ID A0A0V0WW32_9BILA Unreviewed; 1094 AA.
AC A0A0V0WW32;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Transmembrane protease serine 9 {ECO:0000313|EMBL:KRX79523.1};
GN Name=SYNGR2 {ECO:0000313|EMBL:KRX79523.1};
GN ORFNames=T06_6547 {ECO:0000313|EMBL:KRX79523.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX79523.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX79523.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX79523.1};
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:KRX79523.1}.
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DR EMBL; JYDK01000051; KRX79523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WW32; -.
DR STRING; 92179.A0A0V0WW32; -.
DR Proteomes; UP000054673; 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; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 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:KRX79523.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
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..1094
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006872183"
FT TRANSMEM 685..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 891..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 934..956
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 968..992
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1012..1032
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 355..594
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 885..1036
FT /note="MARVEL"
FT /evidence="ECO:0000259|PROSITE:PS51225"
FT REGION 1068..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 123038 MW; B8902352E183D00F CRC64;
MILFFYIVSF SFLLELHLIL SEIVNSPYCG KSVHQEKLTY HKKIQNRIVG GWKAYDGSLP
WMVHLTFPAE EGFSQMCGGS LISLDGKNST CLVLTAAHCV KLGNRYKEPG DILVAIRQNH
LKHARNEAIF FHVKNYVSHF FHEDSLENDI AILRLEKWVL FTKYVRPLCL PSANMRLPIG
EECYAAGWGR TNVEKEEGML KIVKMRLQMS KFCPRPFIQE KMLCAGNLGG GHDVCNGDSG
GPLFCMVGDR FYLFGIVSFG YNDCALQGAS SAFVRVTSYL DWIEKTAITL KNIKINNRRN
GTVSSIFLPK MQSKFSNSMM VKAHNSPFEN SPSRLIAAMG VYQNKLKNLP SQNRIVGGWN
SYPGSIPWMV FLVFPHDESY IQSCGATLIS IDGENRTSLV LTAAHCLMMN NKYKQPGNIN
VAVGQYNVKR AEPEALFLSV KNYVSHFYHN TSFENDVAIL KLEKPVVFTD HIRPVCLPKV
NMELPSDADC YASGWGKTYE EDHGYLKVVQ VKLQDAFFCP KEYRSDNMIC AGNLEGGHSI
CQGDSGGPLF CLIDDRFYQI GIASFSYVAC DLPNTAAVFV RVNTYLEWIE MAGRKLSLSK
IKNTKRETYS SIYLPKIQST VANSLLAKAY QSPFEKSPSR LIAAMGVHAY LHKCCSGKLL
RHTFVMNTDV HAHLPPYMYT QTDTMNIYIL TFFIFCAFAK DDIVTNDFQE SSESQNLTIT
DEPVVVASVR FNAFDMAKET LYNQEKSKSQ GFFHRVLKLE HTSQNRVLTY VNFIAAETSC
SVQEKISVEE VYSKQCSPTF PRKLHDCEGT LWHYRANSSA ALKRHDKLFM LFSKYIIYSM
TDFSDFKGAL NFGKIISFYV HIEMDMTGRA YGAGMAGSEI NWRKAIQNPR CILRAVCMLF
AIIVFGSISS RAWYKNPGGD VICLFGESNF SCALGNGLGI WSFLMCIGMI VSDIMFENIS
AISTRKRVVV GDLASSGIMT FLWFIAFCTL ANKWSSMKLT DAMKVAASPC EAAIAFSFFS
TISWAGLAFL GWKRYKEGAE SAFAPTYDQD FSASPYTYPT GYAEEPYQQS TFPGSTQSTF
APTNFEAPYQ PPTY
//
