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Database: UniProt
Entry: A0A091D171_FUKDA
LinkDB: A0A091D171_FUKDA
Original site: A0A091D171_FUKDA 
ID   A0A091D171_FUKDA        Unreviewed;      1261 AA.
AC   A0A091D171;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Papilin {ECO:0000313|EMBL:KFO24233.1};
GN   ORFNames=H920_14363 {ECO:0000313|EMBL:KFO24233.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO24233.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO24233.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO24233.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN123629; KFO24233.1; -; Genomic_DNA.
DR   RefSeq; XP_010643734.1; XM_010645432.2.
DR   AlphaFoldDB; A0A091D171; -.
DR   STRING; 885580.ENSFDAP00000019224; -.
DR   Ensembl; ENSFDAT00000012935; ENSFDAP00000019224; ENSFDAG00000009295.
DR   GeneID; 104877102; -.
DR   CTD; 89932; -.
DR   eggNOG; KOG3510; Eukaryota.
DR   eggNOG; KOG4597; Eukaryota.
DR   OMA; KLDSGWF; -.
DR   OrthoDB; 2910701at2759; -.
DR   Proteomes; UP000028990; 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; cd00096; Ig; 1.
DR   CDD; cd22635; Kunitz_papilin; 1.
DR   Gene3D; 2.60.120.830; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
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; 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; IPR013106; Ig_V-set.
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   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; PF07679; I-set; 1.
DR   Pfam; PF13927; Ig_3; 2.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   Pfam; PF16626; Papilin_u7; 1.
DR   Pfam; PF08686; PLAC; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 4.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00406; IGv; 3.
DR   SMART; SM00131; KU; 1.
DR   SMART; SM00209; TSP1; 5.
DR   SUPFAM; SSF57362; BPTI-like; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
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; PS50835; IG_LIKE; 3.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 5.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR613273-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1261
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001871229"
FT   DOMAIN          740..790
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   DOMAIN          889..981
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1019..1106
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1113..1198
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1212..1251
FT                   /note="PLAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50900"
FT   REGION          546..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          797..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          983..1037
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..601
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..833
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        38..74
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        42..79
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        53..64
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ   SEQUENCE   1261 AA;  136238 MW;  F7544B28C0C49D5A CRC64;
     MRLLLLLPLL VVWAPGSSAP EARQQSDTWG PWGEWSPCSR TCGGGISFRE RPCYSQRKDG
     GPSCVGPARS HRICRTESCP EGARDFRAEQ CAELDGALFH GRRYRWLPYY GAPNKCELNC
     IPEGENFYYK HREAVLDGTP CDPSRRDVCV DGHCRVVGCD HELDSSKEED KCLQCGGDGT
     TCYPVTGTFA ANDLSRGYNR IFIIPAGATS IRIEEATASR NFLAVRSVRG EYYLNGHWAI
     SEAKALPVAS TILHYERGSE GDLAPERLQA RGPTSEPLII ELISQEANPG VHYEYYLPLR
     SPESSQGFSW SHTSWGDCSA ECGGGHQSRL VFCTSDKEVY PSHMCQRHPR PADHRSCNSH
     PCPQTKRWKI GPWAPCSASC GGGVQSRSVY CVSSDGAGGQ EAAEEAECAG LPGKPPSTQA
     CNLQRCAAWS AGPWGECSVT CGAGIRRRSV TCRGDQGSLF PASACSLEDR PPIMETCVQA
     ACPLLSDQAW RVSAWGLCSK SCSSGIRKRQ VICAIGPPSH CRNMQQSKPR DVEHCNMQPC
     HLPQEVPSVQ DSHAHPRGPW MPLGPRKTLA SDSRDQRPWV PNRSRGLPDS PPSPPGQTPS
     LQQPPRSGLR AHNCRHSTYG CCPDGHTASL GPQGQGCPRT EAWCQQSRYG CCPDGVSAAK
     GPQQAGCGRS YGSDNAGRRP GSKEVPSTAS KVHRPQAQQN EPTECRGSQF GCCYDNMASA
     AGPLGEGCTG QPSSAYPVRC LLPSAHGSCA DWAPRWYFIP SVGLCNRFWY GGCHGNANNF
     ASEQECMDSC RGAQHGPHLP EPAATGLGTH TDGRGSGARG RQETNRHRPG DTDQRLSPSS
     GGPWRREQEP LPGETHPTRT FGEWPGGQEI GHRTPGLGRD SRWPVPPSPS SSYRISLAGS
     GPSEVQAAMG QQIQLFCPAD VSRESQAGWQ KDGQPISSDR HQLQSDGSLV IGPLRAEDAG
     VYSCGGNRPG RDPQRIQLRV TGGDLAVPSE SEPRHFPRTR DPARGQGEGT GVPSSQPRPA
     TRLRLDHTQP GVVDTNPGQQ VRLSCRAEGF PSPVIQWQRD GQPVASPRHQ VQPDGSLVIS
     RVAVEDGGFY ACVAFNGQYQ DQRWVQLRVL GELTITGLPP SMTVSEGDTA RLSCVVGDAS
     ANIRWSRNGV PVQADGHRVH QSPDGTLLIH NLRAQDEGSY TCSAYRGSQA VSRSTEVKVA
     VPAATTQPRE AGGGECIDQP ELANCDLILQ AQLCGNEYYS SFCCASCARF QPRARPAQQQ
     G
//
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