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SPC2_SCHPO
ID   SPC2_SCHPO              Reviewed;         167 AA.
AC   Q9UTQ9;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Signal peptidase complex subunit 2;
DE   AltName: Full=Microsomal signal peptidase subunit 2;
GN   Name=spc2; ORFNames=SPAC1071.04c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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:0000250|UniProtKB:Q04969}.
CC   -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC       catalytic subunit sec11 and three accessory subunits spc1, spc2 and
CC       spc3 (By similarity). The complex induces a local thinning of the ER
CC       membrane which is used to measure the length of the signal peptide (SP)
CC       h-region of protein substrates. This ensures the selectivity of the
CC       complex towards h-regions shorter than 18-20 amino acids (By
CC       similarity). SPC associates with the translocon complex (By
CC       similarity). {ECO:0000250|UniProtKB:P67812,
CC       ECO:0000250|UniProtKB:Q04969}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the SPCS2 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB59880.1; -; Genomic_DNA.
DR   PIR; T37486; T37486.
DR   RefSeq; NP_594354.1; NM_001019775.1.
DR   AlphaFoldDB; Q9UTQ9; -.
DR   SMR; Q9UTQ9; -.
DR   BioGRID; 278190; 26.
DR   STRING; 4896.SPAC1071.04c.1; -.
DR   MaxQB; Q9UTQ9; -.
DR   PaxDb; Q9UTQ9; -.
DR   EnsemblFungi; SPAC1071.04c.1; SPAC1071.04c.1:pep; SPAC1071.04c.
DR   GeneID; 2541694; -.
DR   KEGG; spo:SPAC1071.04c; -.
DR   PomBase; SPAC1071.04c; spc2.
DR   VEuPathDB; FungiDB:SPAC1071.04c; -.
DR   HOGENOM; CLU_1595504_0_0_1; -.
DR   InParanoid; Q9UTQ9; -.
DR   OMA; LLTWWIS; -.
DR   PhylomeDB; Q9UTQ9; -.
DR   PRO; PR:Q9UTQ9; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005787; C:signal peptidase complex; ISO:PomBase.
DR   GO; GO:0045047; P:protein targeting to ER; ISO:PomBase.
DR   GO; GO:0006465; P:signal peptide processing; ISO:PomBase.
DR   InterPro; IPR009582; Spc2/SPCS2.
DR   PANTHER; PTHR13085; PTHR13085; 1.
DR   Pfam; PF06703; SPC25; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..167
FT                   /note="Signal peptidase complex subunit 2"
FT                   /id="PRO_0000362161"
FT   TOPO_DOM        1..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        58..68
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..167
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   167 AA;  19051 MW;  E8A906BBC7F98A74 CRC64;
     MPKYNVSDFK SKFDKELTNH FNKNGYKQSF VFEDIRLLIA IACIIPAGLA FGIEYVYGFG
     VLKSYLKYLL PLYFLASCLL TFWSSVVKGS TVYVATKKER HIKISADTFL PLKNKPLITT
     KFTVLKNRNA VQLEWSVPVA HIFEEDGQIS SATFEAEISK YLSQIEN
 
 
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