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Protein

Signal peptide peptidase-like 3

Gene

SPPL3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane protein substrates in or close to their luminal transmembrane domain boundaries (PubMed:16873890, PubMed:25354954, PubMed:25827571). Acts like a sheddase by mediating the proteolytic release and secretion of active site-containing ectodomains of glycan-modifiying glycosidase and glycosyltransferase enzymes such as MGAT5, B4GAT1 and B4GALT1 (PubMed:25354954, PubMed:25827571). Catalyzes the intramembrane cleavage of the envelope glycoprotein gp130 and/or the leader peptide gp18LP of the simian foamy virus independent of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis (PubMed:23132852). May also have the ability to serve as a shedding protease for subsequent intramembrane proteolysis by SPPL2A and SPPL2B of the envelope glycoprotein gp130 (PubMed:23132852). Plays a role in the regulation of cellular glycosylation processes (PubMed:25354954). Required to link T-cell antigen receptor (TCR) and calcineurin-NFAT signaling cascades in lymphocytes by promoting the association of STIM1 and ORAI1 during store-operated calcium entry (SOCE) in a protease-independent manner (PubMed:25384971).5 Publications

Enzyme regulationi

Its proteolytic activity is blocked by a signal peptide peptidase (SPP) inhibitor, (ZLL)2-ketone (ZLL) or a gamma-secretase inhibitor, LY411,575 (PubMed:16873890). However, is not inhibited by ZLL and LY411,575 for activity on simian foamy virus envelope glycoprotein gp130 (PubMed:23132852).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei201 – 2011By similarity
Active sitei272 – 2721By similarity

GO - Molecular functioni

  • aspartic endopeptidase activity, intramembrane cleaving Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • membrane protein proteolysis Source: UniProtKB
  • positive regulation of calcineurin-NFAT signaling cascade Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  • positive regulation of NFAT protein import into nucleus Source: UniProtKB
  • positive regulation of protein binding Source: UniProtKB
  • positive regulation of protein dephosphorylation Source: UniProtKB
  • T cell receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Protein family/group databases

MEROPSiA22.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal peptide peptidase-like 31 PublicationImported (EC:3.4.23.-)
Short name:
SPP-like 31 Publication
Alternative name(s):
Intramembrane protease 21 Publication
Short name:
IMP-21 Publication
Presenilin homologous protein 11 Publication
Short name:
PSH11 Publication
Presenilin-like protein 41 Publication
Gene namesi
Name:SPPL31 PublicationImported
Synonyms:IMP21 Publication, PSL41 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:30424. SPPL3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88Lumenal1 Publication
Transmembranei9 – 2921HelicalSequence AnalysisAdd
BLAST
Topological domaini30 – 7546Cytoplasmic1 PublicationAdd
BLAST
Transmembranei76 – 9621HelicalSequence AnalysisAdd
BLAST
Topological domaini97 – 982LumenalSequence Analysis
Transmembranei99 – 11921HelicalSequence AnalysisAdd
BLAST
Topological domaini120 – 13718CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei138 – 16023HelicalSequence AnalysisAdd
BLAST
Topological domaini161 – 1655LumenalSequence Analysis
Transmembranei166 – 18621HelicalSequence AnalysisAdd
BLAST
Topological domaini187 – 1915CytoplasmicSequence Analysis
Transmembranei192 – 21221HelicalSequence AnalysisAdd
BLAST
Topological domaini213 – 26351Lumenal1 PublicationAdd
BLAST
Transmembranei264 – 28421HelicalSequence AnalysisAdd
BLAST
Topological domaini285 – 31228CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei313 – 33321HelicalSequence AnalysisAdd
BLAST
Topological domaini334 – 3407LumenalSequence Analysis
Transmembranei341 – 36121HelicalSequence AnalysisAdd
BLAST
Topological domaini362 – 38524Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • cytosol Source: GOC
  • endoplasmic reticulum-Golgi intermediate compartment membrane Source: UniProtKB
  • Golgi-associated vesicle membrane Source: UniProtKB
  • integral component of cytoplasmic side of endoplasmic reticulum membrane Source: UniProtKB
  • integral component of lumenal side of endoplasmic reticulum membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • rough endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi201 – 2011D → A: Does not affect complex glycosylation pattern of cellular glycoproteins; when associated with A-272. 1 Publication
Mutagenesisi272 – 2721D → A: Loss of intramembrane-cleaving activity toward the simian foamy virus envelope glycoprotein gp130. Does not affect complex glycosylation pattern of cellular glycoproteins; when associated with A-201. 2 Publications

Polymorphism and mutation databases

BioMutaiSPPL3.
DMDMi25008979.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385Signal peptide peptidase-like 3PRO_0000073912Add
BLAST

Post-translational modificationi

Not glycosylated (PubMed:15385547, PubMed:15998642).2 Publications

Proteomic databases

MaxQBiQ8TCT6.
PaxDbiQ8TCT6.
PRIDEiQ8TCT6.

Expressioni

Tissue specificityi

Widely expressed (PubMed:15385547). Expressed in the brain (PubMed:11978763).2 Publications

Gene expression databases

ExpressionAtlasiQ8TCT6. baseline and differential.
GenevisibleiQ8TCT6. HS.

Organism-specific databases

HPAiHPA059958.

Interactioni

Subunit structurei

Monomer (PubMed:15385547, PubMed:15998642, PubMed:16873890). Homodimer (PubMed:15385547, PubMed:15998642, PubMed:16873890). Interacts with STIM1 (via the transmembrane region and the SOAR/CAD domain); the interaction promotes the binding of STIM1 to ORAI1 (PubMed:25384971). Interacts with the simian foamy virus envelope glycoprotein gp130 and its processed leader peptide gp18LP; preferentially interacts with the envelope glycoprotein gp130 (PubMed:23132852).By similarity5 Publications

Protein-protein interaction databases

BioGridi125743. 5 interactions.
STRINGi9606.ENSP00000288680.

Structurei

3D structure databases

ProteinModelPortaliQ8TCT6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi342 – 3443PAL

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi375 – 3806Poly-Ser

Domaini

The first transmembrane domain may act as a type I signal anchor (PubMed:15385547). The catalytic loops is exposed toward the lumen (PubMed:15385547). The PAL motif is required for normal active site conformation. The catalytic domains embedded in the membrane are in the opposite orientation to that of the presenilin protein family (By similarity).By similarity1 Publication

Sequence similaritiesi

Belongs to the peptidase A22B family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG250196.
GeneTreeiENSGT00530000062920.
HOGENOMiHOG000243413.
HOVERGENiHBG023986.
InParanoidiQ8TCT6.
KOiK09598.
OMAiYKKQANG.
OrthoDBiEOG7NW69W.
PhylomeDBiQ8TCT6.
TreeFamiTF323842.

Family and domain databases

InterProiIPR007369. Peptidase_A22B_SPP.
IPR006639. Preselin/SPP.
[Graphical view]
PANTHERiPTHR12174. PTHR12174. 1 hit.
PfamiPF04258. Peptidase_A22B. 1 hit.
[Graphical view]
SMARTiSM00730. PSN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q8TCT6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEQTYSWAY SLVDSSQVST FLISILLIVY GSFRSLNMDF ENQDKEKDSN
60 70 80 90 100
SSSGSFNGEQ EPIIGFQPMD STRARFLPMG ACVSLLVMFF FFDSVQVVFT
110 120 130 140 150
ICTAVLATIA FAFLLLPMCQ YLTRPCSPQN KISFGCCGRF TAAELLSFSL
160 170 180 190 200
SVMLVLIWVL TGHWLLMDAL AMGLCVAMIA FVRLPSLKVS CLLLSGLLIY
210 220 230 240 250
DVFWVFFSAY IFNSNVMVKV ATQPADNPLD VLSRKLHLGP NVGRDVPRLS
260 270 280 290 300
LPGKLVFPSS TGSHFSMLGI GDIVMPGLLL CFVLRYDNYK KQASGDSCGA
310 320 330 340 350
PGPANISGRM QKVSYFHCTL IGYFVGLLTA TVASRIHRAA QPALLYLVPF
360 370 380
TLLPLLTMAY LKGDLRRMWS EPFHSKSSSS RFLEV
Length:385
Mass (Da):42,563
Last modified:June 1, 2002 - v1
Checksum:iBF829565E14A2996
GO
Isoform 2 (identifier: Q8TCT6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     59-82: EQEPIIGFQPMDSTRARFLPMGAC → NSTNNSIQTIDSTQALFLPIGAS

Show »
Length:384
Mass (Da):42,261
Checksum:i04D8C036355B32A1
GO
Isoform 3 (identifier: Q8TCT6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-216: Missing.

Show »
Length:169
Mass (Da):18,478
Checksum:i7A97E2C1713CB938
GO

Sequence cautioni

The sequence BAC11290.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401F → Y in BAC11290 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 216216Missing in isoform 3. 1 PublicationVSP_005205Add
BLAST
Alternative sequencei59 – 8224EQEPI…PMGAC → NSTNNSIQTIDSTQALFLPI GAS in isoform 2. 4 PublicationsVSP_005206Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ345030 mRNA. Translation: CAC87791.1.
AJ420898 mRNA. Translation: CAD13135.1.
AY169313 mRNA. Translation: AAO12538.1.
AB252457 mRNA. Translation: BAF30928.1.
CH471054 Genomic DNA. Translation: EAW98220.1.
BC009551 mRNA. Translation: AAH09551.1.
BC025781 mRNA. Translation: AAH25781.1.
BC073910 mRNA. Translation: AAH73910.1.
BC101625 mRNA. Translation: AAI01626.1.
BC101627 mRNA. Translation: AAI01628.1.
AK074916 mRNA. Translation: BAC11290.1. Different initiation.
CCDSiCCDS9208.1. [Q8TCT6-2]
RefSeqiNP_620584.2. NM_139015.4. [Q8TCT6-2]
UniGeneiHs.507087.
Hs.683964.

Genome annotation databases

EnsembliENST00000353487; ENSP00000288680; ENSG00000157837. [Q8TCT6-2]
GeneIDi121665.
KEGGihsa:121665.
UCSCiuc001tzc.3. human. [Q8TCT6-1]
uc001tzd.3. human. [Q8TCT6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ345030 mRNA. Translation: CAC87791.1.
AJ420898 mRNA. Translation: CAD13135.1.
AY169313 mRNA. Translation: AAO12538.1.
AB252457 mRNA. Translation: BAF30928.1.
CH471054 Genomic DNA. Translation: EAW98220.1.
BC009551 mRNA. Translation: AAH09551.1.
BC025781 mRNA. Translation: AAH25781.1.
BC073910 mRNA. Translation: AAH73910.1.
BC101625 mRNA. Translation: AAI01626.1.
BC101627 mRNA. Translation: AAI01628.1.
AK074916 mRNA. Translation: BAC11290.1. Different initiation.
CCDSiCCDS9208.1. [Q8TCT6-2]
RefSeqiNP_620584.2. NM_139015.4. [Q8TCT6-2]
UniGeneiHs.507087.
Hs.683964.

3D structure databases

ProteinModelPortaliQ8TCT6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125743. 5 interactions.
STRINGi9606.ENSP00000288680.

Protein family/group databases

MEROPSiA22.005.

Polymorphism and mutation databases

BioMutaiSPPL3.
DMDMi25008979.

Proteomic databases

MaxQBiQ8TCT6.
PaxDbiQ8TCT6.
PRIDEiQ8TCT6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353487; ENSP00000288680; ENSG00000157837. [Q8TCT6-2]
GeneIDi121665.
KEGGihsa:121665.
UCSCiuc001tzc.3. human. [Q8TCT6-1]
uc001tzd.3. human. [Q8TCT6-2]

Organism-specific databases

CTDi121665.
GeneCardsiGC12M121252.
HGNCiHGNC:30424. SPPL3.
HPAiHPA059958.
MIMi608240. gene.
neXtProtiNX_Q8TCT6.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG250196.
GeneTreeiENSGT00530000062920.
HOGENOMiHOG000243413.
HOVERGENiHBG023986.
InParanoidiQ8TCT6.
KOiK09598.
OMAiYKKQANG.
OrthoDBiEOG7NW69W.
PhylomeDBiQ8TCT6.
TreeFamiTF323842.

Miscellaneous databases

ChiTaRSiSPPL3. human.
GeneWikiiUNQ1887.
GenomeRNAii121665.
NextBioi80798.
PROiQ8TCT6.
SOURCEiSearch...

Gene expression databases

ExpressionAtlasiQ8TCT6. baseline and differential.
GenevisibleiQ8TCT6. HS.

Family and domain databases

InterProiIPR007369. Peptidase_A22B_SPP.
IPR006639. Preselin/SPP.
[Graphical view]
PANTHERiPTHR12174. PTHR12174. 1 hit.
PfamiPF04258. Peptidase_A22B. 1 hit.
[Graphical view]
SMARTiSM00730. PSN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a new protein family with homology to presenilins."
    Irmler M., Tomiuk S., Korner M.R., Hofmann K., Conradt M.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Identification of signal peptide peptidase, a presenilin-type aspartic protease."
    Weihofen A., Binns K., Lemberg M.K., Ashman K., Martoglio B.
    Science 296:2215-2218(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  3. "Novel class of polytopic proteins with domains associated with putative protease activity."
    Grigorenko A.P., Moliaka Y.K., Korovaitseva G.I., Rogaev E.I.
    Biochemistry (Mosc.) 67:826-834(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Blood.
  4. "Proteolytic processing, N-glycosylation, and proteasomal degradation of human signal peptide peptidase-like protein 3: the YD and PAL motifs, but not the GXGD motif, are critical for protein stability."
    Kondo K., Heike T., Yorifuji T., Nishikomori R., Kawai M., Ma F., Ma L., Adachi S., Nakahata T.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal brain.
  5. 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] (ISOFORMS 1; 2 AND 3).
    Tissue: Liver, Pancreas and Testis.
  7. "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] OF 12-385 (ISOFORM 2).
    Tissue: Teratocarcinoma.
  8. "Identification of a novel family of presenilin homologues."
    Ponting C.P., Hutton M., Nyborg A., Baker M., Jansen K., Golde T.E.
    Hum. Mol. Genet. 11:1037-1044(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Consensus analysis of signal peptide peptidase and homologous human aspartic proteases reveals opposite topology of catalytic domains compared with presenilins."
    Friedmann E., Lemberg M.K., Weihofen A., Dev K.K., Dengler U., Rovelli G., Martoglio B.
    J. Biol. Chem. 279:50790-50798(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, TOPOLOGY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ABSENCE OF GLYCOSYLATION.
  10. "Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3."
    Krawitz P., Haffner C., Fluhrer R., Steiner H., Schmid B., Haass C.
    J. Biol. Chem. 280:39515-39523(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, ABSENCE OF GLYCOSYLATION.
  11. "Intramembrane proteolytic cleavage by human signal peptide peptidase like 3 and malaria signal peptide peptidase."
    Nyborg A.C., Ladd T.B., Jansen K., Kukar T., Golde T.E.
    FASEB J. 20:1671-1679(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBUNIT.
  12. "SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production."
    Friedmann E., Hauben E., Maylandt K., Schleeger S., Vreugde S., Lichtenthaler S.F., Kuhn P.H., Stauffer D., Rovelli G., Martoglio B.
    Nat. Cell Biol. 8:843-848(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. Cited for: FUNCTION, ABSENCE OF ENZYME REGULATION, INTERACTION WITH ENV, MUTAGENESIS OF ASP-272.
  14. "Shedding of glycan-modifying enzymes by signal peptide peptidase-like 3 (SPPL3) regulates cellular N-glycosylation."
    Voss M., Kunzel U., Higel F., Kuhn P.H., Colombo A., Fukumori A., Haug-Kroper M., Klier B., Grammer G., Seidl A., Schroder B., Obst R., Steiner H., Lichtenthaler S.F., Haass C., Fluhrer R.
    EMBO J. 33:2890-2905(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-201 AND ASP-272.
  15. "A protease-independent function for SPPL3 in NFAT activation."
    Makowski S.L., Wang Z., Pomerantz J.L.
    Mol. Cell. Biol. 35:451-467(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH STIM1.
  16. "Secretome analysis identifies novel signal peptide peptidase-like 3 (SPPL3) substrates and reveals a role of SPPL3 in multiple Golgi glycosylation pathways."
    Kuhn P.H., Voss M., Haug-Kroper M., Schroder B., Schepers U., Brase S., Haass C., Lichtenthaler S.F., Fluhrer R.
    Mol. Cell. Proteomics 0:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiSPPL3_HUMAN
AccessioniPrimary (citable) accession number: Q8TCT6
Secondary accession number(s): Q3MJ04, Q8TAU4, Q96DD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: June 1, 2002
Last modified: July 22, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.