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
//