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Database: UniProt
Entry: A0A3B4ZAA8_9TELE
LinkDB: A0A3B4ZAA8_9TELE
Original site: A0A3B4ZAA8_9TELE 
ID   A0A3B4ZAA8_9TELE        Unreviewed;       781 AA.
AC   A0A3B4ZAA8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Papilin, proteoglycan like sulfated glycoprotein {ECO:0000313|Ensembl:ENSSPAP00000003454.1};
GN   Name=PAPLN {ECO:0000313|Ensembl:ENSSPAP00000003454.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000003454.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000003454.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3B4ZAA8; -.
DR   STRING; 144197.ENSSPAP00000003454; -.
DR   Ensembl; ENSSPAT00000003521.1; ENSSPAP00000003454.1; ENSSPAG00000002606.1.
DR   GeneTree; ENSGT00940000156891; -.
DR   Proteomes; UP000261400; Unplaced.
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   Gene3D; 2.60.120.830; -; 1.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
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; 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:SF317; PAPILIN ISOFORM X1; 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; 4.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SMART; SM00209; TSP1; 5.
DR   SUPFAM; SSF57362; BPTI-like; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR   PROSITE; PS50092; TSP1; 5.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR613273-3}; Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          679..729
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   REGION          527..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..754
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        16..51
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        20..56
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        31..41
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ   SEQUENCE   781 AA;  85816 MW;  6EE52689E0292D2A CRC64;
     VPGGDYWESW GPYGDCSRSC GSGVTVRTRR CITHTDGGHN CVGPDKSYSS CNIQDCPEGS
     KDFREEQCSK FDGTDFQGKR FKWLPYYGEN PCELICMPRG ENFFYRHGNA VVDGTPCHPG
     RRDICVDGVC KRLGCDSILE SHQQEDPCLQ CGGNGQSCHQ VKNSFKVYNQ MFIIPVGATT
     ISIRETVASR NYLIKNLRGE YYLNGHWVIE FSRATPIAGT VLFYQRGAEG DNVPETIIGR
     GPTTEPLVVE LISQEPNQGV EYEYYLPNGR SRDGYYWSFG SWSACSRECG SYQSRLVFCT
     IDNEAYSDYL CASLPRPQTN RTCNPHQCPQ VRMAYLYPPQ LWRSSERPRA YWKTGEWNAC
     SVTCGGGSQL RSVQCISHDA SGPRVVEDAV CAAYAEAPPT LQTCNMHKCA EYQVTAWSAC
     SVTCGSGEQT REVTCVGSGG MRLEETSCST LLRPAAVQPC QMVACSRQIS WHVGEWGLCS
     RSCGSGSRER QVICSDQERN LYPVAQCSAQ PKPTTVERCN SQPCYSPQVP SVQDPRGHDN
     SQTGFQPYVP DHATRRPETR DPAQTNTVQD PHSSAPALHC SQSYYGCCPD GRTSAGGPQG
     LGCPHTPAPT PSQPSCSRTY GCCQDGVTAA QGPNMLGCAA PSLPTENAVQ CRTTTYGCCY
     DRTTPAEGPN GEGCPNPPNH LPRGAGSCSG WVSRYHFDVI TSKCVHFWYG GCHGNSNNFM
     TRAECQRACP GPSHQADPRR GVHRQDRPLH RGGSGRPDGR AALQSQSSAF VRRRRGVETR
     R
//
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