ID H0WDR9_CAVPO Unreviewed; 1282 AA.
AC H0WDR9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Papilin, proteoglycan like sulfated glycoprotein {ECO:0000313|Ensembl:ENSCPOP00000021142.2};
GN Name=PAPLN {ECO:0000313|Ensembl:ENSCPOP00000021142.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000021142.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000021142.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000021142.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AAKN02025307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003472447.2; XM_003472399.3.
DR MEROPS; I02.972; -.
DR Ensembl; ENSCPOT00000024277.2; ENSCPOP00000021142.2; ENSCPOG00000019279.2.
DR GeneID; 100728435; -.
DR KEGG; cpoc:100728435; -.
DR CTD; 89932; -.
DR VEuPathDB; HostDB:ENSCPOG00000019279; -.
DR eggNOG; KOG3510; Eukaryota.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000156891; -.
DR HOGENOM; CLU_000660_7_0_1; -.
DR OrthoDB; 2910701at2759; -.
DR TreeFam; TF316874; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000019279; Expressed in adult mammalian kidney and 8 other cell types or tissues.
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; 2.
DR Pfam; PF13927; Ig_3; 1.
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; 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; 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; 5.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1282
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011579505"
FT DOMAIN 751..801
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 900..992
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1041..1128
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1135..1220
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1233..1272
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 556..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 50..86
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 54..91
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 65..76
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1282 AA; 138150 MW; 66F4F379C5F44987 CRC64;
MGAGFPTRAQ AEMQLILLVP LLLALQPGSS APEARQQSDT WGPWGDWSSC SRTCGGGISF
RERTCYSQRR DGGTSCVGPA RSYRTCRTES CPDGARDFRA EQCAELDGAS FHGRQYRWLP
YYGAPNKCEL NCIPKGENFY YKHREAVLDG TPCEPGGRDV CVDGRCRVVG CDHELDSPKQ
EDKCLQCGGD GTSCYPVTGT FDANDLSRGY NQIFIIPPGA TSIHIEEAAA SRNFLAVRSV
RGEYYLNGHW TIAEAKALPV ANTILHYERG AEGDLAPERL QARGPTSEPL IIELISQEAN
PGVHYEYYLP LHGPRSSQGF SWSHTSWGDC SVECGGGHQS RLVFCTSDSE AYPSHMCQRQ
PRPADSRPCN PHPCPQTKRW KVGPWTPCSA SCGGGSQSRS VYCVSSDGSG GQEAAEEAEC
AGLPRKPPST QACNLHRCAA WSAGPWGECS VTCGAGSGRQ ALGACDALFP LSPSACSLED
RPPFMETCVQ AACPLHSDQA WRVSAWGLCS KSCSSGTRRR QVVCAIGPPS HCKNLQQSKP
RDVELCNTQP CHLPQEVPSV QDPDVHPRRP WMPSDPREAL ASDSRDQRPW VPNRPGRFHN
SPPSTRGPNP SLRQPPRSGS GAQDCRHSPY GCCPDGRMAS PGPQGQGCPR TEAWCQQSRY
GCCPDGVSAA KGPQQAGCTR PYGSGDAGRR PGSKVVPSAA PKAHRPQPQQ NEPAECRGSQ
FGCCYDNVAS AAGPLGEGCA GQPSSAYPVR CLLPSAHGSC TDWAPRWYFI ASVGRCNRFW
YGGCHGNANN FASEQECMSS CQGAQRGPHH PEPGATGLDT HTDGCSSGPR GRQESNRHRT
EDAGPRLTSS SGGLWRREQE PVPGEAHPTR AFGERPRGQE AGPRTPGLGR DARWPMPPSP
SSSYRISLAG SEPVLVQGAL GQSMQLFCSK DASLDPQVEW HKDGQPISSD RHQLQPDGSL
VISPLWAEDA GIYSCGGNRL GHDSQKIQLR VAGSDFSEPS EAEPRHFPWT RDPAQGHGPR
DSTLGGDAGG PGAVPSPQPQ PATRLRLDRT QPGVVDASPG QRIRLPCRAD GFPPPVIEWQ
RDGQPLSSPR HQTQPDGSLV ISRVGVEDGG FYACVAFNGQ HRDQRWVQLR VLGELTITGL
PPTVTVPEGD TARLPCVVGD ESVNIRWSRN GLPVQADGRR VYQSPDGTLL IHNLQARDEG
SYTCSAYRGS QAVSRSTEVK VATPAAVAQP REPSGECIDQ PELANCGLIL QAQLCGNEYY
ASFCCASCSR FQPHPQPAQQ QG
//