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 03-AUG-2022, entry version 140.
DE RecName: Full=Preprotein translocase subunit SCY1, chloroplastic;
DE AltName: Full=CpSecY;
DE Flags: Precursor;
GN Name=SCY1; Synonyms=SECY; OrderedLocusNames=At2g18710; ORFNames=MSF3.9;
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 [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 cDNA
RT 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., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [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., 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 [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 translocation of
RT the 33-kDa but not the 23-kDa subunit of the oxygen-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-translocase
RT 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 protein
RT 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 other
CC proteins to allow the translocation of proteins across the chloroplast
CC thylakoid membranes. Required for normal greening during embryogenesis.
CC Central subunit of the protein translocation channel SecYE. Consists of
CC two halves formed by TMs 1-5 and 6-10. These two domains form a lateral
CC gate at the front which open onto the bilayer between TMs 2 and 7, and
CC are clamped together by SecE at the back. The channel is closed by both
CC a pore ring composed of hydrophobic SecY resides and a short helix
CC (helix 2A) on the extracellular side of the membrane which forms a plug
CC (By similarity). {ECO:0000250, ECO:0000269|PubMed:21051552}.
CC -!- SUBUNIT: Part of the Sec protein translocation apparatus. Interacts
CC with SECE1, ALB3 and probably with SECA1. {ECO:0000269|PubMed:10207046,
CC ECO:0000269|PubMed:12217076, ECO:0000269|PubMed:15988575}.
CC -!- INTERACTION:
CC Q38885; Q8LBP4: ALB3; NbExp=8; IntAct=EBI-1806802, EBI-1806831;
CC Q38885; 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-pass
CC membrane protein {ECO:0000269|PubMed:10207046,
CC ECO:0000269|PubMed:12217076}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethal. Albino seedlings with yellow and
CC translucent (glassy) lateral organs when grown heterotrophically.
CC {ECO:0000269|PubMed:21051552}.
CC -!- MISCELLANEOUS: Cannot substitute for SCY2.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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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 AlphaFoldDB; Q38885; -.
DR SMR; Q38885; -.
DR BioGRID; 1743; 3.
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 PRIDE; Q38885; -.
DR ProteomicsDB; 232716; -.
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; ENOG502QSNV; Eukaryota.
DR HOGENOM; CLU_030313_0_0_1; -.
DR InParanoid; Q38885; -.
DR OMA; FAMWLGE; -.
DR OrthoDB; 912533at2759; -.
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; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0010027; P:thylakoid membrane organization; ISS:TAIR.
DR Gene3D; 1.10.3370.10; -; 1.
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_dom_sf.
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;
KW Chloroplast; Membrane; Plastid; Protein transport; Reference proteome;
KW Thylakoid; Transit peptide; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..551
FT /note="Preprotein translocase subunit SCY1, chloroplastic"
FT /id="PRO_0000031995"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 281
FT /note="V -> L (in Ref. 1; AAB60305)"
FT /evidence="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
