ID T1PCP7_MUSDO Unreviewed; 2926 AA.
AC T1PCP7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Pancreatic trypsin inhibitor {ECO:0000313|EMBL:AFP61083.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EMBL:AFP61083.1};
RN [1] {ECO:0000313|EMBL:AFP61083.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ALHF {ECO:0000313|EMBL:AFP61083.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:AFP61083.1};
RA Liu N., Zhang L., Li M., Reid W.;
RT "Transcriptome of adult Musca domestica launches a platform for comparative
RT house fly gene expression and characterization of differential gene
RT expression among resistant and susceptible house flies.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KA646454; AFP61083.1; -; mRNA.
DR MEROPS; I02.955; -.
DR VEuPathDB; VectorBase:MDOA000157; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR CDD; cd00109; Kunitz-type; 8.
DR CDD; cd22639; Kunitz_papilin_lacunin-like; 1.
DR CDD; cd00199; WAP; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 12.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR008197; WAP_dom.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF281; NO LONG NERVE CORD, ISOFORM C; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF00014; Kunitz_BPTI; 12.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 5.
DR Pfam; PF00090; TSP_1; 1.
DR Pfam; PF00095; WAP; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00131; KU; 12.
DR SMART; SM00209; TSP1; 7.
DR SMART; SM00217; WAP; 1.
DR SUPFAM; SSF57362; BPTI-like; 12.
DR SUPFAM; SSF57256; Elafin-like; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 7.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 6.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 12.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
DR PROSITE; PS51390; WAP; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..2926
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004583146"
FT DOMAIN 1765..1815
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1824..1874
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1883..1933
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1943..1993
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2002..2052
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2076..2126
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2158..2208
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2244..2294
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2301..2351
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2369..2419
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2428..2478
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2493..2546
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2625..2671
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 2690..2787
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2789..2878
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2885..2924
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 699..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1452..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2053..2076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2129..2151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2215..2236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..722
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 69..105
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 73..110
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 84..95
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 2926 AA; 315666 MW; 29E5C6E15C910258 CRC64;
MDLSGRSRLP PLIALLIIVC VQTSQARFFG DRLKRQNGAN MYLPASSIVP GGEGDDPNEW
TEWSSPSECS RSCGGGVSYQ TRECRRTGPD GSPMCSGGNR RYFSCNTQDC PEDEPDFRSQ
QCARFNNVPF DGIFYNWVPY KSAPNPCELN CMPKGERFYY RHKAKVIDGT RCNDEDLNVC
VDGQCLPVGC DMMLGSNAKE DKCRQCGGDG TTCRTLKDRF TTNNLATGYN DILLVPSGAT
NIRITETAPS NNYLACRNLT SHYYLNGNWR IDFPRPMFFA GSWWTYQRKP HGFAAPDQLT
CRGPITESIY IVVLVQDKNV SVDYEYSIPQ TVISNTPAVY NWTHMEFGPC SASCGGGVQH
RNVSCNNRFN LDRVDDHFCD ERTKPVESQE CGTEPCAPHW QTAEWGKCSK GCGSDGVQNR
TVTCERISPT GERTVEDDAV CLQEVGNKPA TEQECNRDVK NCPKYHLGPW SPCDKLCGEG
KKTRKVTCYI EENGRKRVLS DEDCVEEKPE TETTCMLAPC EGVDWIISQW SGCDACGQTT
ETRTAICGSK SGKVYPDEFC APEVPLLSRP CESKKCKTQW FTSEWSKCSS PCGKGVQSRV
VLCGEFDGNT VTKVTDESKC DAAMKPEASK ECEGEEKECP GQWFTGPWGE CSKLCGGGER
QREVMCLANG TKSDNCDKNK IEALSEKCNT QACTDDEVLP VDSADKEISD DDEEDCEDEE
EEDVKVVTAK MSEDLKISDG IELDEETTVS SFITDELMMS DSTPPTDTTD EAASTDAPLT
TVEGSGDATE STSLSSMDTE EGSGDMETTS ESGVTESQTG STEGSVGTED TTVDLLETTG
SSSTDETTDA PVTDSTDSSA STESSTDLTK EPEGVSGSTQ DFTEESTESP GTTDGVTEAT
GSTDVSSSTD ATQTTDITSS TDASEPTGAT GSSTDVSGST EASTESSTTI DVSDTTDATD
STAASVSTDA SDSTDATSST DVSDTTDAPA STDASSSTEN SAATEDSTTS DTSTETSAST
LSDVTETTSS DITDPTDTTP SDTTPPTDTT PSDTTPSTDT TASDATSSTD ASSSTDATSD
TTPSSDATTE ESGSTGVSET TTAASSDATD VSGTTDVSAS TDVSGSTDPS TSTEGSDSTT
DVSESTDSSG STEASTATET TDSSDTTDVS GSTESFVSTD ASASTTDSSD STDESSSTDE
STESSGSTVT EAEATLSTDE TSESSPAAST ASTDVGSTDF SSTVATDITD TTTDSGISTS
TEAAEDTTTD ASGQTTSSDT TGLSDVTTET GSEATTSGSD TTSAESSETT TSSQDLSTSS
DVFDSTTESS GDTSLSTDEA TTVDIWTSED DEFEKSTPNT LQAVITKETR PRKCKRKKPK
DCSKTKYGCC PDGKSLAKGP FDEGCPIPKT CKDTEFGCCP DGVSPAAGSN NEGCPKSQCA
ETLFGCCPDK FTPAEGEDDE GCPEPTTEPP TTTTEMPEEE TTMSTEPALE NYVSTEEPES
SESTEVPETT EAPATPEIIQ SCSFAEFGCC PDGTTEATGP DFAGCDAPTL TSSTDCRSSE
FGCCPDGRTA ASGPNYQGCP ACTHEPFGCC PDNETPAHGS MGEGCCLNSV YGCCPDNINS
ARGPNFEGCE CQYAPYGCCP DNKTAALGPN NKGCDCESSQ FGCCPDKLTA AQGSNFEGCA
CHTFQFGCCP DGITVAQGPQ QQGCHCLQTP FKCCPDEKTP AKGWNFEGCT CLESKYGCCP
DGVTSAQGSK FEGCENVKEP PQKACGLPKE TGPCGDFSIK YFFDTSYGAC AKFWYGGCEG
NGNRFESESE CKETCQEYTG KEACYLPKSS GPCTGDLTKW YFDAERGRCE QFKYGGCFGT
NNRFDTKEEC QSFCAVSETT PPCDQPMDEG PCEGNFERWY YDNQTDVCRP FRYGGCKGNK
NNYPTEYACN YHCRQPGVHK DYCSLPKQTG DCSEKHPRWH YSETEKKCLP FYYTGCGGNK
NNFPSLESCE VHCPKEVAKD ICEIPAETGG CDNYQPMWYY DTKHQRCREF YYGGCGGNEN
KFASEESCMR RCEKKPEPKP QPQPEPEQPA VSTNVCDEPP AQGPCGNFTL NWHYDRERGQ
CRQFYYGGCE GNGNRFETEE DCARKCISQA EPEPQPQPQP ESRPVEKAEP ETVEDNICLL
GQDMGDCDDY SVMWYFDSQE SRCNVFYYGG CGGNGNRFAT KEECDRRCLA ESEPEDLGNR
FGAPEPEPEP EVESSPEVES SNKCFLPVAH GNCLENEVRW YYNSEDGVCD RFVYTGCGGN
ANNYATESEC EDECFAVHNT CQLPALSGNC NETMIRWHFS EAEGRCLEFE FSGCRGNRNN
FVTERECVSM CGGEESQPQP EPQPAYSVCD LPMEAGECDN STTAWHYDRE SSSCVAFTYT
GCGGNGNRFL SREQCERQCG EFKGVDVCNE EVSSGPCRQW QTRFYFNKES RTCEAFTYGG
CQGTANRFES RAECEARCII GQEPTYTDTK DICKQQVDVG RCNGEALTER RWYYDDARGN
CVSFIYSGCA GNQNNFRSYE SCYNYCAKAE PAVNEVLPVN RCEQYENECA ALSCPYGKHR
VAVDEECSRC ECDNPCADYE CPDGQQCAVE VSNERSGEFK PECRLINKPG ICPRLTASDG
VCGRECNTDA DCRENNKCCS NGCGFVCVHP AVPTRPTTAP TTPAPVVVYP EDVKASLVPK
EKAETDVNTP LGGIAVLRCF ATGNPAPNVT WSRNNVVVDT NQGRYVLTSS GDLTIVQVRQ
TDSGSYVCLA SNGLGEPVRR EIELQVTVPV NAVIGKDPSN TYQPGSTVAF SCSVQGYPTP
NVTWTKDGLP LVPSERVQIS VREPYRVIIN NVSTTDSGKY GCKAANAVSY SFSEENINIE
STIPLNPECI DNGHFANCNL IVRGRYCKNK YYAKFCCRSC ALAGQL
//
