SCO12_ARATH
ID SCO12_ARATH Reviewed; 276 AA.
AC Q8LAL0; O65661;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein SCO1 homolog 2, mitochondrial;
DE AltName: Full=Homolog of the copper chaperone SCO1 member 2;
DE Short=HCC2;
DE Flags: Precursor;
GN Name=HCC2; Synonyms=SCO1-2; OrderedLocusNames=At4g39740;
GN ORFNames=T19P19.130;
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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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 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).
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 (By similarity). Participates in copper and redox
CC homeostasis. {ECO:0000250, ECO:0000269|PubMed:21543521}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the whole plant with highest
CC expression in imbibed seeds and embryos, and the root hair zone.
CC {ECO:0000269|PubMed:21543521}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:21543521}.
CC -!- SIMILARITY: Belongs to the SCO1/2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18760.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80637.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022605; CAA18760.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161595; CAB80637.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87111.1; -; Genomic_DNA.
DR EMBL; BT024500; ABD19681.1; -; mRNA.
DR EMBL; AY087747; AAM65284.1; -; mRNA.
DR PIR; T05011; T05011.
DR RefSeq; NP_568068.1; NM_120135.5.
DR AlphaFoldDB; Q8LAL0; -.
DR SMR; Q8LAL0; -.
DR STRING; 3702.AT4G39740.1; -.
DR PaxDb; Q8LAL0; -.
DR PRIDE; Q8LAL0; -.
DR ProteomicsDB; 232820; -.
DR EnsemblPlants; AT4G39740.1; AT4G39740.1; AT4G39740.
DR GeneID; 830129; -.
DR Gramene; AT4G39740.1; AT4G39740.1; AT4G39740.
DR KEGG; ath:AT4G39740; -.
DR Araport; AT4G39740; -.
DR TAIR; locus:2135232; AT4G39740.
DR eggNOG; KOG2792; Eukaryota.
DR HOGENOM; CLU_050131_0_4_1; -.
DR InParanoid; Q8LAL0; -.
DR OMA; CRPRVFP; -.
DR OrthoDB; 1462537at2759; -.
DR PhylomeDB; Q8LAL0; -.
DR PRO; PR:Q8LAL0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LAL0; baseline and differential.
DR Genevisible; Q8LAL0; 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:0055070; P:copper ion homeostasis; IMP:UniProtKB.
DR GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; IBA:GO_Central.
DR CDD; cd02968; SCO; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12151; PTHR12151; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 15..276
FT /note="Protein SCO1 homolog 2, mitochondrial"
FT /id="PRO_0000412568"
FT TRANSMEM 66..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 110..273
FT /note="Thioredoxin"
SQ SEQUENCE 276 AA; 30771 MW; 547FB75D2B262B06 CRC64;
MLPCRRLVLS CKNQAASFLR RCGPSKRIQS VNYCKSTRQG HEIPDVKPLF PTGGGTQAPS
RSRARYAVPA ILLGFAGFVG FLHYNDERRA VPRGQASSNS GCGCGSNTTV KGPIIGGPFT
LVSTENKIVT ENDFCGKWVL LYFGYSFSPD VGPEQLKMMS KAVDKLESKH NEKILPVFVT
LDPQRDTPSH LHAYLKEFDS RILGLTGTAS AMRQMAQEYR VYFKKVQEDG EDYLVDTSHN
MYLINPKMEI VRCFGVEYNP DELSQELLKE VASVSQ
