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Database: UniProt
Entry: Q5RC30
LinkDB: Q5RC30
Original site: Q5RC30 
ID   SC11C_PONAB             Reviewed;         192 AA.
AC   Q5RC30;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   14-MAY-2014, entry version 71.
DE   RecName: Full=Signal peptidase complex catalytic subunit SEC11C;
DE            EC=3.4.21.89;
DE   AltName: Full=Microsomal signal peptidase 21 kDa subunit;
DE            Short=SPase 21 kDa subunit;
DE   AltName: Full=SEC11 homolog C;
DE   AltName: Full=SEC11-like protein 3;
DE   AltName: Full=SPC21;
GN   Name=SEC11C; Synonyms=SEC11L3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the microsomal signal peptidase complex
CC       which removes signal peptides from nascent proteins as they are
CC       translocated into the lumen of the endoplasmic reticulum (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Cleavage of hydrophobic, N-terminal signal or
CC       leader sequences from secreted and periplasmic proteins.
CC   -!- SUBUNIT: Component of the microsomal signal peptidase complex
CC       which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and
CC       SPCS3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Single-pass type II
CC       membrane protein (By similarity). Endoplasmic reticulum membrane;
CC       Single-pass type II membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S26B family.
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DR   EMBL; CR858452; CAH90680.1; -; mRNA.
DR   RefSeq; NP_001127320.1; NM_001133848.2.
DR   UniGene; Pab.10996; -.
DR   ProteinModelPortal; Q5RC30; -.
DR   SMR; Q5RC30; 62-113.
DR   MEROPS; S26.010; -.
DR   PRIDE; Q5RC30; -.
DR   Ensembl; ENSPPYT00000010728; ENSPPYP00000010320; ENSPPYG00000009189.
DR   GeneID; 100174381; -.
DR   KEGG; pon:100174381; -.
DR   CTD; 90701; -.
DR   GeneTree; ENSGT00390000015600; -.
DR   HOVERGEN; HBG057279; -.
DR   InParanoid; Q5RC30; -.
DR   KO; K13280; -.
DR   OMA; VYNVKDK; -.
DR   OrthoDB; EOG7V4B0P; -.
DR   TreeFam; TF313648; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   Gene3D; 2.10.109.10; -; 1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR028360; Peptidase_S24/S26_b-rbn.
DR   InterPro; IPR019759; Peptidase_S24_S26.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR   InterPro; IPR001733; Peptidase_S26B.
DR   PANTHER; PTHR10806; PTHR10806; 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.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Endoplasmic reticulum; Hydrolase; Membrane;
KW   Microsome; Protease; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    192       Signal peptidase complex catalytic
FT                                subunit SEC11C.
FT                                /FTId=PRO_0000109550.
FT   TOPO_DOM      2     28       Cytoplasmic (Potential).
FT   TRANSMEM     29     48       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     49    192       Lumenal (Potential).
FT   ACT_SITE     68     68       By similarity.
SQ   SEQUENCE   192 AA;  21542 MW;  74FBC5F765791D9F CRC64;
     MVRAGAVGAH LPASGLDIFG DLKKMNKRQL YYQVLNFAMI VSSALMIWKG LIVLTGSESP
     IVVVLSGSME PAFHRGDLLF LTNFREDPIR AGEIVVFKVE GRDIPIVHRV IKVHEKDNGD
     IKFLTKGDNN EVDDRGLYKE GQNWLEKKDV VGRARGFLPY VGMVTIIMND YPKFKYALLA
     VMGAYVLLKR ES
//
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