ID A0A2R9CC84_PANPA Unreviewed; 195 AA.
AC A0A2R9CC84;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11 {ECO:0000256|RuleBase:RU362047};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362047};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000035945.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000035945.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000035945.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000677,
CC ECO:0000256|RuleBase:RU362047};
CC -!- SUBUNIT: Component of the signal peptidase complex.
CC {ECO:0000256|RuleBase:RU362047}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004648}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family.
CC {ECO:0000256|ARBA:ARBA00011035, ECO:0000256|RuleBase:RU362047}.
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; AJFE02021830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02021831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02021832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02021833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02021834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02021835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02021836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9CC84; -.
DR STRING; 9597.ENSPPAP00000035945; -.
DR Ensembl; ENSPPAT00000058834.1; ENSPPAP00000035945.1; ENSPPAG00000040737.1.
DR GeneTree; ENSGT00390000015600; -.
DR Proteomes; UP000240080; Chromosome 15.
DR Bgee; ENSPPAG00000040737; Expressed in placenta and 6 other cell types or tissues.
DR GO; GO:0005787; C:signal peptidase complex; IEA:UniProt.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:UniProtKB-UniRule.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR001733; Peptidase_S26B.
DR NCBIfam; TIGR02228; sigpep_I_arch; 1.
DR PANTHER; PTHR10806; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11; 1.
DR PANTHER; PTHR10806:SF36; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11A; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU362047}; Hydrolase {ECO:0000256|RuleBase:RU362047};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362047};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU362047};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW ECO:0000256|RuleBase:RU362047};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362047};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362047}.
FT TRANSMEM 18..36
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362047"
FT TRANSMEM 166..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362047"
FT DOMAIN 39..127
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
SQ SEQUENCE 195 AA; 22581 MW; 5DBEAA38B9984F95 CRC64;
MLSLDFLDDV RRMNKRQLYY QVLNFGMIVS SALMIWKGLM VITGSESPIV VVLSGSMEPA
FHRGDLLFLT NRVEDPIRVG EIVVFRIEGR EIPIVHRVLK IHEKQNGHIK FLTKGDNNAV
DDRGLYKQGQ HWLEKKDVVG RARGFVPYIG IVTILMNDYP KFKVRVSCLL LSEMLLVWTI
NFVFILPFPY IEFKL
//
