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Database: UniProt
Entry: A0A093ERB4_TYTAL
LinkDB: A0A093ERB4_TYTAL
Original site: A0A093ERB4_TYTAL 
ID   A0A093ERB4_TYTAL        Unreviewed;       935 AA.
AC   A0A093ERB4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   28-JUN-2023, entry version 36.
DE   SubName: Full=Papilin {ECO:0000313|EMBL:KFV42933.1};
DE   Flags: Fragment;
GN   ORFNames=N341_09522 {ECO:0000313|EMBL:KFV42933.1};
OS   Tyto alba (Barn owl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX   NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV42933.1, ECO:0000313|Proteomes:UP000054190};
RN   [1] {ECO:0000313|EMBL:KFV42933.1, ECO:0000313|Proteomes:UP000054190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV42933.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KK369771; KFV42933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093ERB4; -.
DR   Proteomes; UP000054190; Unassembled WGS sequence.
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; cd22635; Kunitz_papilin; 1.
DR   Gene3D; 2.60.120.830; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 4.
DR   InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR   InterPro; IPR045371; ADAMTS_CR_3.
DR   InterPro; IPR010294; ADAMTS_spacer1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR   PANTHER; PTHR13723:SF179; PAPILIN; 1.
DR   Pfam; PF19236; ADAMTS_CR_3; 1.
DR   Pfam; PF05986; ADAMTS_spacer1; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 3.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SMART; SM00209; TSP1; 4.
DR   SUPFAM; SSF57362; BPTI-like; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50092; TSP1; 4.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR613273-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          738..788
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   DOMAIN          905..935
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          544..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          795..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..815
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        18..54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        22..59
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        33..44
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV42933.1"
FT   NON_TER         935
FT                   /evidence="ECO:0000313|EMBL:KFV42933.1"
SQ   SEQUENCE   935 AA;  101963 MW;  F3C5B3B5779EF5F5 CRC64;
     RMKRQLDVWG SWGEWGKCSR SCGGGVSFRQ RRCYSQRTEG ASSCVGPTRS YRSCNIQSCP
     EGSQDFRAEQ CAEFDGTEFQ GKKYKWLPYY GAPNKCELNC IPKGENFYYR HKEAVVDGTT
     CEPGKRDICV EGVCQAVGCD NMLESAKKED KCLQCGGDGS TCYGVKGTFD VPSLPKGYNQ
     IFIIPVGATS IQIKEVMPSR NFLAIKNVRG EYYLNGHWTI DFSRALKVAS TIMHYDRGSE
     GDLAPELLHA QGPTTEPLVI ELISQEPNPG VQYEYYLPVQ GQASGYSWSY GSWRYSLASP
     LGFQSRLVFC TIDNEIYPDY MCRSKPQPDN NRTCGHQTCP QTKRWKTGEW GSCSATCGGG
     TQTRSVYCVA FDGQSSQGVV DNAECMAFAQ QPRSSQPCNV RQCATWSTGP WSECSASCGE
     GVQTRTVTCR TQQGSQAQDF SCLMEPKPSA TQPCLKENCI QEIGWHVGDW GLCSKSCSSG
     IRTRQVICAD GDSKFYSPET CKAIQPQKPA TLGSCNMQPC YLPQQVPSMQ DTMGYDVTRQ
     SLLTRYNPNG PATDSGDERM LSGSSTIQST SGNHYIPSTK DRGINLLPVR WESQSRSSGS
     HQLSFSQDPP GGAGSQDCQR SPHGCCPDGH TPASGPLGRG CSFSSCHRNR YGCCPDGVSA
     AQGPNNMGCP QYYRDVQVSR NQPTAATPTA SQALSQQYPS GECRSSVYGC CFDNVASASG
     PRGEGCLNRP NYPYPVICLL PSAHGPCANW TTRWYFVTVV GKCNRFWYGG CHGNKNSFAS
     EEECMRVCHN SEGVSPLEHQ PSSGTGALQH QHTGSRSHTG DARAVPGPSE RRRSGGGEQW
     HKAFGADVSV TEGFGHQASA DSFPAWALHR GARGEEGCRG ANRITFSFRA ILEEAKPSLV
     TAVVGQNVQL VCKTGVSPSS RVEWVKDGRP VSSDR
//
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