ID   A0A077Z943_TRITR        Unreviewed;       602 AA.
AC   A0A077Z943;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Pregnancy-associated glycoprotein 12 {ECO:0000313|EMBL:CDW56143.1};
GN   ORFNames=TTRE_0000441801 {ECO:0000313|EMBL:CDW56143.1};
OS   Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW56143.1};
RN   [1] {ECO:0000313|EMBL:CDW56143.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Aslett M.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDW56143.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA   Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA   Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT   "The whipworm genome and dual-species transcriptomics of an intimate host-
RT   pathogen interaction.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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   EMBL; HG806012; CDW56143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077Z943; -.
DR   STRING; 36087.A0A077Z943; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 4.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF45; ASPARTIC PROTEASE 6; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 3.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..602
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001728731"
FT   DOMAIN          66..405
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DISULFID        97..102
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   602 AA;  68301 MW;  6A422EA1D5A74D1A CRC64;
     MSALSILPHL FAFLLLFIIC GTEVRIPLRT VDAGTTRSKN VSENMNEQSL KLLGQQRLYD
     YANILTIGDI TIGTPPQTFS VMIDTASADT WIPGRYCSYS GCGSMKEFDS SLSSTYYRNG
     LKVAIGHGPG TVYGFTAADS ICMVNLCSRR QEFVEGYQTS WYYWNFPYDG VLGLAFPASS
     RIYSKNMVIN LAESGLLSQP IFTIWKARQK LEMKYLGTKA NPEKNANYFR RAQKGIESGL
     LTVGAQDSLH CSASCLYVTT ARDYWRFTVN RGYVLSEGFP EGNKTKAYYR TFNAIVSSSS
     LLIHGPSYDI WNIATRLEAW YSTSYAMYMV DCKLAKSLPD VILTINGVDL PISAENYIIK
     TSTGVCLLAF QKMAPTPKFD WVLGEPWLQQ YCHIQSFCSE KQSFIQAYQT TYNFWEIPYD
     GVLGLAPSQD SLIRESNAIT NIVQSKALNQ SIFTIWKARK PWTVSVGQAT FSKRNLTKAQ
     YYSSYECSTS SSLPFILGPQ KEIMRIARLL KAKYNPLYRL FYINCDDEKT LAPVWFNAEN
     VALPINPENY IIRISNMCLL AFQMNTQFRY GPDWVLGEPW FKQYCVVHDF TNRRIGFCPS
     MM
//