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Database: UniProt
Entry: A0A3B4D0H0_PYGNA
LinkDB: A0A3B4D0H0_PYGNA
Original site: A0A3B4D0H0_PYGNA 
ID   A0A3B4D0H0_PYGNA        Unreviewed;      1108 AA.
AC   A0A3B4D0H0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Cubilin-like {ECO:0000313|Ensembl:ENSPNAP00000017053.1};
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:ENSPNAP00000017053.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000017053.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR   AlphaFoldDB; A0A3B4D0H0; -.
DR   STRING; 42514.ENSPNAP00000017053; -.
DR   Ensembl; ENSPNAT00000025707.1; ENSPNAP00000017053.1; ENSPNAG00000023299.1.
DR   GeneTree; ENSGT01030000234528; -.
DR   OMA; QVWPASQ; -.
DR   Proteomes; UP000261440; Unplaced.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00041; CUB; 6.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 6.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24251:SF37; CUB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR   Pfam; PF00431; CUB; 6.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00042; CUB; 6.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 6.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01180; CUB; 6.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157}.
FT   DOMAIN          47..155
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          166..279
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          312..423
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          434..549
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          589..836
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DOMAIN          847..957
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          968..1078
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   REGION          39..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1108 AA;  120894 MW;  5C814FC84DAD26BA CRC64;
     MASKKGLTNL EKSLIVLFVA MTLACIGLIV VYVTERNNSK TENKEGDPGQ LSGNSGEFSS
     GNYPSNYNNG MSCSWHITVE NNKVIHLWFQ DFSLEDSGTC SADSLTLRDN LGIIGKYCGH
     SKPKPVVSLG NTLVVYFDTN DRQMDRGFKA MYHAVDPEAV TEIVGAGGVL QGDRGELMTP
     GFPEQSYESG VLYQWRIVVS AGNKVHLNFT AFDLVPDSCG DFVDVFDGHS DDVSATKLGH
     FCGNQMPEPV VSSSNEMVVR FKSDSGQTAK GFSAVYTVVT DPPVTSTTTT TSTTQTNTTT
     PSITSAPIDS GCGSLETLSG RKGVIHSLGF PNVYPANLQC SWNISVDEGL LIKLHITDLA
     IVGEAGQCGQ DQLTVSDSQQ SLGTHCGFIL PPVLVSVSNR MSLTFQSDGR LADRGFSARW
     EAVYPEDIAE IQGCGVFSHE EMGVIKSENW PMNYPPNREC LWKVQVPEGK TITLTFTQFD
     MEAAGILLGR CLDNVIIYDG SQPMAKKYGP YCGTSIPPVI HTTGNELVMR FYADFFMEAK
     GFRAFWTTDP TLPAPTEPPV PPNPWDDIPI EWPETCGRPA IPPMVNARIV NGEAAKAHSW
     PWQVSMQVWP KSITSCPVTP YTSSAHLSTH ANVYLRYHQL QRWQMCLGKH NLTLSEPGQQ
     CFGVQGIYRH KGFNYPTSPT VEFDIALVRL DGEVTPSDHV HFACLPPIEE VLPEGKTCYA
     TGWGDETGNF SAPKASETLN QVALPVVPYD TCKRMDYWWF QVKSSMICAG YNLPDELKSV
     CQGDSGGPLV CQDGPTGPWE VHGITSFGPI GCIMNKKPSV FTRTSAYLPW IENIMRKDSY
     DGITSGCGGL KEQTGTEGVL SSMNHPQGYE NGARCQWNIV VPAGKRVHLH FDTFSLEESQ
     LCLSDSVSIS DSLGSLGTHC SISPPADLVA VGATLTVHFS SNDRVVDTGF KATWRAVDPA
     DISNLVGCGG EFVGQQGELQ SPNWPNNYPD QAACTWTISS PSAKSLHIVF TDFELQAVNI
     LGKCVDFVEV FDAAGQSQGQ FCGFGPPKLT VTGDRATVRF RTNKEVQGKG FRGYWTTDPN
     VFPTSGKNHM LNNDIIVVNY NYRTVNCS
//
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