SPC1_SCHPO
ID SPC1_SCHPO Reviewed; 78 AA.
AC G2TRR4;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Signal peptidase complex subunit 1;
GN Name=spc1 {ECO:0000312|PomBase:SPBC887.22};
GN Synonyms=new19 {ECO:0000312|PomBase:SPBC887.22}; ORFNames=SPBC887.22;
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 IDENTIFICATION.
RX PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA Hagan I.M., Miller C.J.;
RT "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT additional genes required for growth and viability.";
RL Genetics 187:1207-1217(2011).
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. Dispensable for SPC enzymatic activity.
CC {ECO:0000250|UniProtKB:P46965}.
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:P46965,
CC ECO:0000250|UniProtKB:P67812}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P46965}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SPCS1 family. {ECO:0000305}.
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DR EMBL; CU329671; CCD31381.1; -; Genomic_DNA.
DR RefSeq; XP_004001729.1; XM_004001680.1.
DR AlphaFoldDB; G2TRR4; -.
DR SMR; G2TRR4; -.
DR BioGRID; 4254067; 3.
DR STRING; 4896.SPBC887.22.1; -.
DR MaxQB; G2TRR4; -.
DR PaxDb; G2TRR4; -.
DR EnsemblFungi; SPBC887.22.1; SPBC887.22.1:pep; SPBC887.22.
DR PomBase; SPBC887.22; spc1.
DR VEuPathDB; FungiDB:SPBC887.22; -.
DR HOGENOM; CLU_134505_2_1_1; -.
DR InParanoid; G2TRR4; -.
DR OMA; CIPAWPM; -.
DR PRO; PR:G2TRR4; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
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; IPR037713; Spc1.
DR InterPro; IPR009542; Spc1/SPCS1.
DR PANTHER; PTHR13202; PTHR13202; 1.
DR PANTHER; PTHR13202:SF0; PTHR13202:SF0; 1.
DR Pfam; PF06645; SPC12; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..78
FT /note="Signal peptidase complex subunit 1"
FT /id="PRO_0000416499"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..42
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 78 AA; 8990 MW; A74D2EB139DD0CB6 CRC64;
MNYLEGTIDF AGQLRCQKYM NYGLCTSAVI SYIYGYLVQD SYCVIKLFLI LASLVALVCL
PAWSMYNKNP LKFQKKKE
