ID E4Y1T6_OIKDI Unreviewed; 350 AA.
AC E4Y1T6;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|Pfam:PF00089};
GN ORFNames=GSOID_T00014152001 {ECO:0000313|EMBL:CBY15830.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY15830.1};
RN [1] {ECO:0000313|EMBL:CBY15830.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
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DR EMBL; FN653690; CBY15830.1; -; Genomic_DNA.
DR AlphaFoldDB; E4Y1T6; -.
DR InParanoid; E4Y1T6; -.
DR Proteomes; UP000001307; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24253:SF50; SUPPRESSOR OF TUMORIGENICITY 14 PROTEIN; 1.
DR PANTHER; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 1.
DR Pfam; PF00089; Trypsin; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001307};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 142..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..310
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|Pfam:PF00089"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 38861 MW; B61214149656FED2 CRC64;
MSSTEQSPRK SRLEKKKEHK RILADRLLKY AVLSKDDWTR SPDGRMTHRS VSQHSQSSRS
DFEDFRDGPM ESSPRTPRRV QSISRSSFST IRQPQPSGGT SPDLEDPEYE YVDGTKQKEK
EKGKSAVEGI NRSFGLDAQP RAAIVFGVNN FLILIALIIG FSIVGTQVAS IKSILTTEKN
GAVSNPLASK PRLAIQLREC ILPKHADPVV SYWYRKTGET SDSQHVSNGG RFDHAVNITE
KRAKSSGKDR FWLTQDGRIF GGDPADIEEY PWQTSLHSAA TGHQCGASLI TTKWLLTAAH
CKKASQNPAD WKAFFGIKYQ PSVENCANTN SCVLGQGGHW RLGSATHKIF
//
