SCY2_ARATH
ID SCY2_ARATH Reviewed; 575 AA.
AC F4IQV7; Q8W4F6; Q9SIQ4;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Preprotein translocase subunit SCY2, chloroplastic;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2289;
DE Flags: Precursor;
GN Name=SCY2; Synonyms=EMB2289; OrderedLocusNames=At2g31530; ORFNames=T9H9.5;
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=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 [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] OF 17-575.
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP 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 postimport or conservative sorting pathway for
CC inner membrane proteins in plastids. Central subunit of the protein
CC translocation channel SecYE. Consists of two halves formed by TMs 1-5
CC and 6-10. These two domains form a lateral gate at the front which open
CC onto 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 similarity).
CC {ECO:0000250, ECO:0000269|PubMed:21051552}.
CC -!- SUBUNIT: Part of a second Sec protein translocation apparatus.
CC Interacts probably with SECA2.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:21051552}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21051552}. Plastid, amyloplast membrane
CC {ECO:0000269|PubMed:21051552}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21051552}. Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:21051552}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21051552}. Note=Predominantly localized to envelope
CC membranes.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:21051552}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal. {ECO:0000269|PubMed:21051552}.
CC -!- MISCELLANEOUS: Cannot substitute for SCY1.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24832.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAL32668.1; Type=Miscellaneous discrepancy; Note=Intron retention and frameshift at position 388.; Evidence={ECO:0000305};
CC Sequence=AAM13353.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BX820289; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC007071; AAD24832.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08557.1; -; Genomic_DNA.
DR EMBL; AY062590; AAL32668.1; ALT_SEQ; mRNA.
DR EMBL; AY093354; AAM13353.1; ALT_SEQ; mRNA.
DR EMBL; BX820289; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; H84721; H84721.
DR RefSeq; NP_180711.4; NM_128710.7.
DR AlphaFoldDB; F4IQV7; -.
DR BioGRID; 3058; 1.
DR STRING; 3702.AT2G31530.1; -.
DR TCDB; 3.A.5.4.2; the general secretory pathway (sec) family.
DR PaxDb; F4IQV7; -.
DR PRIDE; F4IQV7; -.
DR ProteomicsDB; 232775; -.
DR EnsemblPlants; AT2G31530.1; AT2G31530.1; AT2G31530.
DR GeneID; 817711; -.
DR Gramene; AT2G31530.1; AT2G31530.1; AT2G31530.
DR KEGG; ath:AT2G31530; -.
DR Araport; AT2G31530; -.
DR TAIR; locus:2065868; AT2G31530.
DR eggNOG; ENOG502QPS8; Eukaryota.
DR HOGENOM; CLU_030313_3_2_1; -.
DR InParanoid; F4IQV7; -.
DR OMA; AVSWWPY; -.
DR OrthoDB; 579504at2759; -.
DR PRO; PR:F4IQV7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IQV7; baseline and differential.
DR Genevisible; F4IQV7; AT.
DR GO; GO:0033097; C:amyloplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
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:0009526; C:plastid envelope; IDA:TAIR.
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:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0072598; P:protein localization to chloroplast; IMP:TAIR.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR Gene3D; 1.10.3370.10; -; 1.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR023201; SecY_dom_sf.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF00344; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
PE 2: Evidence at transcript level;
KW Amyloplast; Chloroplast; Membrane; Plastid; Protein transport;
KW Reference proteome; Thylakoid; Transit peptide; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 35..575
FT /note="Preprotein translocase subunit SCY2, chloroplastic"
FT /id="PRO_0000414227"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 380
FT /note="F -> L (in Ref. 4; BX820289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 64711 MW; C190C821BBC3ED65 CRC64;
MNSSQACFFH FSLRPISLSH PSYAFLSKRD PFLCSQPRKC LTTNLNMSRT RQGHSIQMNR
RHLLMKERKS FSINYSDKFR DDSMSSEEMH TDALDVEIIP PDSQDIRNSQ NSAVSNTLQD
DRPKSFRNRF LDFVRISSVL NTAAERFFKS EIRRRLFVTA VLLVLSRVGY FIPLPGFDRR
LIPQDYLSFV SGSVEELGEF GAEIKLSLFQ LGLSPQIIAS IIMQVLCHVL PSLVKLRKEG
LDGHEKIKSY IWWLSFFFAI VEALVVAYTS LQYSVFAATA QVKHVMMTSS LLVCGAMTMT
WLCDTISESG FGHGSSLIIC VGILTGYTET LHKMLNQISG SFSNWLPYLL GLLGIFTVVT
MFAVVVTEGC RKIKLQYYGF KLASASREGS PITEVEPYIP FNINPAGMQP VLTTTYLLAF
PSILASILGS PFLLNMKEIL NPESTVGAPP WVYYSIYAFF VFLFNIFDIA NLPKEIADYL
NKMGARIPNI KPGKATIEYL TKIQASTRFW GGLLLSFLAT ASTVLDHYLR SINQGFSIGF
TSVLIIVGSI IELRRSYHAY NVMPSLSKAL KRYGV
