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Protein

Signal peptidase complex subunit 3

Gene

Spcs3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

  • fat cell differentiation Source: MGI
  • signal peptide processing Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

ReactomeiR-MMU-422085. Synthesis, secretion, and deacylation of Ghrelin.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal peptidase complex subunit 3 (EC:3.4.-.-)
Alternative name(s):
Microsomal signal peptidase 22/23 kDa subunit
Short name:
SPC22/23
Short name:
SPase 22/23 kDa subunit
Gene namesi
Name:Spcs3
Synonyms:Spc22
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1923469. 6530401D17Rik.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence analysisAdd
BLAST
Transmembranei12 – 3221Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini33 – 180148LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • signal peptidase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 180180Signal peptidase complex subunit 3PRO_0000218939Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiQ9D365.
MaxQBiQ9D365.
PaxDbiQ9D365.
PRIDEiQ9D365.

PTM databases

SwissPalmiQ9D365.

Expressioni

Gene expression databases

BgeeiQ9D365.
GenevisibleiQ9D365. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000062660.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 16421HydrophobicAdd
BLAST

Sequence similaritiesi

Belongs to the SPCS3 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3372. Eukaryota.
ENOG4110TZP. LUCA.
GeneTreeiENSGT00390000009223.
HOGENOMiHOG000246793.
HOVERGENiHBG054497.
InParanoidiQ9D365.
KOiK12948.
OMAiILAFICA.
OrthoDBiEOG773XHG.
PhylomeDBiQ9D365.
TreeFamiTF300185.

Family and domain databases

InterProiIPR007653. SPC22.
[Graphical view]
PANTHERiPTHR12804. PTHR12804. 1 hit.
PfamiPF04573. SPC22. 1 hit.
[Graphical view]
PIRSFiPIRSF016089. SPC22. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9D365-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSLLSRANS LFAFTLSVMA ALTLGCILTT AFKDRSAPVR LHVSRILLKK
60 70 80 90 100
VEDFTGPRKK SDLGFITFHI SADLEKTFDW NVKQLFLYLS AEYSTKSNAV
110 120 130 140 150
NQVVLWDKIL LRGENPKLNL KDVKSKYFFF DDGHGLKGNR NVTLTLSWQV
160 170 180
IPIAGILPLV TGSGRVSVPF PDSYEIATTF
Length:180
Mass (Da):20,146
Last modified:June 1, 2001 - v1
Checksum:i7980A041F61AAFBB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31S → P in BAB28979 (PubMed:16141072).Curated
Sequence conflicti10 – 101S → P in BAB28979 (PubMed:16141072).Curated
Sequence conflicti14 – 141F → P in BAB28979 (PubMed:16141072).Curated
Sequence conflicti24 – 241L → P in BAB28979 (PubMed:16141072).Curated
Sequence conflicti41 – 411L → M in BAB28979 (PubMed:16141072).Curated
Sequence conflicti59 – 591K → N in BAC36797 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK018307 mRNA. Translation: BAB31154.1.
AK013740 mRNA. Translation: BAB28979.1.
AK077432 mRNA. Translation: BAC36797.1.
AL671914 Genomic DNA. Translation: CAM17322.1.
AL671914 Genomic DNA. Translation: CAM17323.1.
CH466616 Genomic DNA. Translation: EDL23842.1.
CH466616 Genomic DNA. Translation: EDL23843.1.
CCDSiCCDS30411.1.
CCDS53192.1.
RefSeqiNP_083817.1. NM_029541.3.
NP_084099.1. NM_029823.2.
UniGeneiMm.328305.
Mm.482965.

Genome annotation databases

EnsembliENSMUST00000057625; ENSMUSP00000062660; ENSMUSG00000048355.
ENSMUST00000058119; ENSMUSP00000051250; ENSMUSG00000048040.
GeneIDi76219.
76976.
KEGGimmu:76219.
mmu:76976.
UCSCiuc009uhz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK018307 mRNA. Translation: BAB31154.1.
AK013740 mRNA. Translation: BAB28979.1.
AK077432 mRNA. Translation: BAC36797.1.
AL671914 Genomic DNA. Translation: CAM17322.1.
AL671914 Genomic DNA. Translation: CAM17323.1.
CH466616 Genomic DNA. Translation: EDL23842.1.
CH466616 Genomic DNA. Translation: EDL23843.1.
CCDSiCCDS30411.1.
CCDS53192.1.
RefSeqiNP_083817.1. NM_029541.3.
NP_084099.1. NM_029823.2.
UniGeneiMm.328305.
Mm.482965.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000062660.

PTM databases

SwissPalmiQ9D365.

Proteomic databases

EPDiQ9D365.
MaxQBiQ9D365.
PaxDbiQ9D365.
PRIDEiQ9D365.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057625; ENSMUSP00000062660; ENSMUSG00000048355.
ENSMUST00000058119; ENSMUSP00000051250; ENSMUSG00000048040.
GeneIDi76219.
76976.
KEGGimmu:76219.
mmu:76976.
UCSCiuc009uhz.2. mouse.

Organism-specific databases

CTDi76219.
76976.
MGIiMGI:1923469. 6530401D17Rik.

Phylogenomic databases

eggNOGiKOG3372. Eukaryota.
ENOG4110TZP. LUCA.
GeneTreeiENSGT00390000009223.
HOGENOMiHOG000246793.
HOVERGENiHBG054497.
InParanoidiQ9D365.
KOiK12948.
OMAiILAFICA.
OrthoDBiEOG773XHG.
PhylomeDBiQ9D365.
TreeFamiTF300185.

Enzyme and pathway databases

ReactomeiR-MMU-422085. Synthesis, secretion, and deacylation of Ghrelin.

Miscellaneous databases

ChiTaRSiSpcs3. mouse.
PROiQ9D365.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D365.
GenevisibleiQ9D365. MM.

Family and domain databases

InterProiIPR007653. SPC22.
[Graphical view]
PANTHERiPTHR12804. PTHR12804. 1 hit.
PfamiPF04573. SPC22. 1 hit.
[Graphical view]
PIRSFiPIRSF016089. SPC22. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryo and Hippocampus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Lung and Testis.

Entry informationi

Entry nameiSPCS3_MOUSE
AccessioniPrimary (citable) accession number: Q9D365
Secondary accession number(s): B1AUR7, Q8BK31, Q9D6F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.