ID   A0A3B3W1W2_9TELE        Unreviewed;       561 AA.
AC   A0A3B3W1W2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Perforin 1.2 {ECO:0008006|Google:ProtNLM};
OS   Poecilia latipinna (sailfin molly).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000031403.1, ECO:0000313|Proteomes:UP000261500};
RN   [1] {ECO:0000313|Ensembl:ENSPLAP00000031403.1}
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3B3W1W2; -.
DR   Ensembl; ENSPLAT00000031955.1; ENSPLAP00000031403.1; ENSPLAG00000023786.1.
DR   GeneTree; ENSGT00530000063725; -.
DR   Proteomes; UP000261500; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
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   PANTHER; PTHR46096:SF5; PERFORIN 1.3-RELATED; 1.
DR   PANTHER; PTHR46096; 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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..561
FT                   /note="Perforin 1.2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017269903"
FT   DOMAIN          16..359
FT                   /note="MACPF"
FT                   /evidence="ECO:0000259|PROSITE:PS51412"
FT   DOMAIN          381..498
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
SQ   SEQUENCE   561 AA;  62517 MW;  92F959028A598CFB CRC64;
     FSVYLILYSV CVFIGSPKQC ETAHFVPGYN LGGEGYDIVT MERKGAYVID TETWDLGNGT
     CKMYRNRYQN GENQKVPVSV VDWRNLPKCS MKVSSMLYDS VESLVNDSTS SVSNDWKIGL
     EIPVDPSVTV GVGLGGSHSR ASEFGMKKSK SDRYEFVRQS VNCNFYRYRL TTSPPLSHDF
     LAAVNSLPPY CPGKASPYRD LIDTYGTHYI TQVYLGGEIK ATTSFQTCKA TMNGFTATDV
     SDCLTVEASA SFANSASVKA MTKHCEDKKK KLNSGQSFSS EFNERFTEVT GGDEMEVALF
     GGGSDPDVYK NWLNSLKTIP DIVQYNLKPL HTILPDNHRA KKGLKKEVEQ YILKNAVLKK
     CSESCQIGHR SNKRDPCACV CNSNKNVKAN CCPGGKGLAT LKVYKLYARG LYGDTFGKTD
     GSVEVKYGDQ LKRTKIISND DNPRWPEKFD FGPIVINMQN KLTFSVYDED TRWNSDLLGK
     CSFDLRKANV SDSCMFNHGT FFFSYSVECA PSLGGSRCDE YISSPMDPSL TKEFYTRNGV
     LLGNSMKKFF KPTRQAGLDQ F
//