ID A0A452RCC3_URSAM Unreviewed; 1280 AA.
AC A0A452RCC3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Papilin, proteoglycan like sulfated glycoprotein {ECO:0000313|Ensembl:ENSUAMP00000016344.1};
GN Name=PAPLN {ECO:0000313|Ensembl:ENSUAMP00000016344.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000016344.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000016344.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A452RCC3; -.
DR STRING; 9643.ENSUAMP00000016344; -.
DR Ensembl; ENSUAMT00000018305.1; ENSUAMP00000016344.1; ENSUAMG00000013018.1.
DR GeneTree; ENSGT00940000156891; -.
DR Proteomes; UP000291022; 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; 3.
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; 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 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 PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00131; KU; 1.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
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; 3.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 750..800
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 896..991
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1039..1114
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1133..1218
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1231..1270
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 485..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1280 AA; 138000 MW; ADD672B1DF0789E3 CRC64;
MGHASPRAVG WADPHGGPTC PSLPHWPLQR CPAGARDFRA EQCSQFDSQD FQGRRYKWLP
YYGAPNKCEL NCIPKGENFY FKHREAVEDG TPCEPGTRDV CVDGSCRVVG CDHNLDSSKE
EDKCLQCGGD GTTCYPVKGT FDANDLSRGY NQILIIPTGA TSIRVEEASA SRNFLAVKSV
RGEYYLNGHW TIGGAWALPV ASTVLHYERG AEGDLAPERL LARGPTSEPL VIELLSQEPN
PGVRYEYHLP LGSPRPGFRW SHGSWSDCSA ECGGGHQSRP VFCTTDNEVY PDHMCQPQLR
PADRRPCSTH PCPQTKRWQT GPWSPCSASC GGGSQSRSVY CVSSDGAGVQ EAAEGAECAG
LPGKPPTTRA CSLQRCAAWS AEPWGECSVS CGAGVRRRSV TCQSDEGSLL HATACSLEDR
PPITEPCVRE DCPPIHDQAW HVGAWGLCSK SCSGGTRRRQ VICALGPPSR CRSLQLSRPR
EVEPCNTQPC HLPPEVPSTQ DVHASPRDPR MSLGPHVAPT SGEKLNGNPQ PRAQEIEVEG
GASGLGGWRR WVWHGQMEVS SQLDTSCVFS FFLDSRDHWW LPQEQPSVQG NPRGAQGLHL
PGLAPSLPQS PHRQPLRSGL APQDCRHSPY GCCPDGHTTS LGPQWQGCPG ASCQQSRYGC
CPDGVSVAEG PHHAGCAGSY SSDSAARRRP GSRAVASSAS EAHQSQAQQN EPSECRGSQF
GCCYDNVASA AGPLGEGCVG QPSYAYPVQC LLPSAHGSCT DWAARWYFVP SVGRCNRFWY
GGCHGNGNNF ASEEECVSSC GGPQPAPRGP EPGASGQSTR IDGAGGSPGG QQEAGWHRTG
TTVQTKPWPS GGLWRRDQEP GPREESHSQV FGGWPWGGEL GPSAPGLGGD AGRPAPPSHG
SSYRVSLAGL QPSLVQAARG QLVRLFCQDD TSLEPHARWQ KDGQPISSDR HKPQPDGSLV
ISPLRAEDAG IYSCGSSRPG RDSQKIQLRV TGGDVAVLSE AVPRHFPQTR FPAQGHSPRD
SSLVGDRGSL WASSLQPRPT TRLLLDRNQP GVVDAQPGQR IRLTCRAEGF PPPAIEWQRD
GQPLSSPRHQ LQPDGSLVIS HVAVEDSGFY ACVAFSGQDR DQRWVQLRVL GELTITELPS
TVMVPEGDTA RLLCVVAGES VNIRWSRNGL PVRADGHRVH QSPDGTLLIH KLQARDEGSY
TCSAYRGSQA VSRSTEVKVI APALPAQPRD LSRECVDRPE LANCDLILQA QLCGNEYYAS
FCCASCSRFQ PPAQPVWQQR
//
