ID M7ALA0_CHEMY Unreviewed; 629 AA.
AC M7ALA0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Perforin-1 {ECO:0000313|EMBL:EMP25239.1};
GN ORFNames=UY3_17679 {ECO:0000313|EMBL:EMP25239.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP25239.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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 EMBL; KB592770; EMP25239.1; -; Genomic_DNA.
DR AlphaFoldDB; M7ALA0; -.
DR STRING; 8469.M7ALA0; -.
DR eggNOG; ENOG502RQWS; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005579; C:membrane attack complex; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
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; IPR001862; MAC_perforin.
DR InterPro; IPR020864; MACPF.
DR InterPro; IPR020863; MACPF_CS.
DR PANTHER; PTHR46096; PERFORIN-1; 1.
DR PANTHER; PTHR46096:SF3; PERFORIN-1; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF01823; MACPF; 1.
DR PRINTS; PR00764; COMPLEMENTC9.
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 Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..629
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004079378"
FT DOMAIN 27..373
FT /note="MACPF"
FT /evidence="ECO:0000259|PROSITE:PS51412"
FT DOMAIN 396..513
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 629 AA; 69791 MW; 1216F2BEF06B8F0F CRC64;
MPRPSSFFPL LLLILLPGVS THCHTGTAEE CEEHTAFVPG HNLAGEGIDV TTLGRKGAYL
VDTSHWQRPD GTCTLCRNSL LEGQLQRLPL AVADWREKVS CRRKLSSAVK ESAMGMVRAA
NAVVQNDWKV GLEVEVKPSA NTQVTLAGSH SKLAEFSTEK SQQDKYRFPR HEAACAYYAF
RVTHKPPLTR HFIRALRDLP EDYTHSSRLE YHELINTYGT HYVSQLQLGG RVRDVTAVRV
CEAALDGMTA DEVKDCLNLE ASASIGAGKG SAQAAFSQCE EQKKKKNFKR SFHETYSERH
TEVTGGHSHA DLLFSEGQDA EVFSAWMESL KASPGLVSYS LHPIHNLVRQ DNPKRKALRQ
AVSEYIAERA LWRNCTHSCP PGTQRSAHDS CSCVCPGDGS TNTMCCSRER GQGKLTVTVE
RASGLWGDYS SRTDAYVKVS FQDREVRTAT VWNTDNPVWD VHLDLGHVRV AETSQLRLQV
WDEDNRYDDD LLGTCDEPLR SGESRHQVCY LNHGRLDFRY SLGVSPYCYT GKAEVCGENM
ASVPAHNLVG EGTDSTTLEW TGAYLVDTRL CRRPNGTCSL CQNPLRGWGQ LQRVPLAVVD
WRVLQPGPQQ LGGSVSHGRG LGNNVGCEK
//
