SPCS2_ARATH
ID SPCS2_ARATH Reviewed; 192 AA.
AC P58684;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Signal peptidase complex subunit 2;
DE AltName: Full=Microsomal signal peptidase 25 kDa subunit;
DE Short=SPase 25 kDa subunit;
GN OrderedLocusNames=At2g39960; ORFNames=T28M21.12;
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).
CC -!- FUNCTION: Component of the signal peptidase complex (SPC) which
CC catalyzes the cleavage of N-terminal signal sequences from nascent
CC proteins as they are translocated into the lumen of the endoplasmic
CC reticulum (By similarity). Enhances the enzymatic activity of SPC and
CC facilitates the interactions between different components of the
CC translocation site (By similarity). {ECO:0000250|UniProtKB:Q04969,
CC ECO:0000250|UniProtKB:Q15005}.
CC -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC catalytic subunit SEC11 and three accessory subunits SPCS1, SPCS2 and
CC SPCS3. The complex induces a local thinning of the ER membrane which is
CC used to measure the length of the signal peptide (SP) h-region of
CC protein substrates. This ensures the selectivity of the complex towards
CC h-regions shorter than 18-20 amino acids.
CC {ECO:0000250|UniProtKB:Q15005}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q28250}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q28250}.
CC -!- SIMILARITY: Belongs to the SPCS2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF002109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC09756.1; -; Genomic_DNA.
DR EMBL; AY065212; AAL38688.1; -; mRNA.
DR EMBL; AY096518; AAM20168.1; -; mRNA.
DR RefSeq; NP_181525.2; NM_129554.4.
DR AlphaFoldDB; P58684; -.
DR SMR; P58684; -.
DR BioGRID; 3921; 18.
DR IntAct; P58684; 6.
DR STRING; 3702.AT2G39960.1; -.
DR PaxDb; P58684; -.
DR PRIDE; P58684; -.
DR ProteomicsDB; 232523; -.
DR EnsemblPlants; AT2G39960.1; AT2G39960.1; AT2G39960.
DR GeneID; 818583; -.
DR Gramene; AT2G39960.1; AT2G39960.1; AT2G39960.
DR KEGG; ath:AT2G39960; -.
DR Araport; AT2G39960; -.
DR TAIR; locus:2061161; AT2G39960.
DR eggNOG; ENOG502QVCN; Eukaryota.
DR HOGENOM; CLU_100048_0_0_1; -.
DR InParanoid; P58684; -.
DR OMA; DMRKYDD; -.
DR OrthoDB; 1395649at2759; -.
DR PhylomeDB; P58684; -.
DR PRO; PR:P58684; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P58684; baseline and differential.
DR Genevisible; P58684; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IBA:GO_Central.
DR GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR InterPro; IPR009582; Spc2/SPCS2.
DR PANTHER; PTHR13085; PTHR13085; 1.
DR Pfam; PF06703; SPC25; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..192
FT /note="Signal peptidase complex subunit 2"
FT /id="PRO_0000221167"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q28250"
FT TRANSMEM 47..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..78
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q28250"
FT TRANSMEM 79..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q28250"
SQ SEQUENCE 192 AA; 21642 MW; E7DCDCF425BBB80C CRC64;
MEEKKTESTN KNVKKANLLD HHSIKHILDE SVSDIVTSRG YKEDVRLSNL KLILGTIIIV
VALVAQFYNK KFPENRDFLI GCIALYVVLN AVLQLILYTK EKNAILFTYP PEGSFTSTGL
VVSSKLPRFS DQYTLTIDSA DPKSISAGKS VQLTKSVTQW FTKDGVLVEG LFWKDVEALI
KNYAEEEPKK KK
