Q9BY50 (SC11C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Signal peptidase complex catalytic subunit SEC11C
EC=3.4.21.89

Alternative name(s):
Microsomal signal peptidase 21 kDa subunit
Short name=SPase 21 kDa subunit
SEC11 homolog C
SEC11-like protein 3
SPC21

Gene names

Name:	SEC11C
Synonyms:	SEC11L3, SPC21, SPCS4C

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Hydrolase Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane Traceable author statement. Source: Reactome energy reserve metabolic process Traceable author statement. Source: Reactome proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of insulin secretion Traceable author statement. Source: Reactome signal peptide processing Inferred from electronic annotation. Source: InterPro small molecule metabolic process Traceable author statement. Source: Reactome translation Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	serine-type peptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 192	191	Signal peptidase complex catalytic subunit SEC11C		PRO_0000109548
Regions
	Topological domain	2 – 28	27	Cytoplasmic Potential
	Transmembrane	29 – 48	20	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	49 – 192	144	Lumenal Potential
Sites
	Active site	68	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9BY50 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 74FBC5F765791D9F	FASTA	192	21,542
	10 20 30 40 50 60 MVRAGAVGAH LPASGLDIFG DLKKMNKRQL YYQVLNFAMI VSSALMIWKG LIVLTGSESP 70 80 90 100 110 120 IVVVLSGSME PAFHRGDLLF LTNFREDPIR AGEIVVFKVE GRDIPIVHRV IKVHEKDNGD 130 140 150 160 170 180 IKFLTKGDNN EVDDRGLYKE GQNWLEKKDV VGRARGFLPY VGMVTIIMND YPKFKYALLA 190 VMGAYVLLKR ES

References

[1]	"A novel gene expressed in human liver cancer tissue." Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver cancer.
[2]	"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. , 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]. Tissue: Cerebellum.
[3]	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. , 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].
[4]	"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: Pancreas.
[5]	"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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF212233 mRNA. Translation: AAK14919.1. AK314107 mRNA. Translation: BAG36800.1. CH471096 Genomic DNA. Translation: EAW63090.1. BC009703 mRNA. Translation: AAH09703.1.
IPI	IPI00219436.
RefSeq	NP_150596.1. NM_033280.2.
UniGene	Hs.45107.
3D structure databases
ProteinModelPortal	Q9BY50.
SMR	Q9BY50. Positions 61-158.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BY50. 2 interactions.
STRING	9606.ENSP00000299714.
Protein family/group databases
MEROPS	S26.010.
PTM databases
PhosphoSite	Q9BY50.
Polymorphism databases
DMDM	17368701.
Proteomic databases
PaxDb	Q9BY50.
PeptideAtlas	Q9BY50.
PRIDE	Q9BY50.
Protocols and materials databases
DNASU	90701.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000587834; ENSP00000468633; ENSG00000166562.
GeneID	90701.
KEGG	hsa:90701.
UCSC	uc002lht.3. human.
Organism-specific databases
CTD	90701.
GeneCards	GC18P056807.
HGNC	HGNC:23400. SEC11C.
HPA	HPA026816.
neXtProt	NX_Q9BY50.
PharmGKB	PA162402587.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0681.
HOGENOM	HOG000111516.
HOVERGEN	HBG057279.
InParanoid	Q9BY50.
KO	K13280.
OMA	NNVDDRG.
OrthoDB	EOG4ZPDW9.
PhylomeDB	Q9BY50.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease. REACT_17015. Metabolism of proteins. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q9BY50.
Bgee	Q9BY50.
CleanEx	HS_SEC11C.
Genevestigator	Q9BY50.
GermOnline	ENSG00000166562. Homo sapiens.
Family and domain databases
Gene3D	2.10.109.10. 1 hit.
InterPro	IPR019758. Pept_S26A_signal_pept_1_CS. IPR019756. Pept_S26A_signal_pept_1_Ser-AS. IPR019759. Peptidase_S24_S26. IPR015927. Peptidase_S24_S26A/B/C. IPR011056. Peptidase_S24_S26A/B/C_b-rbn. IPR001733. Peptidase_S26B. [Graphical view]
PANTHER	PTHR10806. PTHR10806. 1 hit.
Pfam	PF00717. Peptidase_S24. 1 hit. [Graphical view]
PRINTS	PR00728. SIGNALPTASE.
SUPFAM	SSF51306. Pept_S24_S26_C. 1 hit.
TIGRFAMs	TIGR02228. sigpep_I_arch. 1 hit.
PROSITE	PS00501. SPASE_I_1. 1 hit. PS00761. SPASE_I_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	90701.
NextBio	76939.

Entry information

Entry name

SC11C_HUMAN

Accession

Primary (citable) accession number: Q9BY50
Secondary accession number(s): B2RAA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.