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P10820

- PERF_MOUSE

UniProt

P10820 - PERF_MOUSE

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Protein
Perforin-1
Gene
Prf1, Pfp
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a key role in secretory granule-dependent cell death, and in defense against virus-infected or neoplastic cells. Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores. Promotes cytolysis and apoptosis of target cells by facilitating the uptake of cytotoxic granzymes.5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei213 – 2131Important for oligomerization
Sitei343 – 3431Important for oligomerization
Metal bindingi435 – 4351Calcium 1
Metal bindingi483 – 4831Calcium 1
Metal bindingi484 – 4841Calcium 1; via carbonyl oxygen
Metal bindingi485 – 4851Calcium 2; via carbonyl oxygen
Metal bindingi488 – 4881Calcium 2; via carbonyl oxygen
Metal bindingi490 – 4901Calcium 2

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. wide pore channel activity Source: UniProtKB

GO - Biological processi

  1. cytolysis Source: UniProtKB
  2. defense response to tumor cell Source: UniProtKB
  3. defense response to virus Source: UniProtKB
  4. immune response to tumor cell Source: UniProtKB
  5. protein homooligomerization Source: UniProtKB
  6. transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Biological processi

Cytolysis

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Perforin-1
Short name:
P1
Alternative name(s):
Cytolysin
Lymphocyte pore-forming protein
Gene namesi
Name:Prf1
Synonyms:Pfp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:97551. Prf1.

Subcellular locationi

Cytoplasmic granule lumen. Secreted. Cell membrane; Multi-pass membrane protein. Endosome lumen By similarity
Note: Stored in cytoplasmic granules of cytolytic T-lymphocytes and secreted into the cleft between T-lymphocyte and target cell. May be taken up via endocytosis involving clathrin-coated vesicles and accumulate in a first time in large early endosomes By similarity. Inserts into the cell membrane of target cells and forms pores. Membrane insertion and pore formation requires a major conformation change.5 Publications

GO - Cellular componenti

  1. cytolytic granule Source: UniProtKB
  2. cytoplasmic membrane-bounded vesicle Source: MGI
  3. endosome lumen Source: UniProtKB-SubCell
  4. extracellular region Source: UniProtKB-SubCell
  5. integral component of membrane Source: UniProtKB
  6. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile, but die of virus infections that are normally efficiently dealt with by the immune system. They cannot eliminate lymphocytic choriomeningitis virus, but die of the infection. Young mice are abnormally susceptible to mouse hepatitis virus. Cytolytic activity towards tumor cells and transplants is also severely reduced.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi191 – 1911D → K or V: Loss of cytotoxicity. 1 Publication
Mutagenesisi191 – 1911D → S: Strongly decreased cytotoxicity. 1 Publication
Mutagenesisi213 – 2131R → E or L: Strongly decreased cytotoxicity. 1 Publication
Mutagenesisi343 – 3431E → R: Strongly decreased cytotoxicity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20202 Publications
Add
BLAST
Chaini21 – 554534Perforin-1
PRO_0000023610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi22 ↔ 751 Publication
Disulfide bondi30 ↔ 721 Publication
Disulfide bondi101 ↔ 1751 Publication
Glycosylationi204 – 2041N-linked (GlcNAc...)1 Publication
Disulfide bondi241 ↔ 4071 Publication
Glycosylationi375 – 3751N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi376 ↔ 3921 Publication
Disulfide bondi380 ↔ 3941 Publication
Disulfide bondi396 ↔ 4061 Publication
Disulfide bondi496 ↔ 5091 Publication
Disulfide bondi524 ↔ 5331 Publication
Glycosylationi548 – 5481N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylated. The glycosylation sites are facing the interior of the pore.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP10820.
PRIDEiP10820.

Expressioni

Tissue specificityi

Detected in cytotoxic T-lymphocytes and natural killer cells.3 Publications

Gene expression databases

ArrayExpressiP10820.
BgeeiP10820.
CleanExiMM_PRF1.
GenevestigatoriP10820.

Interactioni

Subunit structurei

Monomer, as sobluble protein. Homooligomer. Oligomerization is required for pore formation.2 Publications

Protein-protein interaction databases

BioGridi202128. 1 interaction.
DIPiDIP-59218N.
IntActiP10820. 1 interaction.
MINTiMINT-4107132.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 254
Helixi27 – 315
Helixi40 – 423
Turni49 – 513
Beta strandi72 – 765
Turni78 – 825
Beta strandi84 – 874
Beta strandi91 – 966
Beta strandi106 – 1105
Helixi113 – 1219
Turni128 – 1314
Turni140 – 1434
Turni147 – 1504
Helixi152 – 16312
Beta strandi166 – 18217
Helixi190 – 1978
Helixi208 – 21811
Beta strandi220 – 23920
Helixi240 – 2456
Helixi250 – 26415
Helixi273 – 28412
Helixi291 – 2944
Beta strandi298 – 3058
Helixi307 – 3093
Beta strandi313 – 3153
Helixi321 – 33010
Turni331 – 3333
Beta strandi336 – 3449
Helixi345 – 3484
Helixi355 – 36915
Beta strandi384 – 3863
Beta strandi394 – 3974
Turni399 – 4013
Helixi404 – 4063
Beta strandi408 – 4103
Beta strandi413 – 42513
Beta strandi436 – 4427
Beta strandi445 – 4484
Beta strandi464 – 4707
Turni471 – 4733
Beta strandi477 – 4837
Beta strandi486 – 4883
Beta strandi491 – 4988
Beta strandi502 – 5109
Beta strandi512 – 52413
Beta strandi528 – 5303
Beta strandi541 – 5433

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NSJX-ray2.75A21-554[»]
ProteinModelPortaliP10820.
SMRiP10820. Positions 21-551.

Miscellaneous databases

EvolutionaryTraceiP10820.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 374349MACPF
Add
BLAST
Domaini375 – 40733EGF-like
Add
BLAST
Domaini416 – 49782C2
Add
BLAST

Domaini

The C2 domain mediates calcium-dependent binding to lipid membranes. A subsequent conformation change leads to membrane insertion of beta-hairpin structures and pore formation. The pore is formed by transmembrane beta-strands.

Sequence similaritiesi

Contains 1 C2 domain.
Contains 1 EGF-like domain.
Contains 1 MACPF domain.

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiNOG39137.
GeneTreeiENSGT00530000063725.
HOGENOMiHOG000236309.
HOVERGENiHBG008168.
InParanoidiP10820.
KOiK07818.
OMAiNYGTHFI.
OrthoDBiEOG7SJD49.
PhylomeDBiP10820.
TreeFamiTF330498.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR020864. MACPF.
IPR020863. MACPF_CS.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF01823. MACPF. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00457. MACPF. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10820-1 [UniParc]FASTAAdd to Basket

« Hide

MATCLFLLGL FLLLPRPVPA PCYTATRSEC KQKHKFVPGV WMAGEGMDVT    50
TLRRSGSFPV NTQRFLRPDR TCTLCKNSLM RDATQRLPVA ITHWRPHSSH 100
CQRNVAAAKV HSTEGVAREA AANINNDWRV GLDVNPRPEA NMRASVAGSH 150
SKVANFAAEK TYQDQYNFNS DTVECRMYSF RLVQKPPLHL DFKKALRALP 200
RNFNSSTEHA YHRLISSYGT HFITAVDLGG RISVLTALRT CQLTLNGLTA 250
DEVGDCLNVE AQVSIGAQAS VSSEYKACEE KKKQHKMATS FHQTYRERHV 300
EVLGGPLDST HDLLFGNQAT PEQFSTWTAS LPSNPGLVDY SLEPLHTLLE 350
EQNPKREALR QAISHYIMSR ARWQNCSRPC RSGQHKSSHD SCQCECQDSK 400
VTNQDCCPRQ RGLAHLVVSN FRAEHLWGDY TTATDAYLKV FFGGQEFRTG 450
VVWNNNNPRW TDKMDFENVL LSTGGPLRVQ VWDADYGWDD DLLGSCDRSP 500
HSGFHEVTCE LNHGRVKFSY HAKCLPHLTG GTCLEYAPQG LLGDPPGNRS 550
GAVW 554
Length:554
Mass (Da):62,081
Last modified:April 1, 1990 - v2
Checksum:i9E5964CE9FE8A0D8
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31T → M in CAA31251. 1 Publication
Sequence conflicti176 – 1761R → P in AAA39909. 1 Publication
Sequence conflicti229 – 2291G → A in CAA31251. 1 Publication
Sequence conflicti229 – 2291G → A in CAA42731. 1 Publication
Sequence conflicti435 – 4351D → E in AAA39909. 1 Publication
Sequence conflicti543 – 5508GDPPGNRS → EILQETAC in AAA39909. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23182 mRNA. Translation: AAA39910.1.
X51340, X51446 Genomic DNA. Translation: CAA35721.1.
X12760 mRNA. Translation: CAA31251.1.
J04148 mRNA. Translation: AAA39909.1.
X60165 mRNA. Translation: CAA42731.1.
M95527 Genomic DNA. Translation: AAB01574.1.
CCDSiCCDS23875.1.
PIRiJL0146. A31300.
RefSeqiNP_035203.3. NM_011073.3.
XP_006513433.1. XM_006513370.1.
UniGeneiMm.240313.

Genome annotation databases

EnsembliENSMUST00000035419; ENSMUSP00000041483; ENSMUSG00000037202.
GeneIDi18646.
KEGGimmu:18646.
UCSCiuc007ffv.2. mouse.

Cross-referencesi

Web resourcesi

Protein Spotlight

Our hollow architecture - Issue 126 of February 2011

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23182 mRNA. Translation: AAA39910.1 .
X51340 , X51446 Genomic DNA. Translation: CAA35721.1 .
X12760 mRNA. Translation: CAA31251.1 .
J04148 mRNA. Translation: AAA39909.1 .
X60165 mRNA. Translation: CAA42731.1 .
M95527 Genomic DNA. Translation: AAB01574.1 .
CCDSi CCDS23875.1.
PIRi JL0146. A31300.
RefSeqi NP_035203.3. NM_011073.3.
XP_006513433.1. XM_006513370.1.
UniGenei Mm.240313.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3NSJ X-ray 2.75 A 21-554 [» ]
ProteinModelPortali P10820.
SMRi P10820. Positions 21-551.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202128. 1 interaction.
DIPi DIP-59218N.
IntActi P10820. 1 interaction.
MINTi MINT-4107132.

Proteomic databases

PaxDbi P10820.
PRIDEi P10820.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035419 ; ENSMUSP00000041483 ; ENSMUSG00000037202 .
GeneIDi 18646.
KEGGi mmu:18646.
UCSCi uc007ffv.2. mouse.

Organism-specific databases

CTDi 5551.
MGIi MGI:97551. Prf1.

Phylogenomic databases

eggNOGi NOG39137.
GeneTreei ENSGT00530000063725.
HOGENOMi HOG000236309.
HOVERGENi HBG008168.
InParanoidi P10820.
KOi K07818.
OMAi NYGTHFI.
OrthoDBi EOG7SJD49.
PhylomeDBi P10820.
TreeFami TF330498.

Miscellaneous databases

EvolutionaryTracei P10820.
NextBioi 294644.
PROi P10820.
SOURCEi Search...

Gene expression databases

ArrayExpressi P10820.
Bgeei P10820.
CleanExi MM_PRF1.
Genevestigatori P10820.

Family and domain databases

Gene3Di 2.60.40.150. 1 hit.
InterProi IPR000008. C2_dom.
IPR020864. MACPF.
IPR020863. MACPF_CS.
[Graphical view ]
Pfami PF00168. C2. 1 hit.
PF01823. MACPF. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 1 hit.
SM00457. MACPF. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
PROSITEi PS50004. C2. 1 hit.
PS00279. MACPF_1. 1 hit.
PS51412. MACPF_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genomic organization of the mouse pore-forming protein (perforin) gene and localization to chromosome 10. Similarities to and differences from C9."
    Trapani J.A., Kwon B.S., Kozak C.A., Chintamaneni C., Young J.D., Dupont B.
    J. Exp. Med. 171:545-557(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Homology of perforin to the ninth component of complement (C9)."
    Shinkai Y., Takio K., Okumura K.
    Nature 334:525-527(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Cloning, analysis, and expression of murine perforin 1 cDNA, a component of cytolytic T-cell granules with homology to complement component C9."
    Lowrey D.M., Aebischer Y., Olsen K., Lichtenheld M., Rupp F., Hengartner H., Podack E.R.
    Proc. Natl. Acad. Sci. U.S.A. 86:247-251(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  5. Mueller C., Lowin B., Tschopp J.
    Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  6. "Structure and function of the murine perforin promoter and upstream region. Reciprocal gene activation or silencing in perforin positive and negative cells."
    Lichtenheld M.G., Podack E.R.
    J. Immunol. 149:2619-2626(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-117.
    Strain: BALB/c.
  7. "The primary structure of the lymphocyte pore-forming protein perforin: partial amino acid sequencing and determination of isoelectric point."
    Persechini P.M., Young J.D.-E.
    Biochem. Biophys. Res. Commun. 156:740-745(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-52; 76-96; 160-187; 255-278; 312-328; 400-420 AND 439-464.
  8. "Subcellular localization of perforin and serine esterase in lymphokine-activated killer cells and cytotoxic T cells by immunogold labeling."
    Ojcius D.M., Zheng L.M., Sphicas E.C., Zychlinsky A., Young J.D.-E.
    J. Immunol. 146:4427-4432(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Cytotoxicity mediated by T cells and natural killer cells is greatly impaired in perforin-deficient mice."
    Kagi D., Ledermann B., Burki K., Seiler P., Odermatt B., Olsen K.J., Podack E.R., Zinkernagel R.M., Hengartner H.
    Nature 369:31-37(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  10. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  11. Cited for: SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-191; ARG-213 AND GLU-343.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 21-554 OF MUTANT GLU-213 IN COMPLEX WITH CALCIUM, ELECTRON MICROSCOPY OF PORE COMPLEX, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION AT ASN-204, DISULFIDE BONDS, CALCIUM-BINDING.

Entry informationi

Entry nameiPERF_MOUSE
AccessioniPrimary (citable) accession number: P10820
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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