Full text data of SEC11A
SEC11A
(SEC11L1, SPC18, SPCS4A)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Signal peptidase complex catalytic subunit SEC11A; 3.4.21.89 (Endopeptidase SP18; Microsomal signal peptidase 18 kDa subunit; SPase 18 kDa subunit; SEC11 homolog A; SEC11-like protein 1; SPC18)
Signal peptidase complex catalytic subunit SEC11A; 3.4.21.89 (Endopeptidase SP18; Microsomal signal peptidase 18 kDa subunit; SPase 18 kDa subunit; SEC11 homolog A; SEC11-like protein 1; SPC18)
UniProt
P67812
ID SC11A_HUMAN Reviewed; 179 AA.
AC P67812; B2RAD7; O75957; P21378; Q53FQ8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-OCT-2004, sequence version 1.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11A;
DE EC=3.4.21.89;
DE AltName: Full=Endopeptidase SP18;
DE AltName: Full=Microsomal signal peptidase 18 kDa subunit;
DE Short=SPase 18 kDa subunit;
DE AltName: Full=SEC11 homolog A;
DE AltName: Full=SEC11-like protein 1;
DE AltName: Full=SPC18;
GN Name=SEC11A; Synonyms=SEC11L1, SPC18, SPCS4A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hepatoma;
RA Xie T.P., Wu M.C., Liu X.P., Wang H.J., Liang Y., Guo Y.J.;
RT "Human signal peptidase 18 kDa subunit, mRNA complete cds.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang J., Mao M., Liu T., Wu J., Zhang Q., Fu G., Shen Y., Zhou J.,
RA Yu Y., Wang Z., Chen S., Chen Z.;
RT "Human microsomal signal peptidase.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-179.
RC TISSUE=Hepatoma;
RA Xie T.P., Liu X.P., Wang H.J., Liang Y., Wang H., Qian W.Z., Wei L.X.,
RA Liu Y.J., He P., Guo Y.J.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF108945; AAD19640.1; -; mRNA.
DR EMBL; AF061737; AAD17526.1; -; mRNA.
DR EMBL; AK223224; BAD96944.1; -; mRNA.
DR EMBL; AK314146; BAG36834.1; -; mRNA.
DR EMBL; CH471101; EAX01954.1; -; Genomic_DNA.
DR EMBL; BC000359; AAH00359.3; -; mRNA.
DR EMBL; BC014508; AAH14508.1; -; mRNA.
DR EMBL; AF090315; AAC36354.1; -; mRNA.
DR RefSeq; NP_001258847.1; NM_001271918.1.
DR RefSeq; NP_001258848.1; NM_001271919.1.
DR RefSeq; NP_001258849.1; NM_001271920.1.
DR RefSeq; NP_001258850.1; NM_001271921.1.
DR RefSeq; NP_001258851.1; NM_001271922.1.
DR RefSeq; NP_055115.1; NM_014300.3.
DR UniGene; Hs.9534; -.
DR ProteinModelPortal; P67812; -.
DR IntAct; P67812; 2.
DR MINT; MINT-1387363; -.
DR STRING; 9606.ENSP00000268220; -.
DR MEROPS; S26.009; -.
DR PhosphoSite; P67812; -.
DR DMDM; 54039634; -.
DR PaxDb; P67812; -.
DR PRIDE; P67812; -.
DR DNASU; 23478; -.
DR Ensembl; ENST00000268220; ENSP00000268220; ENSG00000140612.
DR GeneID; 23478; -.
DR KEGG; hsa:23478; -.
DR UCSC; uc002blb.2; human.
DR CTD; 23478; -.
DR GeneCards; GC15M085212; -.
DR HGNC; HGNC:17718; SEC11A.
DR neXtProt; NX_P67812; -.
DR PharmGKB; PA162402586; -.
DR eggNOG; COG0681; -.
DR HOGENOM; HOG000111516; -.
DR HOVERGEN; HBG057279; -.
DR InParanoid; P67812; -.
DR KO; K13280; -.
DR OMA; TILISEN; -.
DR PhylomeDB; P67812; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SEC11A; human.
DR GenomeRNAi; 23478; -.
DR NextBio; 45823; -.
DR PRO; PR:P67812; -.
DR ArrayExpress; P67812; -.
DR Bgee; P67812; -.
DR CleanEx; HS_SEC11A; -.
DR Genevestigator; P67812; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
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 1: Evidence at protein level;
KW Complete proteome; Endoplasmic reticulum; Hydrolase; Membrane;
KW Microsome; Protease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 179 Signal peptidase complex catalytic
FT subunit SEC11A.
FT /FTId=PRO_0000109543.
FT TOPO_DOM 1 16 Cytoplasmic (Potential).
FT TRANSMEM 17 36 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 37 179 Lumenal (Potential).
FT ACT_SITE 56 56 By similarity.
FT CONFLICT 19 19 Y -> C (in Ref. 1; AAD19640 and 6;
FT AAC36354).
FT CONFLICT 42 42 I -> T (in Ref. 4; BAD96944).
FT CONFLICT 163 163 K -> R (in Ref. 1; AAD19640 and 6;
FT AAC36354).
SQ SEQUENCE 179 AA; 20625 MW; DFD245A17BA3B47F CRC64;
MLSLDFLDDV RRMNKRQLYY QVLNFGMIVS SALMIWKGLM VITGSESPIV VVLSGSMEPA
FHRGDLLFLT NRVEDPIRVG EIVVFRIEGR EIPIVHRVLK IHEKQNGHIK FLTKGDNNAV
DDRGLYKQGQ HWLEKKDVVG RARGFVPYIG IVTILMNDYP KFKYAVLFLL GLFVLVHRE
//
ID SC11A_HUMAN Reviewed; 179 AA.
AC P67812; B2RAD7; O75957; P21378; Q53FQ8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-OCT-2004, sequence version 1.
DT 22-JAN-2014, entry version 88.
DE RecName: Full=Signal peptidase complex catalytic subunit SEC11A;
DE EC=3.4.21.89;
DE AltName: Full=Endopeptidase SP18;
DE AltName: Full=Microsomal signal peptidase 18 kDa subunit;
DE Short=SPase 18 kDa subunit;
DE AltName: Full=SEC11 homolog A;
DE AltName: Full=SEC11-like protein 1;
DE AltName: Full=SPC18;
GN Name=SEC11A; Synonyms=SEC11L1, SPC18, SPCS4A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hepatoma;
RA Xie T.P., Wu M.C., Liu X.P., Wang H.J., Liang Y., Guo Y.J.;
RT "Human signal peptidase 18 kDa subunit, mRNA complete cds.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang J., Mao M., Liu T., Wu J., Zhang Q., Fu G., Shen Y., Zhou J.,
RA Yu Y., Wang Z., Chen S., Chen Z.;
RT "Human microsomal signal peptidase.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-179.
RC TISSUE=Hepatoma;
RA Xie T.P., Liu X.P., Wang H.J., Liang Y., Wang H., Qian W.Z., Wei L.X.,
RA Liu Y.J., He P., Guo Y.J.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF108945; AAD19640.1; -; mRNA.
DR EMBL; AF061737; AAD17526.1; -; mRNA.
DR EMBL; AK223224; BAD96944.1; -; mRNA.
DR EMBL; AK314146; BAG36834.1; -; mRNA.
DR EMBL; CH471101; EAX01954.1; -; Genomic_DNA.
DR EMBL; BC000359; AAH00359.3; -; mRNA.
DR EMBL; BC014508; AAH14508.1; -; mRNA.
DR EMBL; AF090315; AAC36354.1; -; mRNA.
DR RefSeq; NP_001258847.1; NM_001271918.1.
DR RefSeq; NP_001258848.1; NM_001271919.1.
DR RefSeq; NP_001258849.1; NM_001271920.1.
DR RefSeq; NP_001258850.1; NM_001271921.1.
DR RefSeq; NP_001258851.1; NM_001271922.1.
DR RefSeq; NP_055115.1; NM_014300.3.
DR UniGene; Hs.9534; -.
DR ProteinModelPortal; P67812; -.
DR IntAct; P67812; 2.
DR MINT; MINT-1387363; -.
DR STRING; 9606.ENSP00000268220; -.
DR MEROPS; S26.009; -.
DR PhosphoSite; P67812; -.
DR DMDM; 54039634; -.
DR PaxDb; P67812; -.
DR PRIDE; P67812; -.
DR DNASU; 23478; -.
DR Ensembl; ENST00000268220; ENSP00000268220; ENSG00000140612.
DR GeneID; 23478; -.
DR KEGG; hsa:23478; -.
DR UCSC; uc002blb.2; human.
DR CTD; 23478; -.
DR GeneCards; GC15M085212; -.
DR HGNC; HGNC:17718; SEC11A.
DR neXtProt; NX_P67812; -.
DR PharmGKB; PA162402586; -.
DR eggNOG; COG0681; -.
DR HOGENOM; HOG000111516; -.
DR HOVERGEN; HBG057279; -.
DR InParanoid; P67812; -.
DR KO; K13280; -.
DR OMA; TILISEN; -.
DR PhylomeDB; P67812; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SEC11A; human.
DR GenomeRNAi; 23478; -.
DR NextBio; 45823; -.
DR PRO; PR:P67812; -.
DR ArrayExpress; P67812; -.
DR Bgee; P67812; -.
DR CleanEx; HS_SEC11A; -.
DR Genevestigator; P67812; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
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 1: Evidence at protein level;
KW Complete proteome; Endoplasmic reticulum; Hydrolase; Membrane;
KW Microsome; Protease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1 179 Signal peptidase complex catalytic
FT subunit SEC11A.
FT /FTId=PRO_0000109543.
FT TOPO_DOM 1 16 Cytoplasmic (Potential).
FT TRANSMEM 17 36 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 37 179 Lumenal (Potential).
FT ACT_SITE 56 56 By similarity.
FT CONFLICT 19 19 Y -> C (in Ref. 1; AAD19640 and 6;
FT AAC36354).
FT CONFLICT 42 42 I -> T (in Ref. 4; BAD96944).
FT CONFLICT 163 163 K -> R (in Ref. 1; AAD19640 and 6;
FT AAC36354).
SQ SEQUENCE 179 AA; 20625 MW; DFD245A17BA3B47F CRC64;
MLSLDFLDDV RRMNKRQLYY QVLNFGMIVS SALMIWKGLM VITGSESPIV VVLSGSMEPA
FHRGDLLFLT NRVEDPIRVG EIVVFRIEGR EIPIVHRVLK IHEKQNGHIK FLTKGDNNAV
DDRGLYKQGQ HWLEKKDVVG RARGFVPYIG IVTILMNDYP KFKYAVLFLL GLFVLVHRE
//