CC -!- FUNCTION: Thought to play a role in cellular copper homeostasis,
CC mitochondrial redox signaling or insertion of copper into the active
CC site of COX. Plays an essential role in embryo development.
CC {ECO:0000269|PubMed:21041373, ECO:0000269|PubMed:21543521}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:21041373}; Single-pass membrane protein
CC {ECO:0000269|PubMed:21041373}.
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant with highest
CC expression in imbibed seeds, embryos, endosperm, and root tips.
CC {ECO:0000269|PubMed:21543521}.
CC -!- DISRUPTION PHENOTYPE: Embryos arrested at various developmental stages,
CC mostly at the heart or torpedo stage. {ECO:0000269|PubMed:21041373,
CC ECO:0000269|PubMed:21543521}.
CC -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF07830.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010871; AAF07830.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74701.1; -; Genomic_DNA.
DR EMBL; AY070393; AAL49889.1; -; mRNA.
DR EMBL; AY096736; AAM20370.1; -; mRNA.
DR EMBL; AY085259; AAM62491.1; -; mRNA.
DR RefSeq; NP_566339.1; NM_111729.3.
DR PDB; 6N5U; X-ray; 2.66 A; A/B/C=169-334.
DR PDBsum; 6N5U; -.
DR AlphaFoldDB; Q8VYP0; -.
DR SMR; Q8VYP0; -.
DR BioGRID; 5380; 1.
DR IntAct; Q8VYP0; 1.
DR STRING; 3702.AT3G08950.1; -.
DR PaxDb; Q8VYP0; -.
DR PRIDE; Q8VYP0; -.
DR ProteomicsDB; 232819; -.
DR EnsemblPlants; AT3G08950.1; AT3G08950.1; AT3G08950.
DR GeneID; 820046; -.
DR Gramene; AT3G08950.1; AT3G08950.1; AT3G08950.
DR KEGG; ath:AT3G08950; -.
DR Araport; AT3G08950; -.
DR TAIR; locus:2097673; AT3G08950.
DR eggNOG; KOG2792; Eukaryota.
DR HOGENOM; CLU_050131_0_0_1; -.
DR InParanoid; Q8VYP0; -.
DR OMA; IVAHMRP; -.
DR OrthoDB; 1462537at2759; -.
DR PhylomeDB; Q8VYP0; -.
DR PRO; PR:Q8VYP0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VYP0; baseline and differential.
DR Genevisible; Q8VYP0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IMP:UniProtKB.
DR CDD; cd02968; SCO; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151; PTHR12151; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Copper; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 14..334
FT /note="Protein SCO1 homolog 1, mitochondrial"
FT /id="PRO_0000412567"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 166..331
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 74..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 206
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:31348612,
FT ECO:0007744|PDB:6N5U"
FT BINDING 210
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:31348612,
FT ECO:0007744|PDB:6N5U"
FT BINDING 295
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:31348612,
FT ECO:0007744|PDB:6N5U"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:6N5U"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6N5U"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:6N5U"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:6N5U"
FT HELIX 209..228
FT /evidence="ECO:0007829|PDB:6N5U"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:6N5U"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:6N5U"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:6N5U"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:6N5U"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:6N5U"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:6N5U"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:6N5U"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:6N5U"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:6N5U"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:6N5U"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:6N5U"
SQ SEQUENCE 334 AA; 37195 MW; FF5BA38D8C335A3C CRC64;
MASALCRTAS RLRSVQLFRR IRVSSDLLSA SSPSPACISD ALRHGDFSLP RSFFSLNCGI
EMLKMDQRCL LSTSASDTTS KHDSGKPETK SSEKNEKSGG SESSDGGSDH KNERASGKDV
RGGPVSWMSF FLLFATGAGL VYYYDTQKKR HIEDINKNSI AVKEGPSAGK AAIGGPFSLI
RDDGKRVTEK NLMGKWTILY FGFTHCPDIC PDELIKLAAA IDKIKENSGV DVVPVFISVD
PERDTVQQVH EYVKEFHPKL IGLTGSPEEI KSVARSYRVY YMKTEEEDSD YLVDHSIVMY
LMSPEMNFVK FYGKNHDVDS LTDGVVKEIR QYRK
