ID A0A0V1HCX2_9BILA Unreviewed; 1074 AA.
AC A0A0V1HCX2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Transmembrane protease serine 9 {ECO:0000313|EMBL:KRZ08627.1};
GN Name=Tmprss9 {ECO:0000313|EMBL:KRZ08627.1};
GN ORFNames=T11_14767 {ECO:0000313|EMBL:KRZ08627.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ08627.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ08627.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ08627.1};
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 -!- 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:KRZ08627.1}.
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DR EMBL; JYDP01000084; KRZ08627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HCX2; -.
DR STRING; 268475.A0A0V1HCX2; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 4.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR PANTHER; PTHR24250; CHYMOTRYPSIN-RELATED; 1.
DR PANTHER; PTHR24250:SF27; ELASTASE 2 LIKE; 1.
DR Pfam; PF00089; Trypsin; 4.
DR SMART; SM00020; Tryp_SPc; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 4.
DR PROSITE; PS50240; TRYPSIN_DOM; 4.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KRZ08627.1};
KW Membrane {ECO:0000313|EMBL:KRZ08627.1};
KW Protease {ECO:0000313|EMBL:KRZ08627.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000313|EMBL:KRZ08627.1}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1074
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006879054"
FT DOMAIN 52..225
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 238..487
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 513..771
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 804..1058
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
SQ SEQUENCE 1074 AA; 120635 MW; EA42E14F94918BC7 CRC64;
MNRLINFLLI WLLNFNVNVE SEVECGQNLH ENMSPVNKWK LNSTISMPKF NPWNVFISGK
NKACGGVLIQ VFQNNPTSEI VLTSSQCFID KDGHRLNHAN YKVFLGAYNF DENKRTTSRT
VGIKHITVME FDNQTMLNDL ALITLETTIQ FDYNIRAVCL PHFDFDLKDA DWISLTGWKT
DTKKNYELGG TGILQQIPIA TLSAEECQEI IPTFHRTYHT CDIECGISHY LPATLYTSVG
YPPNYTNAIA SPYSMPWNVI IQAEHKICGG VLIRIQKTAN SSNTVLSSSS CFSKKFGMKP
NHANTKVHLG VHKFPSDTDK VTVGIKHVTS TPYEQGMMKK DIALITLQAE VEFNEKIRPI
CFPHINFKPP VAYKYPLVGW ALSEIAKIKG IPYLLQVPVK LIDSSDCATM LKEFSKDDHI
CGYFADPHIF NNTVPLDHGS VITSLYQKNI FLIGMLSGII PIQNSSAHIL LFSRISTSVE
WIMRSSDPSS LVDFQQFLPS SETEVNIPCG RAIVQGPEIQ ASVGYPPNFK NVMAVPQSMP
WNVIVQAEIG TCGGVLIRFN EESNYTDIVL TSSRCFFKSY KADHANVKVH LGVHKLPLSR
NTVTIGVKYV TTTPFTKNDT QKDLALITLE GDVEISEKIR PICLPARDLE IPTPTVLWLV
GWNTMDGYGL PSKKIPFLMQ LPVLIITPSN CKKLFTNYSN NDHICGRYVD QFLFNITKNV
DYGSPLIGKN QDNMYVLGTF NGHIMNPNGT GSLLIFSRVS TAMEWIVRSS NPSSYIEENE
FVVVTNHKCG VEKFPQRKVY YEFMPNGTND EENLKEHIHA LPHSFPWSAL IRGKNRICGG
ALVAMPINYF YAEYVLTTAQ CFLDENDKYI NHDNYKVVLG AHNLARRQGQ VVVGIKQVTL
SAFDRSTMGP DLALITLETA VDLNDQIQLI CLPIGDISMA ENDRLPLVGW NTSPDSNSTQ
QSIVLQQIPI ELHSDEQCEE VFQNYSPNKH ICGSIFDPAV KAFKPTVDIG SILSAEIANQ
TFLYGLFSGH LSSSSAENDI FLFNRIQYSA EWLMRTADPA FYTFHDIQIV YLHS
//