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Database: UniProt
Entry: P35763
LinkDB: P35763
Original site: P35763 
ID   PERF_RAT                Reviewed;         554 AA.
AC   P35763;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   23-MAY-2018, entry version 116.
DE   RecName: Full=Perforin-1;
DE            Short=P1;
DE   AltName: Full=Cytolysin;
DE   AltName: Full=Lymphocyte pore-forming protein;
DE   Flags: Precursor;
GN   Name=Prf1; Synonyms=Pfp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=2809217;
RA   Ishikawa H., Shinkai Y., Yagita H., Yue C.C., Henkart P.A., Sawada S.,
RA   Young H.A., Reynolds C.W., Okumura K.;
RT   "Molecular cloning of rat cytolysin.";
RL   J. Immunol. 143:3069-3073(1989).
CC   -!- FUNCTION: Plays a key role in secretory granule-dependent cell
CC       death, and in defense against virus-infected or neoplastic cells.
CC       Can insert into the membrane of target cells in its calcium-bound
CC       form, oligomerize and form large pores. Promotes cytolysis and
CC       apoptosis of target cells by facilitating the uptake of cytotoxic
CC       granzymes. {ECO:0000269|PubMed:2809217}.
CC   -!- SUBUNIT: Monomer. Homooligomer. Oligomerization is required for
CC       pore formation (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule lumen
CC       {ECO:0000269|PubMed:2809217}. Secreted
CC       {ECO:0000269|PubMed:2809217}. Cell membrane
CC       {ECO:0000269|PubMed:2809217}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:2809217}. Endosome lumen {ECO:0000250}.
CC       Note=Stored in cytoplasmic granules of cytolytic T-lymphocytes and
CC       secreted into the cleft between T-lymphocyte and target cell.
CC       Inserts into the cell membrane of target cells and forms pores.
CC       Membrane insertion and pore formation requires a major
CC       conformation change. May be taken up via endocytosis involving
CC       clathrin-coated vesicles and accumulate in a first time in large
CC       early endosomes (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in large granular lymphocytes and
CC       lymphokine-activated killer cells. {ECO:0000269|PubMed:2809217}.
CC   -!- DOMAIN: The C2 domain mediates calcium-dependent binding to lipid
CC       membranes. A subsequent conformation change leads to membrane
CC       insertion of beta-hairpin structures and pore formation. The pore
CC       is formed by transmembrane beta-strands (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC       {ECO:0000305}.
DR   EMBL; M33605; AAA41071.1; -; mRNA.
DR   PIR; A45818; A45818.
DR   UniGene; Rn.11206; -.
DR   ProteinModelPortal; P35763; -.
DR   SMR; P35763; -.
DR   STRING; 10116.ENSRNOP00000000681; -.
DR   TCDB; 1.C.39.2.1; the membrane attack complex/perforin (macpf) family.
DR   PaxDb; P35763; -.
DR   PRIDE; P35763; -.
DR   RGD; 708463; Prf1.
DR   eggNOG; ENOG410IGJ0; Eukaryota.
DR   eggNOG; ENOG410XSHK; LUCA.
DR   HOGENOM; HOG000236309; -.
DR   HOVERGEN; HBG008168; -.
DR   InParanoid; P35763; -.
DR   PhylomeDB; P35763; -.
DR   PRO; PR:P35763; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0044194; C:cytolytic granule; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR   GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0022829; F:wide pore channel activity; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IDA:RGD.
DR   GO; GO:0007623; P:circadian rhythm; IMP:RGD.
DR   GO; GO:0019835; P:cytolysis; ISS:UniProtKB.
DR   GO; GO:0002357; P:defense response to tumor cell; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0002418; P:immune response to tumor cell; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   CDD; cd04032; C2_Perforin; 1.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR020864; MACPF.
DR   InterPro; IPR020863; MACPF_CS.
DR   InterPro; IPR037300; Perforin-1_C2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00457; MACPF; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00279; MACPF_1; 1.
DR   PROSITE; PS51412; MACPF_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Complete proteome; Cytolysis; Disulfide bond;
KW   EGF-like domain; Endosome; Glycoprotein; Membrane; Metal-binding;
KW   Reference proteome; Secreted; Signal; Transmembrane;
KW   Transmembrane beta strand.
FT   SIGNAL        1     20       {ECO:0000250}.
FT   CHAIN        21    554       Perforin-1.
FT                                /FTId=PRO_0000023611.
FT   DOMAIN       26    374       MACPF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00745}.
FT   DOMAIN      375    407       EGF-like.
FT   DOMAIN      415    497       C2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00041}.
FT   METAL       435    435       Calcium 1. {ECO:0000250}.
FT   METAL       483    483       Calcium 1. {ECO:0000250}.
FT   METAL       484    484       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       485    485       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       488    488       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       490    490       Calcium 2. {ECO:0000250}.
FT   SITE        213    213       Important for oligomerization.
FT                                {ECO:0000250}.
FT   SITE        343    343       Important for oligomerization.
FT                                {ECO:0000250}.
FT   CARBOHYD    204    204       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    400    400       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    548    548       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     22     75       {ECO:0000250}.
FT   DISULFID     30     72       {ECO:0000250}.
FT   DISULFID    101    175       {ECO:0000250}.
FT   DISULFID    241    407       {ECO:0000250}.
FT   DISULFID    376    392       {ECO:0000250}.
FT   DISULFID    380    394       {ECO:0000250}.
FT   DISULFID    396    406       {ECO:0000250}.
FT   DISULFID    496    509       {ECO:0000250}.
FT   DISULFID    524    533       {ECO:0000250}.
SQ   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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