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Perforin-1 (P1) (Cytolysin) (Lymphocyte pore-forming protein)

 PERF_RAT                Reviewed;         554 AA.
P35763;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
23-MAY-2018, entry version 116.
RecName: Full=Perforin-1;
Short=P1;
AltName: Full=Cytolysin;
AltName: Full=Lymphocyte pore-forming protein;
Flags: Precursor;
Name=Prf1; Synonyms=Pfp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=2809217;
Ishikawa H., Shinkai Y., Yagita H., Yue C.C., Henkart P.A., Sawada S.,
Young H.A., Reynolds C.W., Okumura K.;
"Molecular cloning of rat cytolysin.";
J. Immunol. 143:3069-3073(1989).
-!- FUNCTION: 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. {ECO:0000269|PubMed:2809217}.
-!- SUBUNIT: Monomer. Homooligomer. Oligomerization is required for
pore formation (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasmic granule lumen
{ECO:0000269|PubMed:2809217}. Secreted
{ECO:0000269|PubMed:2809217}. Cell membrane
{ECO:0000269|PubMed:2809217}; Multi-pass membrane protein
{ECO:0000269|PubMed:2809217}. Endosome lumen {ECO:0000250}.
Note=Stored in cytoplasmic granules of cytolytic T-lymphocytes and
secreted into the cleft between T-lymphocyte and target cell.
Inserts into the cell membrane of target cells and forms pores.
Membrane insertion and pore formation requires a major
conformation change. May be taken up via endocytosis involving
clathrin-coated vesicles and accumulate in a first time in large
early endosomes (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in large granular lymphocytes and
lymphokine-activated killer cells. {ECO:0000269|PubMed:2809217}.
-!- DOMAIN: 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).
{ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
{ECO:0000305}.
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EMBL; M33605; AAA41071.1; -; mRNA.
PIR; A45818; A45818.
UniGene; Rn.11206; -.
ProteinModelPortal; P35763; -.
SMR; P35763; -.
STRING; 10116.ENSRNOP00000000681; -.
TCDB; 1.C.39.2.1; the membrane attack complex/perforin (macpf) family.
PaxDb; P35763; -.
PRIDE; P35763; -.
RGD; 708463; Prf1.
eggNOG; ENOG410IGJ0; Eukaryota.
eggNOG; ENOG410XSHK; LUCA.
HOGENOM; HOG000236309; -.
HOVERGEN; HBG008168; -.
InParanoid; P35763; -.
PhylomeDB; P35763; -.
PRO; PR:P35763; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0044194; C:cytolytic granule; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0022829; F:wide pore channel activity; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IDA:RGD.
GO; GO:0007623; P:circadian rhythm; IMP:RGD.
GO; GO:0019835; P:cytolysis; ISS:UniProtKB.
GO; GO:0002357; P:defense response to tumor cell; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0002418; P:immune response to tumor cell; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
CDD; cd04032; C2_Perforin; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR020864; MACPF.
InterPro; IPR020863; MACPF_CS.
InterPro; IPR037300; Perforin-1_C2.
Pfam; PF00168; C2; 1.
Pfam; PF01823; MACPF; 1.
SMART; SM00239; C2; 1.
SMART; SM00457; MACPF; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS00279; MACPF_1; 1.
PROSITE; PS51412; MACPF_2; 1.
2: Evidence at transcript level;
Calcium; Cell membrane; Complete proteome; Cytolysis; Disulfide bond;
EGF-like domain; Endosome; Glycoprotein; Membrane; Metal-binding;
Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane beta strand.
SIGNAL 1 20 {ECO:0000250}.
CHAIN 21 554 Perforin-1.
/FTId=PRO_0000023611.
DOMAIN 26 374 MACPF. {ECO:0000255|PROSITE-
ProRule:PRU00745}.
DOMAIN 375 407 EGF-like.
DOMAIN 415 497 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
METAL 435 435 Calcium 1. {ECO:0000250}.
METAL 483 483 Calcium 1. {ECO:0000250}.
METAL 484 484 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 485 485 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 488 488 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 490 490 Calcium 2. {ECO:0000250}.
SITE 213 213 Important for oligomerization.
{ECO:0000250}.
SITE 343 343 Important for oligomerization.
{ECO:0000250}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 548 548 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 22 75 {ECO:0000250}.
DISULFID 30 72 {ECO:0000250}.
DISULFID 101 175 {ECO:0000250}.
DISULFID 241 407 {ECO:0000250}.
DISULFID 376 392 {ECO:0000250}.
DISULFID 380 394 {ECO:0000250}.
DISULFID 396 406 {ECO:0000250}.
DISULFID 496 509 {ECO:0000250}.
DISULFID 524 533 {ECO:0000250}.
SEQUENCE 554 AA; 61513 MW; 7BB46B9EEDAB886F CRC64;
MAAYLFLLGL FLLLPRPVPA PCYTATRSEC KQNHKFVPGV WAAGEGVDVT TLRRSSSFPV
NTGKFLRPDR TCTLCKNALM NDGIQRLPVA IAHWRPHGSH CQRNVATTKV SSTEGVAREA
AANINNDWRA GLDVNPKPEA NVHVSVAGSH SKIANFAAEK AHQDQYNFNT DTVECRMYSF
RLAQKPPLHP DFRKALKNLP HNFNSSTEHA YRRLISSYGT HFITAVDLGG RVSVLTALRT
CQLTLDGLTA DEVGDCLSVE AQVSIGAQAS VSSEYKACEE KKKQHKIATS FHQTYRERHV
EVLGGPLDSS NDLLFGNQAT PEHFSTWIAS LPTRPDVVDY SLEPLHILLE DSDPKREALR
QAISHYVMSR ARWRDCNRPC RAGQHKSSRD SCQCVCQDSN VTNQDCCPRQ RGLAKLMVRN
FQAKGLWGDY ITSTDAYLKV FFGGQEIRTG VVWNNNHPSW SDKMDFGNVL LSTGGPLRVQ
VWDADNGWDD DLLGTCDKSP KSGFHEVNCP LNHGSIKFIY QANCLPDLTG ETCLEYAPQG
LLGDPRGNRS GAVW


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