ID J9J9F6_9SPIT Unreviewed; 668 AA.
AC J9J9F6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Gastricsin {ECO:0000313|EMBL:EJY87873.1};
GN ORFNames=OXYTRI_22475 {ECO:0000313|EMBL:EJY87873.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY87873.1};
RN [1] {ECO:0000313|EMBL:EJY87873.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY87873.1};
RX PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT with 16,000 Tiny Chromosomes.";
RL PLoS Biol. 11:E1001473-E1001473(2013).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJY87873.1}.
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; AMCR01000858; EJY87873.1; -; Genomic_DNA.
DR AlphaFoldDB; J9J9F6; -.
DR EnsemblProtists; EJY87873; EJY87873; OXYTRI_22475.
DR OrthoDB; 187067at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
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; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..41
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 42..668
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003825932"
FT TRANSMEM 588..612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..534
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 335..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 75347 MW; CE668E110F5C7E38 CRC64;
MSTNFTTIFS NKNYNIFCLL KSKRCSLYLL LLALILHFSK ACQHECELQN VLQTMNLPEE
HPLPEYIPRA EWSESGSIIL PLLVDDQQYQ QQNFNDYRSD LSDFVTEKSK YTLHSTNQRK
NINTNLKQSQ IPSAPQTNKQ LDYDGTFYTY LFVGNRSQPM KMIVSISSSW MILPNETIKQ
DTVNKYNSSN SQTYRELLTS HTYDDLQVSK YTINKDKAFV TGSVAQDIVQ LAYGDASLIV
DKFKFFSYNQ VSAYNKNYGI IGFGRDFISP SQNSGPLLLQ TLRQSGNLKN GVFSILIGGP
NDKSTIEIGG YNQLVVENIT SSQINLRPGF LAQSNSVNSS TPNQNSNQGS TTPSNNGSSG
NTGGNTQSKT KIKWFDNLFY AQEWQVEMNG YYINQTSKIL NGTQPGGNYT GKAIFSSTIQ
YLQFPDAVKD QILKRLTMDK QNQTLQFLNS EDGQYLTFAT CNASRYPSLW LRLEDAWFEI
KPQTFIMEKP ATVQGDYCPI GISSSGSNDV VLGLVFLRNY YMIFDFDNDN IGLSKNKYTL
SSFYDGPPPQ MINFTAQISQ PIPANTSPTN NGGSTSSSNW FNMSDQTILI IEIVVLSILV
VCIGGFLVWY YFFRTMLSGQ YQNKFDMDGQ LPMHPYNISP NQLKKVSLKS SLNLITQPTT
ISIVMLDV
//
