PPN_MOUSE
ID PPN_MOUSE Reviewed; 1280 AA.
AC Q9EPX2; A2RTE8; B2RQC4; Q99JQ8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Papilin;
DE Flags: Precursor;
GN Name=Papln;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1;
RX PubMed=11076767; DOI=10.1242/dev.127.24.5475;
RA Kramerova I.A., Kawaguchi N., Fessler L.I., Nelson R.E., Chen Y.,
RA Kramerov A.A., Kusche-Gullberg M., Kramer J.M., Ackley B.D., Sieron A.L.,
RA Prockop D.J., Fessler J.H.;
RT "Papilin in development; a pericellular protein with a homology to the
RT ADAMTS metalloproteinases.";
RL Development 127:5475-5485(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the papilin family. {ECO:0000305}.
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DR EMBL; AF314171; AAG41980.1; -; mRNA.
DR EMBL; BC005747; AAH05747.1; -; mRNA.
DR EMBL; BC132475; AAI32476.1; -; mRNA.
DR EMBL; BC137854; AAI37855.1; -; mRNA.
DR CCDS; CCDS26031.1; -.
DR RefSeq; NP_570957.2; NM_130887.3.
DR AlphaFoldDB; Q9EPX2; -.
DR SMR; Q9EPX2; -.
DR BioGRID; 228393; 1.
DR IntAct; Q9EPX2; 1.
DR STRING; 10090.ENSMUSP00000021646; -.
DR MEROPS; I02.972; -.
DR iPTMnet; Q9EPX2; -.
DR PhosphoSitePlus; Q9EPX2; -.
DR CPTAC; non-CPTAC-3604; -.
DR MaxQB; Q9EPX2; -.
DR PaxDb; Q9EPX2; -.
DR PRIDE; Q9EPX2; -.
DR ProteomicsDB; 291787; -.
DR Antibodypedia; 63258; 122 antibodies from 16 providers.
DR DNASU; 170721; -.
DR Ensembl; ENSMUST00000021646; ENSMUSP00000021646; ENSMUSG00000021223.
DR GeneID; 170721; -.
DR KEGG; mmu:170721; -.
DR UCSC; uc007odr.3; mouse.
DR CTD; 89932; -.
DR MGI; MGI:2386139; Papln.
DR VEuPathDB; HostDB:ENSMUSG00000021223; -.
DR eggNOG; KOG3510; Eukaryota.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000156891; -.
DR HOGENOM; CLU_000660_7_0_1; -.
DR InParanoid; Q9EPX2; -.
DR TreeFam; TF316874; -.
DR BioGRID-ORCS; 170721; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Papln; mouse.
DR PRO; PR:Q9EPX2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9EPX2; protein.
DR Bgee; ENSMUSG00000021223; Expressed in molar tooth and 38 other tissues.
DR ExpressionAtlas; Q9EPX2; baseline and differential.
DR Genevisible; Q9EPX2; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR CDD; cd00109; KU; 1.
DR Gene3D; 2.20.100.10; -; 5.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 4.10.410.10; -; 1.
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; IPR013151; Immunoglobulin.
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 Pfam; PF19236; ADAM_CR_3; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF08686; PLAC; 1.
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; SSF48726; SSF48726; 3.
DR SUPFAM; SSF57362; SSF57362; 1.
DR SUPFAM; SSF82895; SSF82895; 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 2: Evidence at transcript level;
KW Disulfide bond; Immunoglobulin domain; Protease inhibitor;
KW Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1280
FT /note="Papilin"
FT /id="PRO_0000324551"
FT DOMAIN 27..81
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 305..362
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 363..422
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 424..482
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 485..540
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 750..800
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 900..990
FT /note="Ig-like C2-type 1"
FT DOMAIN 1039..1128
FT /note="Ig-like C2-type 2"
FT DOMAIN 1133..1218
FT /note="Ig-like C2-type 3"
FT DOMAIN 1231..1270
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 541..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 39..75
FT /evidence="ECO:0000250"
FT DISULFID 43..80
FT /evidence="ECO:0000250"
FT DISULFID 54..65
FT /evidence="ECO:0000250"
FT DISULFID 425..464
FT /evidence="ECO:0000250"
FT DISULFID 436..476
FT /evidence="ECO:0000250"
FT DISULFID 440..481
FT /evidence="ECO:0000250"
FT DISULFID 750..800
FT /evidence="ECO:0000250"
FT DISULFID 759..783
FT /evidence="ECO:0000250"
FT DISULFID 775..796
FT /evidence="ECO:0000250"
FT DISULFID 926..973
FT /evidence="ECO:0000250"
FT DISULFID 1065..1112
FT /evidence="ECO:0000250"
FT DISULFID 1154..1202
FT /evidence="ECO:0000250"
FT CONFLICT 411
FT /note="V -> A (in Ref. 1; AAG41980)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="M -> I (in Ref. 1; AAG41980)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="R -> K (in Ref. 2; AAH05747)"
FT /evidence="ECO:0000305"
FT CONFLICT 858
FT /note="E -> D (in Ref. 2; AAH05747)"
FT /evidence="ECO:0000305"
FT CONFLICT 870
FT /note="Y -> H (in Ref. 2; AAH05747)"
FT /evidence="ECO:0000305"
FT CONFLICT 883
FT /note="V -> I (in Ref. 2; AAH05747)"
FT /evidence="ECO:0000305"
FT CONFLICT 932
FT /note="S -> P (in Ref. 2; AAH05747)"
FT /evidence="ECO:0000305"
FT CONFLICT 997
FT /note="F -> L (in Ref. 1; AAG41980 and 2; AAH05747)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1280 AA; 138904 MW; 4288A2EE204CB3E2 CRC64;
MQLFPLLFSL LLTSTPGSWA RNVRRQSDTW GTWGEWSPCS RTCGGGISFR ERPCYSQRRD
GGTSCVGPAR SHRTCHTESC PDGVRDFRAE QCAEFDGTDF QGRRYRWLPY YAAPNKCELN
CIPKGQNFYY KHKDAVVDGT PCEPGQRDIC VDGVCRVVGC DHKLDSIKQE DKCLQCGGDG
SSCYPVTGTF DGNDLSRGYN QIFIIPAGAT SIRIEEAAAS RNFLAVKSIR GEYYLNGHWT
IEAAQALPVA STVLQYERGV EGDLAPERLQ ARGPTSEPLV IELLSQESNP GVHYEYYLPA
NDPGRGFSWS HGSWGDCSAE CGGGHQSRLV FCTIDNEAYP DHMCQHQPRP THRRSCNTQP
CPKTKRWKVG PWTPCSVSCG GGVQSRSVYC ISSDGTGGQE AAEETQCAGL VGKPPTTQAC
NLQHCAVWSV EPWGECSVTC GTGIRKRSVT CRGDEGSPVH AAACLLKDQP TLTEPCVQEA
CPVFRGQAWH VGSWSLCSKS CGSGIRRRQV VCTIGPPGRC VDLQSSKPAE MEACNRQPCH
LPQEVPSIQD PRTRSSDPRM LSGPRVSPVS DGREQQWAPL ERPRAQSNPR EGQDPNLSSA
GRAPTLQRPP HQPPLRPSSG PRDCRHSPHG CCPDGHTPSL GPQWQGCPLA GASCLQSRYG
CCPDGVSAAE GPQQAGCTRS HGSDNTGNRP GSRAVASKNP KIHQPQAHEG EPSECRSSRF
GCCYDNVASA AGPLGEGCVG QPSYAYPVRC LLPSAQGSCG DWAARWYFVA SVGRCNRFWY
GGCHGNANNF ASEQECMNTC RGQHGPRRPE AGAAGHRAHV DGGQRGPGGQ QEPDWHRAGA
TIPRLPSPSG SPWRREQEPA PGEPPHIPAY GNRPGGQEIR PRVPGLDREA RPAVPPTHSP
SYRIRLAGSE PSLVQAAPGQ AVQLFCPGNI PSEFQAGWQK EGRPISSNRY QLQADGSLII
SRLRPEDAGI YSCGSHRPGH EPQEIQLRVT GGDMAVFPEG QPRHFPEPRN PDLGHGPPHR
GTGAEAGGHR VLSPSHPRPA TRLRLDRTQP GVVDASPGQR IRLTCRAEGF PVPTIEWQRD
GQLVSSPRHQ VQPDGSLVIS RVDVEDGGYY SCVAFNGQDR DQRWVQLRVL RELTITGLPP
AVTVAEGDTA RLLCVVAGES VNIRWSRNGL PIQADGHRVH QSPDGTLLIH NLRPRDEGSY
TCSAFRGSQA VSRSTEVKVA LPAPAAQSRD LGKDCIDQPE LANCALILQA QLCGNEYYSS
FCCASCSRFQ PNAQPVWQQG
