ID A0A3P9PQI9_POERE Unreviewed; 1651 AA.
AC A0A3P9PQI9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Pappalysin 1 {ECO:0000313|Ensembl:ENSPREP00000024059.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000024059.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000024059.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000024059.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase M43B family.
CC {ECO:0000256|ARBA:ARBA00008721}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR RefSeq; XP_008422601.1; XM_008424379.2.
DR STRING; 8081.ENSPREP00000024059; -.
DR Ensembl; ENSPRET00000024305.1; ENSPREP00000024059.1; ENSPREG00000016205.1.
DR GeneID; 103473832; -.
DR KEGG; pret:103473832; -.
DR CTD; 101448000; -.
DR GeneTree; ENSGT00940000156654; -.
DR OMA; KQVVCEP; -.
DR OrthoDB; 5483399at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000016205; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR CDD; cd00033; CCP; 3.
DR CDD; cd04275; ZnMc_pappalysin_like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR011936; Myxo_disulph_rpt.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR043543; PAPPA/PAPPA2.
DR InterPro; IPR008754; Peptidase_M43.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR NCBIfam; TIGR02232; myxo_disulf_rpt; 1.
DR PANTHER; PTHR46130; LAMGL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46130:SF2; PAPPALYSIN-1; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF05572; Peptidase_M43; 1.
DR Pfam; PF00084; Sushi; 1.
DR SMART; SM00032; CCP; 4.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00004; NL; 2.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50923; SUSHI; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1651
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017975230"
FT DOMAIN 1220..1291
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1353..1418
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 65..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1651 AA; 184983 MW; ED5518477033B7CC CRC64;
MKLWTSPWVS CLVILILCFG SECGTVRRKG RSKRELVRIR EARATIPGAC ATRLPRGKRS
LPGLERRVLR QRRRSSHAEE DSPERGKAVY FTGRGDQLRL KPGVEIPRGN FTLEMWIKPE
GGQRSPTVIA GLYDKCFYAS SDRGWLLGIQ AVSEHGNRDP RFFFSLKTDR AHKVTSIHAN
VRYVPKQWAY VAITYDGVYM RLFVNGAQVG VSREQSGDVF SHMTKKCKVL MIGGNALNHN
YRGAVEKVGL WRQARGQRDI IRDMQGHEHP RDLPHLVIHE NFEHPGRKWL TVKDGNFPQP
EKQGLGQKEY LGTDGMGNTE GLLDTTLEPP ACGQTVCDNV DVIKNYNQLW TFRQRKVVQY
RVVNIWDDER KRPTVSDNQI ILQHQKLNDA FNPYNISWNL SIHNVTSSSL RDRLILANCD
IGKIGNDECD PECNHPLTGF DAGDCLFGHP SNCPNHKLGN GVCDAECNCD TYFYDNADCC
NPNVTDVTKT CIDSSSPHKA FLDMKEVKEI LRLDGSTHLN VFFANSSDED LAGVATWPWD
KEALTHLGGI VLNPSFYGTF GHTDTMVHEI GHSLGLYHVF RGVSEIDSCN DACLETEPSM
ETGDLCADTN PTPKCKECND PEPGNETCGH QHFMHTPFNN YMSYTDDACT NSFTLNQVAR
MHCYLDLVYQ KWQTSFKSPP VVMAPHVVEQ HHNSVTLEWF PPISGHFYDR EVGLACDKCT
EGRVLLQYAS NSSSPRPCDP SGHWSPREAE GPPDVEQACE PSVRTWSPNA GTDQGVVGLS
ECPPQGCMLQ LEFQHPVVPD SLTVWVTFFS PEESALPAIH DILLLTVSGN NISLGPSNVF
CDTPLTLKLD VEEAVYGVQF YTMEQHLEID ATLLTSKPDC KVCRHCKPLH YNLLRQPPFT
FAPKGLQLIE PIRRYTDRDV VLHVPYTYQI QTVSHVGMSE PSPPLVHELG GPYCGDGRIQ
SFKGEECDDM NSVNGDGCSS QCKEEPFFNC VEEPSMCYYY DGDGVCEDFE RETGVRDCGL
YTPSGFLDQW ASHVNVSHEE KPYCSGDVAA GYPAATKTCL SKVFDLSDGV SQYAWFPCQE
AYRQRSEYST YWLKANFSHP MVAAAVIVHL AADGTKFIDQ TQCNITVQLV DTKDGFHSLG
EWRLSCRTNP LVIPVSHDLS VAFYHTKAIL VMFSCQLVAI SGIGLRSFQS FDPITISGCQ
SNEIYNPTGQ SCVHYSCEAI DCQEPLIRNA ELKCSSPGRH FYNGDRCTIS CNSGYVLQVH
QEDDIIKTQS DSSVTITCTN GKWNKQVSCE PVDCGLPDKY HVHPAHFTFS EGTTYGKKST
FLCREPAQLI GTNNTLICQE DGLWSFPEAL CELRCPAPPP VPNAVLQTKR CNETGLKVGT
LCKYKCKPGY HVTNKPKRRA FKRQCTEDGT WLEGACEPVT CDPPPPIFHG SYYCTDGFRF
DSICRLNCSE STGNRQGVSV HTVRLLHSSC KQGTASNMIR CRKDGNWTGS FRLCPNSKGQ
CSLPQNLHYS LQYSCKRGHG IGEECELSCR EGNSEVVILP SNVTANFLLR QHWWNPQKVK
SIVCTMGLKW YPPPEFLHCI KGCEPFMGDN YCDPVNNRAF CNYDGGDCCQ TTVKTKKVIP
FPISCDIRNE CSCRDPKAAE NRKHERNHSL G
//
