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Protein

Perforin-1

Gene

Prf1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei213Important for oligomerizationBy similarity1
Sitei343Important for oligomerizationBy similarity1
Metal bindingi435Calcium 1By similarity1
Metal bindingi483Calcium 1By similarity1
Metal bindingi484Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi485Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi488Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi490Calcium 2By similarity1

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: RGD
  • circadian rhythm Source: RGD
  • cytolysis Source: UniProtKB
  • defense response to tumor cell Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • immune response to tumor cell Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • response to ethanol Source: RGD
Complete GO annotation...

Keywords - Biological processi

Cytolysis

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

TCDBi1.C.39.2.1. the membrane attack complex/perforin (macpf) family.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi708463. Prf1.

Subcellular locationi

GO - Cellular componenti

  • cytolytic granule Source: UniProtKB
  • cytoplasmic vesicle Source: RGD
  • endosome lumen Source: UniProtKB-SubCell
  • extracellular space Source: RGD
  • integral component of membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20By similarityAdd BLAST20
ChainiPRO_000002361121 – 554Perforin-1Add BLAST534

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi22 ↔ 75By similarity
Disulfide bondi30 ↔ 72By similarity
Disulfide bondi101 ↔ 175By similarity
Glycosylationi204N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi241 ↔ 407By similarity
Disulfide bondi376 ↔ 392By similarity
Disulfide bondi380 ↔ 394By similarity
Disulfide bondi396 ↔ 406By similarity
Glycosylationi400N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi496 ↔ 509By similarity
Disulfide bondi524 ↔ 533By similarity
Glycosylationi548N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP35763.
PRIDEiP35763.

Expressioni

Tissue specificityi

Detected in large granular lymphocytes and lymphokine-activated killer cells.1 Publication

Interactioni

Subunit structurei

Monomer. Homooligomer. Oligomerization is required for pore formation (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000681.

Structurei

3D structure databases

ProteinModelPortaliP35763.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 374MACPFPROSITE-ProRule annotationAdd BLAST349
Domaini375 – 407EGF-likeAdd BLAST33
Domaini415 – 497C2PROSITE-ProRule annotationAdd BLAST83

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the complement C6/C7/C8/C9 family.Curated
Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 EGF-like domain.Curated
Contains 1 MACPF domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IGJ0. Eukaryota.
ENOG410XSHK. LUCA.
HOGENOMiHOG000236309.
HOVERGENiHBG008168.
InParanoidiP35763.
PhylomeDBiP35763.

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.

P35763-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAYLFLLGL FLLLPRPVPA PCYTATRSEC KQNHKFVPGV WAAGEGVDVT
60 70 80 90 100
TLRRSSSFPV NTGKFLRPDR TCTLCKNALM NDGIQRLPVA IAHWRPHGSH
110 120 130 140 150
CQRNVATTKV SSTEGVAREA AANINNDWRA GLDVNPKPEA NVHVSVAGSH
160 170 180 190 200
SKIANFAAEK AHQDQYNFNT DTVECRMYSF RLAQKPPLHP DFRKALKNLP
210 220 230 240 250
HNFNSSTEHA YRRLISSYGT HFITAVDLGG RVSVLTALRT CQLTLDGLTA
260 270 280 290 300
DEVGDCLSVE AQVSIGAQAS VSSEYKACEE KKKQHKIATS FHQTYRERHV
310 320 330 340 350
EVLGGPLDSS NDLLFGNQAT PEHFSTWIAS LPTRPDVVDY SLEPLHILLE
360 370 380 390 400
DSDPKREALR QAISHYVMSR ARWRDCNRPC RAGQHKSSRD SCQCVCQDSN
410 420 430 440 450
VTNQDCCPRQ RGLAKLMVRN FQAKGLWGDY ITSTDAYLKV FFGGQEIRTG
460 470 480 490 500
VVWNNNHPSW SDKMDFGNVL LSTGGPLRVQ VWDADNGWDD DLLGTCDKSP
510 520 530 540 550
KSGFHEVNCP LNHGSIKFIY QANCLPDLTG ETCLEYAPQG LLGDPRGNRS

GAVW
Length:554
Mass (Da):61,513
Last modified:June 1, 1994 - v1
Checksum:i7BB46B9EEDAB886F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33605 mRNA. Translation: AAA41071.1.
PIRiA45818.
UniGeneiRn.11206.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33605 mRNA. Translation: AAA41071.1.
PIRiA45818.
UniGeneiRn.11206.

3D structure databases

ProteinModelPortaliP35763.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000681.

Protein family/group databases

TCDBi1.C.39.2.1. the membrane attack complex/perforin (macpf) family.

Proteomic databases

PaxDbiP35763.
PRIDEiP35763.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi708463. Prf1.

Phylogenomic databases

eggNOGiENOG410IGJ0. Eukaryota.
ENOG410XSHK. LUCA.
HOGENOMiHOG000236309.
HOVERGENiHBG008168.
InParanoidiP35763.
PhylomeDBiP35763.

Miscellaneous databases

PROiP35763.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiPERF_RAT
AccessioniPrimary (citable) accession number: P35763
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 6, 2016
This is version 108 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. 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.