SEC11_DICDI
ID SEC11_DICDI Reviewed; 179 AA.
AC Q86JD4; Q551R3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Signal peptidase complex catalytic subunit sec11;
DE EC=3.4.21.89 {ECO:0000250|UniProtKB:P67812};
GN Name=sec11; ORFNames=DDB_G0276359;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalytic component of the signal peptidase complex (SPC)
CC which catalyzes the cleavage of N-terminal signal sequences from
CC nascent proteins as they are translocated into the lumen of the
CC endoplasmic reticulum. Specifically cleaves N-terminal signal peptides
CC that contain a hydrophobic alpha-helix (h-region) shorter than 18-20
CC amino acids. {ECO:0000250|UniProtKB:P67812}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000250|UniProtKB:P67812};
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:P67812}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P67811}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P67811}.
CC -!- DOMAIN: The C-terminal short (CTS) helix is essential for catalytic
CC activity. It may be accommodated as a transmembrane helix in the
CC thinned membrane environment of the complex, similarly to the signal
CC peptide in the complex substrates. {ECO:0000250|UniProtKB:P67812}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
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DR EMBL; AAFI02000014; EAL69260.1; -; Genomic_DNA.
DR RefSeq; XP_643198.1; XM_638106.1.
DR AlphaFoldDB; Q86JD4; -.
DR SMR; Q86JD4; -.
DR STRING; 44689.DDB0237791; -.
DR MEROPS; S26.010; -.
DR PaxDb; Q86JD4; -.
DR EnsemblProtists; EAL69260; EAL69260; DDB_G0276359.
DR GeneID; 8620472; -.
DR KEGG; ddi:DDB_G0276359; -.
DR dictyBase; DDB_G0276359; sec11.
DR eggNOG; KOG3342; Eukaryota.
DR HOGENOM; CLU_089996_0_0_1; -.
DR InParanoid; Q86JD4; -.
DR OMA; YNVRGKD; -.
DR PhylomeDB; Q86JD4; -.
DR PRO; PR:Q86JD4; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; ISS:dictyBase.
DR GO; GO:0008233; F:peptidase activity; ISS:dictyBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; ISS:dictyBase.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR001733; Peptidase_S26B.
DR InterPro; IPR037712; SEC11A.
DR PANTHER; PTHR10806; PTHR10806; 1.
DR PANTHER; PTHR10806:SF28; PTHR10806:SF28; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR02228; sigpep_I_arch; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..179
FT /note="Signal peptidase complex catalytic subunit sec11"
FT /id="PRO_0000330653"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P67811"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..179
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P67811"
FT REGION 165..176
FT /note="C-terminal short (CTS) helix"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 57
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 96
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P67812"
FT ACT_SITE 122
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P67812"
SQ SEQUENCE 179 AA; 20145 MW; BF5DE6066C1F2D4E CRC64;
MNDIISKINP FSSIPKHQIA QQIVNFGLIV ATALMIWKGL MIFSGSESPI VVVLSGSMIP
AFFRGDLLYL NMEDGPFRVG EIVVFKIEGK EIPIVHRILQ IHEKEDGLYD IRTKGDNNNV
DDVGLYSPGQ RWLSRDHIIG RAKGFLPSVG MVTIVMHDYP QLKFFLVFVL AVFVLSTRE
