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Protein

Signal peptide peptidase-like 2B

Gene

Sppl2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in ITM2B and TNF processing. Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus. May play a role in the regulation of innate and adaptive immunity.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei352By similarity1
Active sitei414By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease

Enzyme and pathway databases

ReactomeiR-RNO-5357905 Regulation of TNFR1 signaling

Names & Taxonomyi

Protein namesi
Recommended name:
Signal peptide peptidase-like 2BBy similarity (EC:3.4.23.-)
Short name:
SPP-like 2BBy similarity
Short name:
SPPL2bBy similarity
Gene namesi
Name:Sppl2bBy similarityImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi1308556 Sppl2b

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 168LumenalBy similarityAdd BLAST149
Transmembranei169 – 189HelicalSequence analysisAdd BLAST21
Topological domaini190 – 216CytoplasmicSequence analysisAdd BLAST27
Transmembranei217 – 237HelicalSequence analysisAdd BLAST21
Topological domaini238 – 239LumenalSequence analysis2
Transmembranei240 – 260HelicalSequence analysisAdd BLAST21
Topological domaini261 – 286CytoplasmicSequence analysisAdd BLAST26
Transmembranei287 – 307HelicalSequence analysisAdd BLAST21
Topological domaini308 – 312LumenalSequence analysis5
Transmembranei313 – 333HelicalSequence analysisAdd BLAST21
Topological domaini334 – 341CytoplasmicSequence analysis8
Transmembranei342 – 362HelicalSequence analysisAdd BLAST21
Topological domaini363 – 405LumenalBy similarityAdd BLAST43
Transmembranei406 – 426HelicalSequence analysisAdd BLAST21
Topological domaini427 – 438CytoplasmicSequence analysisAdd BLAST12
Transmembranei439 – 459HelicalSequence analysisAdd BLAST21
Topological domaini460 – 463LumenalSequence analysis4
Transmembranei464 – 484HelicalSequence analysisAdd BLAST21
Topological domaini485 – 577CytoplasmicBy similarityAdd BLAST93

Keywords - Cellular componenti

Cell membrane, Endosome, Golgi apparatus, Lysosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000023607720 – 577Signal peptide peptidase-like 2BAdd BLAST558

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi91N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ5PQL3
PRIDEiQ5PQL3

PTM databases

PhosphoSitePlusiQ5PQL3

Expressioni

Gene expression databases

BgeeiENSRNOG00000057881 Expressed in 10 organ(s), highest expression level in testis
GenevisibleiQ5PQL3 RN

Interactioni

Subunit structurei

Monomer. Homodimer. Interacts with ITM2B and TNF.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000050649

Structurei

3D structure databases

ProteinModelPortaliQ5PQL3
SMRiQ5PQL3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini49 – 149PAAdd BLAST101

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi465 – 467PAL3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi343 – 348Poly-Leu6

Domaini

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; therefore, it is predicted to cleave type II-oriented substrate peptides like the prototypic protease SPP.By similarity

Sequence similaritiesi

Belongs to the peptidase A22B family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2442 Eukaryota
ENOG410ZP52 LUCA
GeneTreeiENSGT00530000062920
HOGENOMiHOG000231496
HOVERGENiHBG024193
InParanoidiQ5PQL3
KOiK09597
OMAiFSNQIPL
OrthoDBiEOG091G05NG
PhylomeDBiQ5PQL3
TreeFamiTF319186

Family and domain databases

InterProiView protein in InterPro
IPR003137 PA_domain
IPR007369 Peptidase_A22B_SPP
IPR006639 Preselin/SPP
IPR033149 SPPL2B
PANTHERiPTHR12174 PTHR12174, 1 hit
PTHR12174:SF39 PTHR12174:SF39, 1 hit
PfamiView protein in Pfam
PF02225 PA, 1 hit
PF04258 Peptidase_A22B, 1 hit
SMARTiView protein in SMART
SM00730 PSN, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5PQL3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAAARLAASL LLLAAQVACE FGVLRVVPQS GGTRGRDYCI LYNPQWAHLP
60 70 80 90 100
HDLNKVSLLK LRDLSTTQLC SHLDVPVEDF TNQIALVARG NCTFYEKVRL
110 120 130 140 150
AQGSGAHGLL IVSKERLVPP RGNKTQYEEI SIPVALLSHR DLQDIFRRFG
160 170 180 190 200
HEVMVALYAP SEPVMDYNMV IIFIMAVGTV ALGGYWAGSH DVKKYMKHKR
210 220 230 240 250
DDVPEKQEDE AVDVTPVMIC VFVVMCCFML VLLYYFYDRL VYVIIGIFCL
260 270 280 290 300
ASSTGLYSCL APCVRKLPFC TCRVPDNNLP YFHKRPQARM LLLALFCVTV
310 320 330 340 350
SVVWGVFRNE DQWAWVLQDT LGIAFCLYML RTIRLPTFKA CTLLLLVLFV
360 370 380 390 400
YDIFFVFITP YLTKSGNSIM VEVATGPSNS STHEKLPMVL KVPRLNTSPL
410 420 430 440 450
SLCDRPFSLL GFGDILVPGL LVAYCHRFDI QVQSSRIYFV ACTIAYGLGL
460 470 480 490 500
LVTFVALVLM RHGQPALLYL VPCTLLTSCT VALWRREMGA FWTGSGFADA
510 520 530 540 550
PQTPWAAPQG PVPPKDVDAS LSEQPRGEEL AQSPLATEEA GATDPAKDPD
560 570
SPVAGPLSPS NGDQVQPIPV VTPGTSA
Length:577
Mass (Da):63,737
Last modified:January 4, 2005 - v1
Checksum:i3247629232E44CE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC087132 mRNA Translation: AAH87132.1
RefSeqiNP_001014222.1, NM_001014200.1
UniGeneiRn.18529

Genome annotation databases

EnsembliENSRNOT00000084144; ENSRNOP00000074120; ENSRNOG00000057881
GeneIDi362828
KEGGirno:362828
UCSCiRGD:1308556 rat

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC087132 mRNA Translation: AAH87132.1
RefSeqiNP_001014222.1, NM_001014200.1
UniGeneiRn.18529

3D structure databases

ProteinModelPortaliQ5PQL3
SMRiQ5PQL3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000050649

PTM databases

PhosphoSitePlusiQ5PQL3

Proteomic databases

PaxDbiQ5PQL3
PRIDEiQ5PQL3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000084144; ENSRNOP00000074120; ENSRNOG00000057881
GeneIDi362828
KEGGirno:362828
UCSCiRGD:1308556 rat

Organism-specific databases

CTDi56928
RGDi1308556 Sppl2b

Phylogenomic databases

eggNOGiKOG2442 Eukaryota
ENOG410ZP52 LUCA
GeneTreeiENSGT00530000062920
HOGENOMiHOG000231496
HOVERGENiHBG024193
InParanoidiQ5PQL3
KOiK09597
OMAiFSNQIPL
OrthoDBiEOG091G05NG
PhylomeDBiQ5PQL3
TreeFamiTF319186

Enzyme and pathway databases

ReactomeiR-RNO-5357905 Regulation of TNFR1 signaling

Miscellaneous databases

PROiPR:Q5PQL3

Gene expression databases

BgeeiENSRNOG00000057881 Expressed in 10 organ(s), highest expression level in testis
GenevisibleiQ5PQL3 RN

Family and domain databases

InterProiView protein in InterPro
IPR003137 PA_domain
IPR007369 Peptidase_A22B_SPP
IPR006639 Preselin/SPP
IPR033149 SPPL2B
PANTHERiPTHR12174 PTHR12174, 1 hit
PTHR12174:SF39 PTHR12174:SF39, 1 hit
PfamiView protein in Pfam
PF02225 PA, 1 hit
PF04258 Peptidase_A22B, 1 hit
SMARTiView protein in SMART
SM00730 PSN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSPP2B_RAT
AccessioniPrimary (citable) accession number: Q5PQL3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 4, 2005
Last modified: September 12, 2018
This is version 94 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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