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Q8IUH8

- SPP2C_HUMAN

UniProt

Q8IUH8 - SPP2C_HUMAN

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Protein

Signal peptide peptidase-like 2C

Gene

SPPL2C

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

Functioni

Intramembrane-cleaving aspartic protease (I-CLiP) that may be able to cleave type II membrane signal peptides in the hydrophobic plane of the membrane.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei386 – 3861By similarity
Active sitei448 – 4481By similarity

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: InterPro
  2. protein homodimerization activity Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Protein family/group databases

MEROPSiA22.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal peptide peptidase-like 2C (EC:3.4.23.-)
Short name:
SPP-like 2C
Short name:
SPPL2c
Alternative name(s):
Intramembrane protease 5
Short name:
IMP-5
Gene namesi
Name:SPPL2C
Synonyms:IMP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:28902. SPPL2C.

Subcellular locationi

Membrane 1 Publication; Multi-pass membrane protein 1 Publication. Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB
  2. integral component of cytoplasmic side of endoplasmic reticulum membrane Source: UniProtKB
  3. integral component of lumenal side of endoplasmic reticulum membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 684663Signal peptide peptidase-like 2CPRO_0000314797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi100 – 1001N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ8IUH8.
PRIDEiQ8IUH8.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ8IUH8.
GenevestigatoriQ8IUH8.

Organism-specific databases

HPAiHPA024444.

Structurei

3D structure databases

ProteinModelPortaliQ8IUH8.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 186165LumenalSequence AnalysisAdd
BLAST
Topological domaini208 – 25346CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini275 – 2762LumenalSequence Analysis
Topological domaini298 – 31922CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini341 – 3466LumenalSequence Analysis
Topological domaini366 – 37611CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini398 – 43942LumenalSequence AnalysisAdd
BLAST
Topological domaini461 – 47212CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini494 – 4952LumenalSequence Analysis
Topological domaini517 – 684168CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei187 – 20721HelicalSequence AnalysisAdd
BLAST
Transmembranei254 – 27421HelicalSequence AnalysisAdd
BLAST
Transmembranei277 – 29721HelicalSequence AnalysisAdd
BLAST
Transmembranei320 – 34021HelicalSequence AnalysisAdd
BLAST
Transmembranei347 – 36519HelicalSequence AnalysisAdd
BLAST
Transmembranei377 – 39721HelicalSequence AnalysisAdd
BLAST
Transmembranei440 – 46021HelicalSequence AnalysisAdd
BLAST
Transmembranei473 – 49321HelicalSequence AnalysisAdd
BLAST
Transmembranei496 – 51621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini83 – 16381PAAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi499 – 5013PAL

Domaini

The PAL motif is required for normal active site conformation By similarity. 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

eggNOGiNOG268366.
GeneTreeiENSGT00530000062920.
HOGENOMiHOG000231496.
HOVERGENiHBG024193.
InParanoidiQ8IUH8.
KOiK14212.
OMAiILWVAYR.
OrthoDBiEOG769ZJ4.
PhylomeDBiQ8IUH8.
TreeFamiTF319186.

Family and domain databases

InterProiIPR007369. Peptidase_A22B_SPP.
IPR006639. Preselin/SPP.
IPR003137. Protease-assoc_domain.
[Graphical view]
PANTHERiPTHR12174. PTHR12174. 1 hit.
PfamiPF02225. PA. 1 hit.
PF04258. Peptidase_A22B. 1 hit.
[Graphical view]
SMARTiSM00730. PSN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8IUH8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MACLGFLLPV GFLLLISTVA GGKYGVAHVV SENWSKDYCI LFSSDYITLP
60 70 80 90 100
RDLHHAPLLP LYDGTKAPWC PGEDSPHQAQ LRSPSQRPLR QTTAMVMRGN
110 120 130 140 150
CSFHTKGWLA QGQGAHGLLI VSRVSDQQCS DTTLAPQDPR QPLADLTIPV
160 170 180 190 200
AMLHYADMLD ILSHTRGEAV VRVAMYAPPE PIIDYNMLVI FILAVGTVAA
210 220 230 240 250
GGYWAGLTEA NRLQRRRARR GGGSGGHHQL QEAAAAEGAQ KEDNEDIPVD
260 270 280 290 300
FTPAMTGVVV TLSCSLMLLL YFFYDHFVYV TIGIFGLGAG IGLYSCLSPL
310 320 330 340 350
VCRLSLRQYQ RPPHSLWASL PLPLLLLASL CATVIIFWVA YRNEDRWAWL
360 370 380 390 400
LQDTLGISYC LFVLHRVRLP TLKNCSSFLL ALLAFDVFFV FVTPFFTKTG
410 420 430 440 450
ESIMAQVALG PAESSSHERL PMVLKVPRLR VSALTLCSQP FSILGFGDIV
460 470 480 490 500
VPGFLVAYCC RFDVQVCSRQ IYFVACTVAY AVGLLVTFMA MVLMQMGQPA
510 520 530 540 550
LLYLVSSTLL TSLAVAACRQ ELSLFWTGQG RAKMCGLGCA PSAGSRQKQE
560 570 580 590 600
GAADAHTAST LERGTSRGAG DLDSNPGEDT TEIVTISENE ATNPEDRSDS
610 620 630 640 650
SEGWSDAHLD PNELPFIPPG ASEELMPLMP MAMLIPLMPL MPPPSELGHV
660 670 680
HAQAQAHETG LPWAGLHKRK GLKVRKSMST QAPL
Length:684
Mass (Da):74,503
Last modified:November 24, 2009 - v3
Checksum:i578DA60509765667
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti123 – 1231R → Q.
Corresponds to variant rs17763658 [ dbSNP | Ensembl ].
VAR_038048
Natural varianti303 – 3031R → H.2 Publications
Corresponds to variant rs242944 [ dbSNP | Ensembl ].
VAR_038049
Natural varianti461 – 4611R → P.
Corresponds to variant rs12185233 [ dbSNP | Ensembl ].
VAR_038050
Natural varianti471 – 4711I → V.
Corresponds to variant rs12185268 [ dbSNP | Ensembl ].
VAR_038051
Natural varianti601 – 6011S → P.
Corresponds to variant rs12373123 [ dbSNP | Ensembl ].
VAR_038052
Natural varianti620 – 6201G → R.
Corresponds to variant rs12373139 [ dbSNP | Ensembl ].
VAR_038053
Natural varianti626 – 6261M → V.1 Publication
VAR_060590
Natural varianti643 – 6431P → R.
Corresponds to variant rs12373142 [ dbSNP | Ensembl ].
VAR_038054
Natural varianti659 – 6591T → I.
Corresponds to variant rs16940694 [ dbSNP | Ensembl ].
VAR_057147

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY169316 Genomic DNA. Translation: AAO12541.1.
AC003662 Genomic DNA. No translation available.
AC217770 Genomic DNA. No translation available.
AC217771 Genomic DNA. No translation available.
BC022041 mRNA. Translation: AAH22041.2.
BC025401 mRNA. Translation: AAH25401.1.
CCDSiCCDS32673.1.
RefSeqiNP_787078.2. NM_175882.2.
UniGeneiHs.144491.

Genome annotation databases

EnsembliENST00000329196; ENSP00000332488; ENSG00000185294.
GeneIDi162540.
KEGGihsa:162540.
UCSCiuc010wka.2. human.

Polymorphism databases

DMDMi269849676.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY169316 Genomic DNA. Translation: AAO12541.1 .
AC003662 Genomic DNA. No translation available.
AC217770 Genomic DNA. No translation available.
AC217771 Genomic DNA. No translation available.
BC022041 mRNA. Translation: AAH22041.2 .
BC025401 mRNA. Translation: AAH25401.1 .
CCDSi CCDS32673.1.
RefSeqi NP_787078.2. NM_175882.2.
UniGenei Hs.144491.

3D structure databases

ProteinModelPortali Q8IUH8.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi A22.006.

Polymorphism databases

DMDMi 269849676.

Proteomic databases

PaxDbi Q8IUH8.
PRIDEi Q8IUH8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000329196 ; ENSP00000332488 ; ENSG00000185294 .
GeneIDi 162540.
KEGGi hsa:162540.
UCSCi uc010wka.2. human.

Organism-specific databases

CTDi 162540.
GeneCardsi GC17P043923.
H-InvDB HIX0013905.
HGNCi HGNC:28902. SPPL2C.
HPAi HPA024444.
MIMi 608284. gene.
neXtProti NX_Q8IUH8.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG268366.
GeneTreei ENSGT00530000062920.
HOGENOMi HOG000231496.
HOVERGENi HBG024193.
InParanoidi Q8IUH8.
KOi K14212.
OMAi ILWVAYR.
OrthoDBi EOG769ZJ4.
PhylomeDBi Q8IUH8.
TreeFami TF319186.

Miscellaneous databases

GenomeRNAii 162540.
NextBioi 88197.
PROi Q8IUH8.
SOURCEi Search...

Gene expression databases

Bgeei Q8IUH8.
Genevestigatori Q8IUH8.

Family and domain databases

InterProi IPR007369. Peptidase_A22B_SPP.
IPR006639. Preselin/SPP.
IPR003137. Protease-assoc_domain.
[Graphical view ]
PANTHERi PTHR12174. PTHR12174. 1 hit.
Pfami PF02225. PA. 1 hit.
PF04258. Peptidase_A22B. 1 hit.
[Graphical view ]
SMARTi SM00730. PSN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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 [GENOMIC DNA], VARIANT HIS-303.
  2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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], VARIANTS HIS-303 AND VAL-626.
    Tissue: Testis.
  4. "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: GLYCOSYLATION, TOPOLOGY, TISSUE SPECIFICITY.
  5. "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.

Entry informationi

Entry nameiSPP2C_HUMAN
AccessioniPrimary (citable) accession number: Q8IUH8
Secondary accession number(s): Q8TC67, Q8WVZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 24, 2009
Last modified: October 29, 2014
This is version 78 of the entry and version 3 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3