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Database: UniProt
Entry: A0A0V0SLD7_9BILA
LinkDB: A0A0V0SLD7_9BILA
Original site: A0A0V0SLD7_9BILA 
ID   A0A0V0SLD7_9BILA        Unreviewed;      1040 AA.
AC   A0A0V0SLD7;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   SubName: Full=Transmembrane protease serine 9 {ECO:0000313|EMBL:KRX27203.1};
GN   Name=CELA2A {ECO:0000313|EMBL:KRX27203.1};
GN   ORFNames=T07_4619 {ECO:0000313|EMBL:KRX27203.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX27203.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX27203.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX27203.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KRX27203.1}.
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DR   EMBL; JYDL01000004; KRX27203.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0SLD7; -.
DR   STRING; 6336.A0A0V0SLD7; -.
DR   Proteomes; UP000054630; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR008253; Marvel.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24253:SF153; FI06405P-RELATED; 1.
DR   PANTHER; PTHR24253; TRANSMEMBRANE PROTEASE SERINE; 1.
DR   Pfam; PF01284; MARVEL; 1.
DR   Pfam; PF00089; Trypsin; 2.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR   PROSITE; PS51225; MARVEL; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 2.
DR   PROSITE; PS00134; TRYPSIN_HIS; 2.
DR   PROSITE; PS00135; TRYPSIN_SER; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Membrane {ECO:0000256|PROSITE-ProRule:PRU00581, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:KRX27203.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00581,
KW   ECO:0000256|SAM:Phobius}; Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1040
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006868949"
FT   TRANSMEM        743..762
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        840..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        880..902
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        914..938
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        958..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          48..288
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DOMAIN          305..544
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DOMAIN          831..982
FT                   /note="MARVEL"
FT                   /evidence="ECO:0000259|PROSITE:PS51225"
FT   REGION          1014..1040
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1014..1034
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1040 AA;  116819 MW;  A81CC104033EA501 CRC64;
     MILFFYIVSF SFLLKLNLIL SEIVNSPYCG KSVHQEKLTY HKKIQNRIVG GWKAYDGSLP
     WMVHLTFPAE EGFSQMCGGS LISVDGKNST CLVLTAAHCV KLGNQYKEPG DILVAIRQNH
     LKHARDEAIF LHVKNYVSHF FHEDSLENDI AILRLEKWVL FTKYVRPLCL PSANMRLPFG
     EECYAAGWGR TNVEKEEGML KIVKMQLQMS KFCPRQFIQE KMLCAGNLGG GHDVCNGDSG
     GPLFCMVGDR FYLFGIVSFG YNDCALQGVS SAFVRVTSYL DWIEKTALTL KNIKINNRKN
     GTNRIVGGWN SHPGSIPWMV YLIFPQDELH IQSCGGTLIS IDGENRTSLV LTAAHCLMMN
     NKYKQPGNIY VAVGQHNVKR AEPEAFFLSV KNYVSHFYHN TSFENDVAIL KLEMPVVFTD
     HIRPVCLPKV NMELPSDADC YASGWGETHE EDHGYLKVVQ AKLQDASFCP KEYRSDNMIC
     AGNLEGGHSI CQGDSGGPLF CLIDDRFYQI GIASFAYFAC DLPNTAAVFV RVNTYLEWIE
     MAGRKLSLSK IKNTKRETYS SIYLPKIQST VANSLLAKAY QSPFEKSPSR LIAAMGVHAW
     YLHKCCSGKL FASHICYEHR RACTSSSIHV YTHKHDEYVH FDFFHILCIC KGCYKSSESQ
     NLTITDEPVV VASVRFNAFD MAKETLFNQE KSKSQGLFHR VLKLEHTSQN RVLTYVNFIA
     VETSCSVQEK LKKCIQNNAH LRFQGSFLIA KELFGIIGLI VLQKIIQCAT KTRTRNTQSS
     CMLFSKYIIY SMTDFSDFKG ALNFGKFYVH IEMDMTGRAY GAGMAGSEIN WRKAIQNPRC
     ILRALFAIIV FGSISSRAWY KNPGGDVICL FGESNFSCTF GNGLGILSFL MCIGMIVSDI
     MFENISAIST RKRVVVGDLA SSGIMTFLWF IAFCTLANKW SSMKLTDAMK VAASPCEAAI
     AFSFFSTISW AGLAFLGWKR YKEGAESAFA PTYDQDFSAS PYTYPTGYAE EPYQQSTFPG
     STQSTFAPTN FEAPYQPPTY
//
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