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P67812 (SC11A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal peptidase complex catalytic subunit SEC11A

EC=3.4.21.89
Alternative name(s):
Endopeptidase SP18
Microsomal signal peptidase 18 kDa subunit
Short name=SPase 18 kDa subunit
SEC11 homolog A
SEC11-like protein 1
SPC18
Gene names
Name:SEC11A
Synonyms:SEC11L1, SPC18, SPCS4A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length179 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum By similarity.

Catalytic activity

Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.

Subunit structure

Component of the microsomal signal peptidase complex which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and SPCS3 By similarity.

Subcellular location

Microsome membrane; Single-pass type II membrane protein By similarity. Endoplasmic reticulum membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the peptidase S26B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 179179Signal peptidase complex catalytic subunit SEC11A
PRO_0000109543

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3620Helical; Signal-anchor for type II membrane protein; Potential
Topological domain37 – 179143Lumenal Potential

Sites

Active site561 By similarity

Experimental info

Sequence conflict191Y → C in AAD19640. Ref.1
Sequence conflict191Y → C in AAC36354. Ref.6
Sequence conflict421I → T in BAD96944. Ref.4
Sequence conflict1631K → R in AAD19640. Ref.1
Sequence conflict1631K → R in AAC36354. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P67812 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: DFD245A17BA3B47F

FASTA17920,625
        10         20         30         40         50         60 
MLSLDFLDDV RRMNKRQLYY QVLNFGMIVS SALMIWKGLM VITGSESPIV VVLSGSMEPA 

        70         80         90        100        110        120 
FHRGDLLFLT NRVEDPIRVG EIVVFRIEGR EIPIVHRVLK IHEKQNGHIK FLTKGDNNAV 

       130        140        150        160        170 
DDRGLYKQGQ HWLEKKDVVG RARGFVPYIG IVTILMNDYP KFKYAVLFLL GLFVLVHRE 

« Hide

References

« Hide 'large scale' references
[1]"Human signal peptidase 18 kDa subunit, mRNA complete cds."
Xie T.P., Wu M.C., Liu X.P., Wang H.J., Liang Y., Guo Y.J.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hepatoma.
[2]"Human microsomal signal peptidase."
Zhang J., Mao M., Liu T., Wu J., Zhang Q., Fu G., Shen Y., Zhou J., Yu Y., Wang Z., Chen S., Chen Z.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Gastric mucosa.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon and Muscle.
[7]Xie T.P., Liu X.P., Wang H.J., Liang Y., Wang H., Qian W.Z., Wei L.X., Liu Y.J., He P., Guo Y.J.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-179.
Tissue: Hepatoma.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF108945 mRNA. Translation: AAD19640.1.
AF061737 mRNA. Translation: AAD17526.1.
AK223224 mRNA. Translation: BAD96944.1.
AK314146 mRNA. Translation: BAG36834.1.
CH471101 Genomic DNA. Translation: EAX01954.1.
BC000359 mRNA. Translation: AAH00359.3.
BC014508 mRNA. Translation: AAH14508.1.
AF090315 mRNA. Translation: AAC36354.1.
RefSeqNP_001258847.1. NM_001271918.1.
NP_001258848.1. NM_001271919.1.
NP_001258849.1. NM_001271920.1.
NP_001258850.1. NM_001271921.1.
NP_001258851.1. NM_001271922.1.
NP_055115.1. NM_014300.3.
UniGeneHs.9534.

3D structure databases

ProteinModelPortalP67812.
SMRP67812. Positions 49-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117037. 5 interactions.
IntActP67812. 2 interactions.
MINTMINT-1387363.
STRING9606.ENSP00000268220.

Protein family/group databases

MEROPSS26.009.

PTM databases

PhosphoSiteP67812.

Polymorphism databases

DMDM54039634.

Proteomic databases

PaxDbP67812.
PRIDEP67812.

Protocols and materials databases

DNASU23478.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268220; ENSP00000268220; ENSG00000140612.
GeneID23478.
KEGGhsa:23478.
UCSCuc002blb.2. human.

Organism-specific databases

CTD23478.
GeneCardsGC15M085212.
HGNCHGNC:17718. SEC11A.
neXtProtNX_P67812.
PharmGKBPA162402586.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0681.
HOGENOMHOG000111516.
HOVERGENHBG057279.
InParanoidP67812.
KOK13280.
OMATILISEN.
PhylomeDBP67812.
TreeFamTF313648.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP67812.
BgeeP67812.
CleanExHS_SEC11A.
GenevestigatorP67812.

Family and domain databases

Gene3D2.10.109.10. 1 hit.
InterProIPR019758. Pept_S26A_signal_pept_1_CS.
IPR019756. Pept_S26A_signal_pept_1_Ser-AS.
IPR028360. Peptidase_S24/S26_b-rbn.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR001733. Peptidase_S26B.
[Graphical view]
PANTHERPTHR10806. PTHR10806. 1 hit.
PfamPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00728. SIGNALPTASE.
SUPFAMSSF51306. SSF51306. 1 hit.
TIGRFAMsTIGR02228. sigpep_I_arch. 1 hit.
PROSITEPS00501. SPASE_I_1. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSEC11A. human.
GenomeRNAi23478.
NextBio45823.
PROP67812.

Entry information

Entry nameSC11A_HUMAN
AccessionPrimary (citable) accession number: P67812
Secondary accession number(s): B2RAD7 expand/collapse secondary AC list , O75957, P21378, Q53FQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM