ID F6X2P5_HORSE Unreviewed; 229 AA.
AC F6X2P5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11 {ECO:0000256|RuleBase:RU362047};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362047};
GN Name=SEC11C {ECO:0000313|VGNC:VGNC:22782};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000014706.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000014706.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000014706.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000014706.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000014706.2};
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}.
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DR AlphaFoldDB; F6X2P5; -.
DR MEROPS; S26.010; -.
DR Ensembl; ENSECAT00000018052.3; ENSECAP00000014706.2; ENSECAG00000017024.4.
DR CTD; 90701; -.
DR VGNC; VGNC:22782; SEC11C.
DR GeneTree; ENSGT00390000015600; -.
DR HOGENOM; CLU_089996_0_0_1; -.
DR OrthoDB; 1114626at2759; -.
DR TreeFam; TF313648; -.
DR Proteomes; UP000002281; Chromosome 8.
DR Bgee; ENSECAG00000017024; Expressed in trophectoderm and 23 other cell types or tissues.
DR ExpressionAtlas; F6X2P5; baseline.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098796; C:membrane protein 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; 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:SF12; SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11C; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 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|RuleBase:RU362047};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
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 30..48
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362047"
FT DOMAIN 105..176
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
SQ SEQUENCE 229 AA; 25377 MW; DB3B787F82D51C21 CRC64;
MVRAGAVGTH LPASGLDIFG DLRKMNKRQL YYQVLNFAMI VSSALMIWKG LIVLTGSESP
IVVVLSMACQ VVPCPHPGSE LANPGLPRSG TCELNCCATR PALGSMEPAF HRGDLLFLTN
FREDPIRAGE IVVFKVEGRD IPIVHRVIKV HEKDNGDIKF LTKGDNNEVD DRGLYKEGQN
WLEKKDVVGR ARGFLPYVGM VTIIMNDYPK FKYALLAVMG AYVLLKRES
//
