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Database: UniProt
Entry: A0A3B4X4K3_SERLL
LinkDB: A0A3B4X4K3_SERLL
Original site: A0A3B4X4K3_SERLL 
ID   A0A3B4X4K3_SERLL        Unreviewed;      1628 AA.
AC   A0A3B4X4K3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Pappalysin 1 {ECO:0000313|Ensembl:ENSSLDP00000010622.1};
OS   Seriola lalandi dorsalis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000010622.1, ECO:0000313|Proteomes:UP000261360};
RN   [1] {ECO:0000313|Ensembl:ENSSLDP00000010622.1}
RP   IDENTIFICATION.
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   STRING; 1841481.ENSSLDP00000010622; -.
DR   Ensembl; ENSSLDT00000011010.1; ENSSLDP00000010622.1; ENSSLDG00000008407.1.
DR   GeneTree; ENSGT00940000156654; -.
DR   Proteomes; UP000261360; Unplaced.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   CDD; cd00033; CCP; 4.
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; IPR036116; FN3_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; 3.
DR   SMART; SM00032; CCP; 4.
DR   SMART; SM00560; LamGL; 1.
DR   SMART; SM00004; NL; 3.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 4.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50923; SUSHI; 3.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1628
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017361748"
FT   DOMAIN          1218..1289
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          1290..1351
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          1417..1473
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          728..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1628 AA;  181966 MW;  8D63674817F97B83 CRC64;
     MKLWTSPWVS CLVILILCFG SECGTARRKG RSKRELVRIR EAKATIPGAC ATRLPRGKRS
     LPGLERRVLR QHRRSSHAEE NSPDRGNAVY FTGMGDQLRL KPGVEIPRGN FTLEMWIKPE
     GGQRSPTVIA GLYDKCFYAS SDRGWLLGIQ AVSEHGNREP RFFFSLKTDR AHKVTSIHSN
     ARYVPNQWAH VAVTYDGVYM KQFVNGAQVG VSREQSGDVF SHLTKKCKVL MIGGNALNHN
     YRGAVERVGL WRQARGQRQI IRDMQGHDDP QDLPQLVIRE TFEHPSRKWL TVKDGSFPLL
     EQGGGGRFMG GGGVGNAEGL LDTTLDPPTC GQTVCDNVEV INNYNQLWTF RRPKKVRYRV
     INIWDDARMR PTVSDHQISL QHQQLNDAFS PYNITWELSI HNVTNSSLRN RLILANCDIS
     KVGDDACDPE CNHPLTGFDA GDCMSGHRSR CPEHKQGNGV CDPECNWENF LYDLGDCCNP
     NVTDVTKTCF NRSSPHKAYL DVKELKEILH LDGSTHLNVF FANSSDEDLA GVATWPWDKE
     ALTHLGGIVL NPSFYGTFGH TDTMVHEIGH SLGLYHVFRG ISEIESCNDA CLETEPSMET
     GDLCADTNPT PKYKGCHDPE PGNETCGCRH FTHTPFNNYM SYADDACTDS FTLNQVARMH
     CYLDLIYQTW QPYSKPPPVP MAPQVVEQHH NSITLEWFPP ISGHFYDREV GSVCDKCTEG
     KVLLQYASNS SSPRPCAPSG HWSPREAEGP PDVEQACEPS VRTWSPNAGT EHGVVGLSEC
     PLQGCMLQLE FPYPLVPDSL TVWVTFFSPE EAALPAIHNI LLLTVSGNNI PLGPSHVFCD
     TPLTLKLDTE EEVYGVQFFT MEQHLEIDAT LLASKPDCIL CRHCQPLRYR LLRQPPFTHA
     PHSLMLNEPT RRYTDRDVVP HVAYTYQVQT ISSRSESEPS PPLVHELGSP YCGDGQIQSS
     KGEECDDMNS MNGDGCSSQC KKEPFFNCVE EPSMCYYYDG DGVCEDFERE TGVRDCGLYT
     PSGFLDQWAS TVEVSHEEKP YCSGEVAAGY PAVTKTCQSK VFDLSDGVSQ YAWFPCREAH
     ESAWGYPSYW LKAHFSHPMV AAAVIIHLAA DGTGYIDQTQ CNITVQLVDT KEGIHSLGEW
     RLSCRTNPLV IPVNHDLSVA FYHTKAILVM FASRLVAISG VGLRSFQSFD PITISGCQSN
     EIYNPTGQSC VHYSCEAIDC QEPLIRNAEL KCSSPGRHFY NGDRCTISCN SGYVLQIHQD
     DDIIKSQSDS SVTITCANGK WNKQVSCEPV DCGLPDKYHV HPAHFNFPDG TTYGKKITFQ
     CREPAQLVGT NNTLTCLEDG LWSFPEALCE LRCPAPPPVP NAVLQTKRCN ETGLKVGTLC
     KYKCKPGYHV TNKPKRRAFK RQCTEDGSWL EGACEPVTCD PPPPIFHGSY HCTDGFRFDS
     VCRLNCSDPG AASNVIRCRK DGNWTGSFRL CPHSKGQCSL PQNLHYSLQY SCKRGHGIGE
     ECELSCRESN NDVVILPSNM TVESVLKEHW RNPNKVKTMV CTMGLKWYPH PEFLHCIKGC
     EPFMGDNYCD SVNNRAFCNY DGGDCCQSTV KTKKVIPFPM SCDIRDECSC RDPNAIENRK
     DEHVHSLG
//
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