Full text data of SPCS3
SPCS3
(SPC22)
[Confidence: high (present in two of the MS resources)]
Signal peptidase complex subunit 3; 3.4.-.- (Microsomal signal peptidase 22/23 kDa subunit; SPC22/23; SPase 22/23 kDa subunit)
Signal peptidase complex subunit 3; 3.4.-.- (Microsomal signal peptidase 22/23 kDa subunit; SPC22/23; SPase 22/23 kDa subunit)
UniProt
P61009
ID SPCS3_HUMAN Reviewed; 180 AA.
AC P61009; P12280; Q9H0S7;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 26-APR-2004, sequence version 1.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=Signal peptidase complex subunit 3;
DE EC=3.4.-.-;
DE AltName: Full=Microsomal signal peptidase 22/23 kDa subunit;
DE Short=SPC22/23;
DE Short=SPase 22/23 kDa subunit;
GN Name=SPCS3; Synonyms=SPC22; ORFNames=UNQ1841/PRO3567;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [6]
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 [7]
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 -!- 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 SPCS3 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; AL136660; CAB66595.1; -; mRNA.
DR EMBL; AK026302; BAB15437.1; -; mRNA.
DR EMBL; AY359044; AAQ89403.1; -; mRNA.
DR EMBL; BC047290; AAH47290.1; -; mRNA.
DR RefSeq; NP_068747.1; NM_021928.3.
DR UniGene; Hs.42194; -.
DR ProteinModelPortal; P61009; -.
DR IntAct; P61009; 1.
DR MINT; MINT-3022145; -.
DR STRING; 9606.ENSP00000264597; -.
DR PhosphoSite; P61009; -.
DR DMDM; 46577648; -.
DR PaxDb; P61009; -.
DR PRIDE; P61009; -.
DR DNASU; 60559; -.
DR Ensembl; ENST00000503362; ENSP00000427463; ENSG00000129128.
DR GeneID; 60559; -.
DR KEGG; hsa:60559; -.
DR UCSC; uc003iur.4; human.
DR CTD; 60559; -.
DR GeneCards; GC04P177241; -.
DR H-InvDB; HIX0200687; -.
DR HGNC; HGNC:26212; SPCS3.
DR HPA; HPA053180; -.
DR neXtProt; NX_P61009; -.
DR PharmGKB; PA134910080; -.
DR eggNOG; NOG294543; -.
DR HOGENOM; HOG000246793; -.
DR HOVERGEN; HBG054497; -.
DR InParanoid; P61009; -.
DR KO; K12948; -.
DR OMA; DMKSKYF; -.
DR OrthoDB; EOG773XHG; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SPCS3; human.
DR GenomeRNAi; 60559; -.
DR NextBio; 65441; -.
DR PRO; PR:P61009; -.
DR Bgee; P61009; -.
DR CleanEx; HS_SPCS3; -.
DR Genevestigator; P61009; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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 InterPro; IPR007653; SPC22.
DR PANTHER; PTHR12804; PTHR12804; 1.
DR Pfam; PF04573; SPC22; 1.
DR PIRSF; PIRSF016089; SPC22; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Membrane; Microsome; Protease; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 180 Signal peptidase complex subunit 3.
FT /FTId=PRO_0000218938.
FT TOPO_DOM 1 11 Cytoplasmic (Potential).
FT TRANSMEM 12 32 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 33 180 Lumenal (Potential).
FT CARBOHYD 141 141 N-linked (GlcNAc...).
FT CONFLICT 68 68 F -> S (in Ref. 1; CAB66595).
SQ SEQUENCE 180 AA; 20313 MW; 342AB8E0F3F6D71A CRC64;
MNTVLSRANS LFAFSLSVMA ALTFGCFITT AFKDRSVPVR LHVSRIMLKN VEDFTGPRER
SDLGFITFDI TADLENIFDW NVKQLFLYLS AEYSTKNNAL NQVVLWDKIV LRGDNPKLLL
KDMKTKYFFF DDGNGLKGNR NVTLTLSWNV VPNAGILPLV TGSGHVSVPF PDTYEITKSY
//
ID SPCS3_HUMAN Reviewed; 180 AA.
AC P61009; P12280; Q9H0S7;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 26-APR-2004, sequence version 1.
DT 22-JAN-2014, entry version 92.
DE RecName: Full=Signal peptidase complex subunit 3;
DE EC=3.4.-.-;
DE AltName: Full=Microsomal signal peptidase 22/23 kDa subunit;
DE Short=SPC22/23;
DE Short=SPase 22/23 kDa subunit;
GN Name=SPCS3; Synonyms=SPC22; ORFNames=UNQ1841/PRO3567;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [6]
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 [7]
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 -!- 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 SPCS3 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; AL136660; CAB66595.1; -; mRNA.
DR EMBL; AK026302; BAB15437.1; -; mRNA.
DR EMBL; AY359044; AAQ89403.1; -; mRNA.
DR EMBL; BC047290; AAH47290.1; -; mRNA.
DR RefSeq; NP_068747.1; NM_021928.3.
DR UniGene; Hs.42194; -.
DR ProteinModelPortal; P61009; -.
DR IntAct; P61009; 1.
DR MINT; MINT-3022145; -.
DR STRING; 9606.ENSP00000264597; -.
DR PhosphoSite; P61009; -.
DR DMDM; 46577648; -.
DR PaxDb; P61009; -.
DR PRIDE; P61009; -.
DR DNASU; 60559; -.
DR Ensembl; ENST00000503362; ENSP00000427463; ENSG00000129128.
DR GeneID; 60559; -.
DR KEGG; hsa:60559; -.
DR UCSC; uc003iur.4; human.
DR CTD; 60559; -.
DR GeneCards; GC04P177241; -.
DR H-InvDB; HIX0200687; -.
DR HGNC; HGNC:26212; SPCS3.
DR HPA; HPA053180; -.
DR neXtProt; NX_P61009; -.
DR PharmGKB; PA134910080; -.
DR eggNOG; NOG294543; -.
DR HOGENOM; HOG000246793; -.
DR HOVERGEN; HBG054497; -.
DR InParanoid; P61009; -.
DR KO; K12948; -.
DR OMA; DMKSKYF; -.
DR OrthoDB; EOG773XHG; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SPCS3; human.
DR GenomeRNAi; 60559; -.
DR NextBio; 65441; -.
DR PRO; PR:P61009; -.
DR Bgee; P61009; -.
DR CleanEx; HS_SPCS3; -.
DR Genevestigator; P61009; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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 InterPro; IPR007653; SPC22.
DR PANTHER; PTHR12804; PTHR12804; 1.
DR Pfam; PF04573; SPC22; 1.
DR PIRSF; PIRSF016089; SPC22; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Membrane; Microsome; Protease; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1 180 Signal peptidase complex subunit 3.
FT /FTId=PRO_0000218938.
FT TOPO_DOM 1 11 Cytoplasmic (Potential).
FT TRANSMEM 12 32 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 33 180 Lumenal (Potential).
FT CARBOHYD 141 141 N-linked (GlcNAc...).
FT CONFLICT 68 68 F -> S (in Ref. 1; CAB66595).
SQ SEQUENCE 180 AA; 20313 MW; 342AB8E0F3F6D71A CRC64;
MNTVLSRANS LFAFSLSVMA ALTFGCFITT AFKDRSVPVR LHVSRIMLKN VEDFTGPRER
SDLGFITFDI TADLENIFDW NVKQLFLYLS AEYSTKNNAL NQVVLWDKIV LRGDNPKLLL
KDMKTKYFFF DDGNGLKGNR NVTLTLSWNV VPNAGILPLV TGSGHVSVPF PDTYEITKSY
//