ID   A0A1Z5RD73_SORBI        Unreviewed;       192 AA.
AC   A0A1Z5RD73;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Signal peptidase complex subunit 2 {ECO:0000256|ARBA:ARBA00017057, ECO:0000256|RuleBase:RU368033};
GN   ORFNames=SORBI_3006G095200 {ECO:0000313|EMBL:OQU81657.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:OQU81657.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:OQU81657.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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. Enhances the enzymatic activity of SPC and facilitates the
CC       interactions between different components of the translocation site.
CC       {ECO:0000256|RuleBase:RU368033}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368033}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU368033}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SPCS2 family.
CC       {ECO:0000256|ARBA:ARBA00007324, ECO:0000256|RuleBase:RU368033}.
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DR   EMBL; CM000765; OQU81657.1; -; Genomic_DNA.
DR   RefSeq; XP_002447918.1; XM_002447873.1.
DR   AlphaFoldDB; A0A1Z5RD73; -.
DR   STRING; 4558.A0A1Z5RD73; -.
DR   EnsemblPlants; OQU81657; OQU81657; SORBI_3006G095200.
DR   GeneID; 8065833; -.
DR   Gramene; OQU81657; OQU81657; SORBI_3006G095200.
DR   KEGG; sbi:8065833; -.
DR   eggNOG; ENOG502QVCN; Eukaryota.
DR   InParanoid; A0A1Z5RD73; -.
DR   OMA; INKWDGT; -.
DR   OrthoDB; 8074at2759; -.
DR   Proteomes; UP000000768; Chromosome 6.
DR   GO; GO:0005787; C:signal peptidase complex; IBA:GO_Central.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-UniRule.
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; MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT; 1.
DR   PANTHER; PTHR13085:SF0; SIGNAL PEPTIDASE COMPLEX SUBUNIT 2; 1.
DR   Pfam; PF06703; SPC25; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU368033};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368033};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU368033};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU368033}.
FT   TRANSMEM        52..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368033"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368033"
SQ   SEQUENCE   192 AA;  21199 MW;  1986387057309E82 CRC64;
     MASDGAAATP AKVTPKKANL LDPYSIKHLL DETISDVVKN KGYTEDTRLG NWKLGIGAAV
     IAVALLAQFY PKKFPQNREF LLGCIALYVV LNVVLLILSY TKEKDAILFT HPPAGSFNST
     GLTISSKLPR FSDMYTLTIA SADPQSISAN KPVHFTKSVT KWFTKEGVLV EGLFWKDVEK
     LIDDYNSERK SK
//