(data stored in ACNUC13479 zone)

SWISSPROT: SCY1_ARATH

ID   SCY1_ARATH              Reviewed;         551 AA.
AC   Q38885; Q9SLG1;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   10-MAY-2017, entry version 120.
DE   RecName: Full=Preprotein translocase subunit SCY1, chloroplastic;
DE   AltName: Full=CpSecY;
DE   Flags: Precursor;
GN   Name=SCY1; Synonyms=SECY; OrderedLocusNames=At2g18710;
GN   ORFNames=MSF3.9;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7629062; DOI=10.1074/jbc.270.30.17664;
RA   Laidler V., Chaddock A.M., Knott T.G., Walker D., Robinson C.;
RT   "A SecY homolog in Arabidopsis thaliana. Sequence of a full-length
RT   cDNA clone and import of the precursor protein into chloroplasts.";
RL   J. Biol. Chem. 270:17664-17667(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH SECE1.
RX   PubMed=10207046; DOI=10.1074/jbc.274.17.12177;
RA   Schuenemann D., Amin P., Hartmann E., Hoffman N.E.;
RT   "Chloroplast SecY is complexed to SecE and involved in the
RT   translocation of the 33-kDa but not the 23-kDa subunit of the oxygen-
RT   evolving complex.";
RL   J. Biol. Chem. 274:12177-12182(1999).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH ALB3.
RX   PubMed=12217076; DOI=10.1042/BJ20021291;
RA   Klostermann E., Droste Gen Helling I., Carde J.P., Schunemann D.;
RT   "The thylakoid membrane protein ALB3 associates with the cpSecY-
RT   translocase in Arabidopsis thaliana.";
RL   Biochem. J. 368:777-781(2002).
RN   [7]
RP   INTERACTION WITH ALB3 AND SECE1.
RX   PubMed=15988575; DOI=10.1007/s00253-005-0029-3;
RA   Pasch J.C., Nickelsen J., Schunemann D.;
RT   "The yeast split-ubiquitin system to study chloroplast membrane
RT   protein interactions.";
RL   Appl. Microbiol. Biotechnol. 69:440-447(2005).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21051552; DOI=10.1104/pp.110.166546;
RA   Skalitzky C.A., Martin J.R., Harwood J.H., Beirne J.J., Adamczyk B.J.,
RA   Heck G.R., Cline K., Fernandez D.E.;
RT   "Plastids contain a second sec translocase system with essential
RT   functions.";
RL   Plant Physiol. 155:354-369(2011).
CC   -!- FUNCTION: Involved in protein export. Probably interacts with
CC       other proteins to allow the translocation of proteins across the
CC       chloroplast thylakoid membranes. Required for normal greening
CC       during embryogenesis. Central subunit of the protein translocation
CC       channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10.
CC       These two domains form a lateral gate at the front which open onto
CC       the bilayer between TMs 2 and 7, and are clamped together by SecE
CC       at the back. The channel is closed by both a pore ring composed of
CC       hydrophobic SecY resides and a short helix (helix 2A) on the
CC       extracellular side of the membrane which forms a plug (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:21051552}.
CC   -!- SUBUNIT: Part of the Sec protein translocation apparatus.
CC       Interacts with SECE1, ALB3 and probably with SECA1.
CC       {ECO:0000269|PubMed:10207046, ECO:0000269|PubMed:12217076,
CC       ECO:0000269|PubMed:15988575}.
CC   -!- INTERACTION:
CC       Q8LBP4:ALB3; NbExp=8; IntAct=EBI-1806802, EBI-1806831;
CC       O23342:SECE1; NbExp=3; IntAct=EBI-1806802, EBI-1806811;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:10207046, ECO:0000269|PubMed:12217076}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:10207046,
CC       ECO:0000269|PubMed:12217076}.
CC   -!- DISRUPTION PHENOTYPE: Seedling lethal. Albino seedlings with
CC       yellow and translucent (glassy) lateral organs when grown
CC       heterotrophically. {ECO:0000269|PubMed:21051552}.
CC   -!- MISCELLANEOUS: Cannot substitute for SCY2.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
DR   EMBL; U37247; AAB60305.1; -; mRNA.
DR   EMBL; AC005724; AAD08940.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06796.1; -; Genomic_DNA.
DR   EMBL; AF424550; AAL11544.1; -; mRNA.
DR   EMBL; AY058103; AAL24211.1; -; mRNA.
DR   EMBL; AY065093; AAL38269.1; -; mRNA.
DR   EMBL; BT002632; AAO11548.1; -; mRNA.
DR   PIR; A57189; A57189.
DR   PIR; F84567; F84567.
DR   RefSeq; NP_179461.1; NM_127427.3.
DR   UniGene; At.10218; -.
DR   ProteinModelPortal; Q38885; -.
DR   BioGrid; 1743; 2.
DR   IntAct; Q38885; 4.
DR   STRING; 3702.AT2G18710.1; -.
DR   TCDB; 3.A.5.4.2; the general secretory pathway (sec) family.
DR   PaxDb; Q38885; -.
DR   EnsemblPlants; AT2G18710.1; AT2G18710.1; AT2G18710.
DR   GeneID; 816386; -.
DR   Gramene; AT2G18710.1; AT2G18710.1; AT2G18710.
DR   KEGG; ath:AT2G18710; -.
DR   Araport; AT2G18710; -.
DR   TAIR; locus:2054038; AT2G18710.
DR   eggNOG; ENOG410IHRV; Eukaryota.
DR   eggNOG; COG0201; LUCA.
DR   HOGENOM; HOG000080585; -.
DR   InParanoid; Q38885; -.
DR   KO; K10956; -.
DR   OMA; QTYVISQ; -.
DR   OrthoDB; EOG093609ZU; -.
DR   PhylomeDB; Q38885; -.
DR   PRO; PR:Q38885; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q38885; baseline and differential.
DR   Genevisible; Q38885; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0010027; P:thylakoid membrane organization; ISS:TAIR.
DR   HAMAP; MF_01465; SecY; 1.
DR   InterPro; IPR026593; SecY.
DR   InterPro; IPR002208; SecY/SEC61-alpha.
DR   InterPro; IPR030659; SecY_CS.
DR   InterPro; IPR023201; SecY_su_dom.
DR   PANTHER; PTHR10906; PTHR10906; 1.
DR   Pfam; PF00344; SecY; 1.
DR   SUPFAM; SSF103491; SSF103491; 1.
DR   TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR   PROSITE; PS00755; SECY_1; 1.
DR   PROSITE; PS00756; SECY_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q38885.
DR   SWISS-2DPAGE; Q38885.
KW   Chloroplast; Complete proteome; Membrane; Plastid; Protein transport;
KW   Reference proteome; Thylakoid; Transit peptide; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT       1     67       Chloroplast. {ECO:0000255}.
FT   CHAIN        68    551       Preprotein translocase subunit SCY1,
FT                                chloroplastic.
FT                                /FTId=PRO_0000031995.
FT   TRANSMEM    142    162       Helical. {ECO:0000255}.
FT   TRANSMEM    192    212       Helical. {ECO:0000255}.
FT   TRANSMEM    241    261       Helical. {ECO:0000255}.
FT   TRANSMEM    268    288       Helical. {ECO:0000255}.
FT   TRANSMEM    295    315       Helical. {ECO:0000255}.
FT   TRANSMEM    328    348       Helical. {ECO:0000255}.
FT   TRANSMEM    382    402       Helical. {ECO:0000255}.
FT   TRANSMEM    415    435       Helical. {ECO:0000255}.
FT   TRANSMEM    482    502       Helical. {ECO:0000255}.
FT   TRANSMEM    503    523       Helical. {ECO:0000255}.
FT   CONFLICT    281    281       V -> L (in Ref. 1; AAB60305).
FT                                {ECO:0000305}.
SQ   SEQUENCE   551 AA;  59492 MW;  526854797A3B8059 CRC64;
     MITVSEVSSY SSSSSNFASL SRLNHKSSSR LRSSSLYKGS FFSVSTKTRR NTCKAKSWNL
     GLVINSRSSE ASVFDPLGIN PDETSGLSSI WESFVSLLSP SFESSSGNRR DKPSSGRGVA
     AAIEDSSIDF GDFFKGPLPG KFLKLLGFLA LSRLGIYIPL GGVNREAFVG NLDQNSILST
     LDTFSGGGIG RLGICSLGIV PFINAQIVFQ LLAQVYPKLQ DLQKKEGEAG RKKILQYTRY
     ASVGFAIVQA IGQVFYLRPY VNDFSTEWVV SSVTLLTLGS VLTTYIGERI SDLKLGNGTS
     LLIFTSIISY LPASFGRTTA EALQEGNYTG LGTIVVSFLL LVLGIVYVQE AERKIPLNYA
     SRYTSKAGGL QKSAYLPFKV NSAGVMPIIF STSSLALPAT LARFTGISAL KNVAFALTPG
     GSFYLPTNIL LIAFFNYYYT FLQLDPDDVS EQLKRQGASI PLVRPGKSTA LFIKTVLGRI
     SVLGSAFLAV LAAGPAVVEQ ITHLTAFRGF AGTSVLILVG CATDTARKVQ AEIISQKYKN
     IEFYELDKYD P
//

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