ID A0A3B4CR35_PYGNA Unreviewed; 557 AA.
AC A0A3B4CR35;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Perforin-1-like {ECO:0000313|Ensembl:ENSPNAP00000013818.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000013818.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000013818.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC {ECO:0000256|ARBA:ARBA00009214}.
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DR AlphaFoldDB; A0A3B4CR35; -.
DR STRING; 42514.ENSPNAP00000013818; -.
DR Ensembl; ENSPNAT00000021530.1; ENSPNAP00000013818.1; ENSPNAG00000019701.1.
DR GeneTree; ENSGT00940000164067; -.
DR OMA; PCICSCH; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0140911; F:pore-forming activity; IEA:InterPro.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0001909; P:leukocyte mediated cytotoxicity; IEA:InterPro.
DR CDD; cd04032; C2_Perforin; 1.
DR Gene3D; 2.60.40.150; C2 domain; 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 PANTHER; PTHR46096; PERFORIN-1; 1.
DR PANTHER; PTHR46096:SF3; PERFORIN-1; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF01823; MACPF; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00457; MACPF; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00279; MACPF_1; 1.
DR PROSITE; PS51412; MACPF_2; 1.
PE 3: Inferred from homology;
KW Cytolysis {ECO:0000256|ARBA:ARBA00022852};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..557
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017288455"
FT DOMAIN 27..371
FT /note="MACPF"
FT /evidence="ECO:0000259|PROSITE:PS51412"
FT DOMAIN 393..512
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 557 AA; 62391 MW; 7585DA6A8004D8F4 CRC64;
MLQAITLRVM LAASFPLLTI PACFKGTSAQ CQDAEFAPGS DLAGEGFDIT TMQRKGAFVI
DMSVWMLKNE TCTLCRNPYM EGKKQKLPLS VVNWRPSKKC TMKLSSSVYQ SSESLLSSST
SAIDNNWKVN LGIIDIRGKG SLMLAGTNSK LAQYSMEKTK KDKFSFTSHA VSCGYYSYRV
SSRPAVHPEL TYEIDRLPEK YDNKTKYSYY KLIDKFGTHY ITKVTLGGAV HSVTSIRQCH
AALQGLSMDE VKTCLDVEAS ASMMGKMSVT TEYHHCQKVE DKTLNKKSFS SSFSDRVTDI
IGGHTENAEL LFSSDKDPAA YKDWLSSLPQ HPEIISYSLN ALHELLPEKK PTHEYLRNAI
KDYILQRGLV KNCSKPCNAG IKTNPKEPCI CSCHNNAGVN NDCCPARRGL AKVTVIAVRA
SGLWGDYFTQ TDGYVKVLRN GKIVVGETPV IWNRNSPTWN WKFDLDINDL TQFTSVKLET
WDRDNKWDDD LLGACQVQLK AGLQDNFCHL NHGLLYYKVQ CKLLSNRSVA TELIVTHSLP
MPVSIFHISD SSDKLYR
//
