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Protein

Papilin

Gene

Ppn

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential extracellular matrix (ECM) protein that influences cell rearrangements. May act by modulating metalloproteinases action during organogenesis. Able to non-competitively inhibit procollagen N-proteinase, an ADAMTS metalloproteinase.1 Publication

GO - Molecular functioni

GO - Biological processi

  • extracellular matrix organization Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Protease inhibitor, Serine protease inhibitor

Protein family/group databases

MEROPSiI02.955.

Names & Taxonomyi

Protein namesi
Recommended name:
Papilin
Gene namesi
Name:Ppn
ORF Names:CG33103
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003137. Ppn.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: UniProtKB
  • proteinaceous extracellular matrix Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 28982872PapilinPRO_0000248544Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi69 ↔ 105By similarity
Disulfide bondi73 ↔ 110By similarity
Disulfide bondi84 ↔ 95By similarity
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence analysis
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence analysis
Glycosylationi419 – 4191N-linked (GlcNAc...)Sequence analysis
Disulfide bondi462 ↔ 504By similarity
Disulfide bondi473 ↔ 515By similarity
Disulfide bondi477 ↔ 520By similarity
Glycosylationi669 – 6691N-linked (GlcNAc...)1 Publication
Glycosylationi889 – 8891N-linked (GlcNAc...)Sequence analysis
Glycosylationi914 – 9141N-linked (GlcNAc...)Sequence analysis
Glycosylationi917 – 9171N-linked (GlcNAc...)Sequence analysis
Glycosylationi950 – 9501N-linked (GlcNAc...)Sequence analysis
Glycosylationi1064 – 10641N-linked (GlcNAc...)Sequence analysis
Glycosylationi1489 – 14891N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1612 ↔ 1662By similarity
Disulfide bondi1621 ↔ 1645By similarity
Glycosylationi1623 – 16231N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1637 ↔ 1658By similarity
Disulfide bondi1671 ↔ 1721By similarity
Disulfide bondi1680 ↔ 1704By similarity
Disulfide bondi1696 ↔ 1717By similarity
Disulfide bondi1730 ↔ 1780By similarity
Disulfide bondi1739 ↔ 1763By similarity
Glycosylationi1750 – 17501N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1755 ↔ 1776By similarity
Disulfide bondi1790 ↔ 1840By similarity
Disulfide bondi1799 ↔ 1823By similarity
Disulfide bondi1815 ↔ 1836By similarity
Disulfide bondi1849 ↔ 1899By similarity
Disulfide bondi1858 ↔ 1882By similarity
Disulfide bondi1874 ↔ 1895By similarity
Disulfide bondi1922 ↔ 1972By similarity
Disulfide bondi1931 ↔ 1955By similarity
Disulfide bondi1947 ↔ 1968By similarity
Disulfide bondi2001 ↔ 2051By similarity
Disulfide bondi2010 ↔ 2034By similarity
Glycosylationi2020 – 20201N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2026 ↔ 2047By similarity
Disulfide bondi2071 ↔ 2121By similarity
Disulfide bondi2080 ↔ 2104By similarity
Glycosylationi2083 – 20831N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2096 ↔ 2117By similarity
Disulfide bondi2128 ↔ 2178By similarity
Disulfide bondi2137 ↔ 2161By similarity
Disulfide bondi2153 ↔ 2174By similarity
Disulfide bondi2194 ↔ 2244By similarity
Disulfide bondi2203 ↔ 2227By similarity
Glycosylationi2205 – 22051N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2219 ↔ 2240By similarity
Disulfide bondi2253 ↔ 2303By similarity
Disulfide bondi2262 ↔ 2286By similarity
Disulfide bondi2278 ↔ 2299By similarity
Disulfide bondi2318 ↔ 2371By similarity
Disulfide bondi2327 ↔ 2354By similarity
Disulfide bondi2346 ↔ 2367By similarity
Glycosylationi2465 – 24651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2543 ↔ 2592By similarity
Glycosylationi2552 – 25521N-linked (GlcNAc...)Sequence analysis
Glycosylationi2625 – 26251N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2640 ↔ 2687By similarity
Disulfide bondi2775 ↔ 2824By similarity
Glycosylationi2784 – 27841N-linked (GlcNAc...)Sequence analysis
Glycosylationi2838 – 28381N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.2 Publications
Sulfated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan, Sulfation

Proteomic databases

PaxDbiQ868Z9.
PRIDEiQ868Z9.

Expressioni

Tissue specificityi

During embryogenesis it first appears in the extracellular matrix during gastrulation and early mesoderm development at sites where basement membranes do not subsequently form. Later, migrating hemocytes prominently produce it together with other ECM components, in basement membranes that underlie epithelia and envelop muscles and emerging organs. At various life stages, it can be synthesized by other cells, such as those of the fat body, and it also occurs in a few, circumscribed regions of relatively amorphous ECM. Isoform E is specifically expressed in ECM of heart and proventriculus. Isoform C is a major component of transitory ECM deposit in the early embryo. Isoform F is a major component of the basement membrane during embryogenesis.2 Publications

Developmental stagei

Expressed throughout development and is prominent in adult basement membranes. Appears after 4 hours of embryogenesis, peaks at 8-12 hours and remains thereafter.1 Publication

Gene expression databases

BgeeiQ868Z9.
ExpressionAtlasiQ868Z9. differential.
GenevisibleiQ868Z9. DM.

Interactioni

Subunit structurei

Homooligomer; disulfide-linked.1 Publication

Protein-protein interaction databases

BioGridi68683. 26 interactions.
IntActiQ868Z9. 4 interactions.
MINTiMINT-330923.
STRINGi7227.FBpp0291051.

Structurei

3D structure databases

ProteinModelPortaliQ868Z9.
SMRiQ868Z9. Positions 60-271, 733-1226, 1611-1899, 1921-2372, 2510-2842.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 11155TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini338 – 39760TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini461 – 52161TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini522 – 57554TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini576 – 63358TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini639 – 69456TSP type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini1612 – 166251BPTI/Kunitz inhibitor 1PROSITE-ProRule annotationAdd
BLAST
Domaini1671 – 172151BPTI/Kunitz inhibitor 2PROSITE-ProRule annotationAdd
BLAST
Domaini1730 – 178051BPTI/Kunitz inhibitor 3PROSITE-ProRule annotationAdd
BLAST
Domaini1790 – 184051BPTI/Kunitz inhibitor 4PROSITE-ProRule annotationAdd
BLAST
Domaini1849 – 189951BPTI/Kunitz inhibitor 5PROSITE-ProRule annotationAdd
BLAST
Domaini1922 – 197251BPTI/Kunitz inhibitor 6PROSITE-ProRule annotationAdd
BLAST
Domaini2001 – 205151BPTI/Kunitz inhibitor 7PROSITE-ProRule annotationAdd
BLAST
Domaini2071 – 212151BPTI/Kunitz inhibitor 8PROSITE-ProRule annotationAdd
BLAST
Domaini2128 – 217851BPTI/Kunitz inhibitor 9PROSITE-ProRule annotationAdd
BLAST
Domaini2194 – 224451BPTI/Kunitz inhibitor 10PROSITE-ProRule annotationAdd
BLAST
Domaini2253 – 230351BPTI/Kunitz inhibitor 11PROSITE-ProRule annotationAdd
BLAST
Domaini2318 – 237154BPTI/Kunitz inhibitor 12PROSITE-ProRule annotationAdd
BLAST
Domaini2452 – 249847WAPPROSITE-ProRule annotationAdd
BLAST
Domaini2523 – 260785Ig-like C2-type 1Add
BLAST
Domaini2617 – 269781Ig-like C2-type 2Add
BLAST
Domaini2749 – 284092Ig-like C2-type 3Add
BLAST
Domaini2847 – 288640PLACPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi776 – 1232457Ser-richAdd
BLAST
Compositional biasi1403 – 1586184Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the papilin family.Curated
Contains 12 BPTI/Kunitz inhibitor domains.PROSITE-ProRule annotation
Contains 1 PLAC domain.PROSITE-ProRule annotation
Contains 6 TSP type-1 domains.PROSITE-ProRule annotation
Contains 1 WAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG4295. Eukaryota.
KOG4475. Eukaryota.
KOG4597. Eukaryota.
ENOG410XQNP. LUCA.
GeneTreeiENSGT00760000118885.
InParanoidiQ868Z9.
OMAiEGCACET.
OrthoDBiEOG73FQKT.
PhylomeDBiQ868Z9.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
4.10.410.10. 12 hits.
InterProiIPR010294. ADAM_spacer1.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR002223. Kunitz_BPTI.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR010909. PLAC.
IPR020901. Prtase_inh_Kunz-CS.
IPR000884. TSP1_rpt.
IPR008197. WAP_dom.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF07679. I-set. 1 hit.
PF00014. Kunitz_BPTI. 12 hits.
PF08686. PLAC. 1 hit.
PF00090. TSP_1. 6 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
PR00759. BASICPTASE.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00131. KU. 12 hits.
SM00209. TSP1. 7 hits.
SM00217. WAP. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF57256. SSF57256. 1 hit.
SSF57362. SSF57362. 12 hits.
SSF82895. SSF82895. 7 hits.
PROSITEiPS00280. BPTI_KUNITZ_1. 11 hits.
PS50279. BPTI_KUNITZ_2. 12 hits.
PS50835. IG_LIKE. 3 hits.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
PS51390. WAP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform E (identifier: Q868Z9-1) [UniParc]FASTAAdd to basket

Also known as: Papilin-3

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDLSRRLCST ALVAFIVLAS IHDSQSRFPG LRQKRQYGAN MYLPESSVTP
60 70 80 90 100
GGEGNDPDEW TPWSSPSDCS RTCGGGVSYQ TRECLRRDDR GEAVCSGGSR
110 120 130 140 150
RYFSCNTQDC PEEESDFRAQ QCSRFDRQQF DGVFYEWVPY TNAPNPCELN
160 170 180 190 200
CMPKGERFYY RQREKVVDGT RCNDKDLDVC VNGECMPVGC DMMLGSDAKE
210 220 230 240 250
DKCRKCGGDG STCKTIRNTI TTKDLAPGYN DLLLLPEGAT NIRIEETVPS
260 270 280 290 300
SNYLACRNHS GHYYLNGDWR IDFPRPMFFA NSWWNYQRKP MGFAAPDQLT
310 320 330 340 350
CSGPISESLF IVMLVQEKNI SLDYEYSIPE SLSHSQQDTH TWTHHQFNAC
360 370 380 390 400
SASCGGGSQS RKVTCNNRIT LAEVNPSLCD QKSKPVEEQA CGTEPCAPHW
410 420 430 440 450
VEGEWSKCSK GCGSDGFQNR SITCERISSS GEHTVEEDAV CLKEVGNKPA
460 470 480 490 500
TKQECNRDVK NCPKYHLGPW TPCDKLCGDG KQTRKVTCFI EENGHKRVLP
510 520 530 540 550
EEDCVEEKPE TEKSCLLTPC EGVDWIISQW SGCNACGQNT ETRTAICGNK
560 570 580 590 600
EGKVYPEEFC EPEVPTLSRP CKSPKCEAQW FSSEWSKCSA PCGKGVKSRI
610 620 630 640 650
VICGEFDGKT VTPADDDSKC NKETKPESEQ DCEGEEKVCP GEWFTGPWGK
660 670 680 690 700
CSKPCGGGER VREVLCLSNG TKSVNCDEEK VEPLSEKCNS EACTEDEILP
710 720 730 740 750
LTSTDKPIED DEEDCDEDGI ELISDGLSDD EKSEDVIDLE GTAKTETTPE
760 770 780 790 800
AEDLMQSDSP TPYDEFESTG TTFEGSGYDS ESTTDSGIST EGSGDDEETS
810 820 830 840 850
EASTDLSSST DSGSTSSDST SSDSSSSISS DATSEAPASS VSDSSDSTDA
860 870 880 890 900
STETTGVSDD STDVSSSTEA SASESTDVSG ASDSTGSTNA SDSTPESSTE
910 920 930 940 950
ASSSTDDSTD SSDNSSNVSE SSTEASSSSV SDSNDSSDGS TDGVSSTTEN
960 970 980 990 1000
SSDSTSDATS DSTASSDSTD STSDQTTETT PESSTDSTES STLDASSTTD
1010 1020 1030 1040 1050
ASSTSESSSE SSTDGSSTTS NSASSETTGL SSDGSTTDAT TAASDNTDIT
1060 1070 1080 1090 1100
TDGSTDESTD GSSNASTEGS TEGASEDTTI STESSGSTES TDAIASDGST
1110 1120 1130 1140 1150
TEGSTVEDLS SSTSSDVTSD STITDSSPST EVSGSTDSSS STDGSSTDAS
1160 1170 1180 1190 1200
STEASSTDVT ESTDSTVSGG TSDTTESGPT EESTTEGSTE STTEGSTDST
1210 1220 1230 1240 1250
QSTDLDSTTS DIWSTSDKDD ESESSTPYSF DSEVTKSKPR KCKPKKSTCA
1260 1270 1280 1290 1300
KSEYGCCPDG KSTPKGPFDE GCPIAKTCAD TKYGCCLDGV SPAKGKNNKG
1310 1320 1330 1340 1350
CPKSQCAETL FGCCPDKFTA ADGENDEGCP ETTTVPPTTT TEETQPETTT
1360 1370 1380 1390 1400
EIEGSGQDST TSEPDTKKSC SFSEFGCCPD AETSAKGPDF EGCGLASPVA
1410 1420 1430 1440 1450
KGCAESENGC CPDGQTPASG PNGEGCSGCT RERFGCCPDS QTPAHGPNKE
1460 1470 1480 1490 1500
GCCLDTQFGC CPDNILAARG PNNEGCECHY TPYGCCPDNK SAATGYNQEG
1510 1520 1530 1540 1550
CACETTQYGC CPDKITAAKG PKHEGCPCET TQFGCCPDGL TFAKGPHHHG
1560 1570 1580 1590 1600
CHCTQTEFKC CDDEKTPAKG PNGDGCTCVE SKFGCCPDGV TKATDEKFGG
1610 1620 1630 1640 1650
CENVQEPPQK ACGLPKETGT CNNYSVKYYF DTSYGGCARF WYGGCDGNDN
1660 1670 1680 1690 1700
RFESEAECKD TCQDYTGKHV CLLPKSAGPC TGFTKKWYFD VDRNRCEEFQ
1710 1720 1730 1740 1750
YGGCYGTNNR FDSLEQCQGT CAASENLPTC EQPVESGPCA GNFERWYYDN
1760 1770 1780 1790 1800
ETDICRPFTY GGCKGNKNNY PTEHACNYNC RQPGVLKDRC ALPKQTGDCS
1810 1820 1830 1840 1850
EKLAKWHFSE SEKRCVPFYY SGCGGNKNNF PTLESCEDHC PRQVAKDICE
1860 1870 1880 1890 1900
IPAEVGECAN YVTSWYYDTQ DQACRQFYYG GCGGNENRFP TEESCLARCD
1910 1920 1930 1940 1950
RKPEPTTTTP ATRPQPSRQD VCDEEPAPGE CSTWVLKWHF DRKIGACRQF
1960 1970 1980 1990 2000
YYGNCGGNGN RFETENDCQQ RCLSQEPPAP TPPRAPAPTR QPDPAPTVAQ
2010 2020 2030 2040 2050
CSQPADPGQC DKWALHWNYN ETEGRCQSFY YGGCGGNDNR FATEEECSAR
2060 2070 2080 2090 2100
CSVNIDIRIG ADPVEHDTSK CFLAFEPGNC YNNVTRWFYN SAEGLCDEFV
2110 2120 2130 2140 2150
YTGCGGNANN YATEEECQNE CNDAQTTCAL PPVRGRCSDL SRRWYFDERS
2160 2170 2180 2190 2200
GECHEFEFTG CRGNRNNFVS QSDCLNFCIG EPVVEPSAPT YSVCAEPPEA
2210 2220 2230 2240 2250
GECDNRTTAW FYDSENMACT AFTYTGCGGN GNRFETRDQC ERQCGEFKGV
2260 2270 2280 2290 2300
DVCNEPVTTG PCTDWQTKYY FNTASQACEP FTYGGCDGTG NRFSDLFECQ
2310 2320 2330 2340 2350
TVCLAGREPR VGSAKEICLL PVATGRCNGP SVHERRWYYD DEAGNCVSFI
2360 2370 2380 2390 2400
YAGCSGNQNN FRSFEACTNQ CRPEPNKQDN EIGQNPCDTF DAECQELRCP
2410 2420 2430 2440 2450
YGVRRVAARS QPECTQCICE NPCEGYSCPE GQQCAIDVAS SDDRQFAPVC
2460 2470 2480 2490 2500
RDIYKPGECP ALSANASGCA RECYTDADCR GDNKCCSDGC GQLCVHPARP
2510 2520 2530 2540 2550
TQPPRTQAPV VSYPGDARAA LEPKEAHELD VQTAIGGIAV LRCFATGNPA
2560 2570 2580 2590 2600
PNITWSLKNL VINTNKGRYV LTANGDLTIV QVRQTDDGTY VCVASNGLGE
2610 2620 2630 2640 2650
PVRREVALQV TEPVSQPAYI YGDKNVTQIV ELNRPAVIRC PAGGFPEPHV
2660 2670 2680 2690 2700
SWWRNGQMFG LKNNLMARDY SLVFNSIQLS DLGLYTCEVY NQRRPVSLRV
2710 2720 2730 2740 2750
TLKAVGPVRP LSPEEEQYMQ YVLNPATRPV TQRPSYPYRP TRPAYVPEPT
2760 2770 2780 2790 2800
VNVHAVLALE PKNSYTPGST IVMSCSVQGY PEPNVTWIKD DVPLYNNERV
2810 2820 2830 2840 2850
QITYQPHRLV LSDVTSADSG KYTCRASNAY TYANGEANVS IQSVVPVSPE
2860 2870 2880 2890
CVDNPYFANC KLIVKGRYCS NPYYTQFCCR SCTLAGQVAS PPLHPNAV
Length:2,898
Mass (Da):313,035
Last modified:September 5, 2006 - v2
Checksum:i5FFF75A4155D49A4
GO
Isoform F (identifier: Q868Z9-2) [UniParc]FASTAAdd to basket

Also known as: Papilin-2

The sequence of this isoform differs from the canonical sequence as follows:
     2251-2373: DVCNEPVTTG...FEACTNQCRP → A

Show »
Length:2,776
Mass (Da):299,526
Checksum:i51E2F29A2D87748C
GO
Isoform C (identifier: Q868Z9-5) [UniParc]FASTAAdd to basket

Also known as: Papilin-1

The sequence of this isoform differs from the canonical sequence as follows:
     1788-2372: Missing.
     2373-2373: P → A
     2612-2750: Missing.

Show »
Length:2,174
Mass (Da):231,767
Checksum:i5FCA6DB89FDED450
GO
Isoform G (identifier: Q868Z9-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1788-1844: Missing.

Note: No experimental confirmation available.
Show »
Length:2,841
Mass (Da):306,554
Checksum:i36F93848BD7641E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti224 – 2241D → N in AAG37995 (PubMed:11076767).Curated
Sequence conflicti224 – 2241D → N in AAO84907 (PubMed:12666201).Curated
Sequence conflicti224 – 2241D → N in AAO84908 (PubMed:12666201).Curated
Sequence conflicti360 – 3601S → N in AAG37995 (PubMed:11076767).Curated
Sequence conflicti360 – 3601S → N in AAO84907 (PubMed:12666201).Curated
Sequence conflicti360 – 3601S → N in AAO84908 (PubMed:12666201).Curated
Sequence conflicti852 – 8521T → P in AAG37995 (PubMed:11076767).Curated
Sequence conflicti852 – 8521T → P in AAO84907 (PubMed:12666201).Curated
Sequence conflicti852 – 8521T → P in AAO84908 (PubMed:12666201).Curated
Sequence conflicti934 – 9341N → S in AAG37995 (PubMed:11076767).Curated
Sequence conflicti934 – 9341N → S in AAO84907 (PubMed:12666201).Curated
Sequence conflicti934 – 9341N → S in AAO84908 (PubMed:12666201).Curated
Sequence conflicti1029 – 10291G → W in AAG37995 (PubMed:11076767).Curated
Sequence conflicti1029 – 10291G → W in AAO84907 (PubMed:12666201).Curated
Sequence conflicti1029 – 10291G → W in AAO84908 (PubMed:12666201).Curated
Sequence conflicti1344 – 13441T → S in AAG37995 (PubMed:11076767).Curated
Sequence conflicti1344 – 13441T → S in AAO84907 (PubMed:12666201).Curated
Sequence conflicti1344 – 13441T → S in AAO84908 (PubMed:12666201).Curated
Sequence conflicti1484 – 14841G → S in AAG37995 (PubMed:11076767).Curated
Sequence conflicti1484 – 14841G → S in AAO84907 (PubMed:12666201).Curated
Sequence conflicti1484 – 14841G → S in AAO84908 (PubMed:12666201).Curated
Sequence conflicti1574 – 15741D → E in AAG37995 (PubMed:11076767).Curated
Sequence conflicti1574 – 15741D → E in AAO84907 (PubMed:12666201).Curated
Sequence conflicti1574 – 15741D → E in AAO84908 (PubMed:12666201).Curated
Sequence conflicti2566 – 25661K → R in AAG37995 (PubMed:11076767).Curated
Sequence conflicti2764 – 27641S → R in AAO84907 (PubMed:12666201).Curated
Sequence conflicti2764 – 27641S → R in AAO84908 (PubMed:12666201).Curated
Sequence conflicti2788 – 27881I → T in AAG37995 (PubMed:11076767).Curated
Sequence conflicti2811 – 28111L → V in AAO84907 (PubMed:12666201).Curated
Sequence conflicti2811 – 28111L → V in AAO84908 (PubMed:12666201).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1788 – 2372585Missing in isoform C. 1 PublicationVSP_041751Add
BLAST
Alternative sequencei1788 – 184457Missing in isoform G. CuratedVSP_041750Add
BLAST
Alternative sequencei2251 – 2373123DVCNE…NQCRP → A in isoform F. 2 PublicationsVSP_020304Add
BLAST
Alternative sequencei2373 – 23731P → A in isoform C. 1 PublicationVSP_041752
Alternative sequencei2612 – 2750139Missing in isoform C. 1 PublicationVSP_041753Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF205357 mRNA. Translation: AAG37995.1.
AF529179 mRNA. Translation: AAO84907.1.
AF529180 mRNA. Translation: AAO84908.1.
AE014297 Genomic DNA. Translation: AAF56794.4.
AE014297 Genomic DNA. Translation: AAF56795.4.
AE014297 Genomic DNA. Translation: ACZ95054.1.
AE014297 Genomic DNA. Translation: ACZ95055.1.
BT011127 mRNA. Translation: AAR82794.1.
RefSeqiNP_001163760.1. NM_001170289.2. [Q868Z9-5]
NP_001163761.1. NM_001170290.2. [Q868Z9-6]
NP_788751.2. NM_176574.3. [Q868Z9-2]
NP_788752.2. NM_176575.3. [Q868Z9-1]
UniGeneiDm.7007.

Genome annotation databases

EnsemblMetazoaiFBtr0301837; FBpp0291051; FBgn0003137. [Q868Z9-1]
GeneIDi43872.
KEGGidme:Dmel_CG33103.
UCSCiCG33103-RA. d. melanogaster. [Q868Z9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF205357 mRNA. Translation: AAG37995.1.
AF529179 mRNA. Translation: AAO84907.1.
AF529180 mRNA. Translation: AAO84908.1.
AE014297 Genomic DNA. Translation: AAF56794.4.
AE014297 Genomic DNA. Translation: AAF56795.4.
AE014297 Genomic DNA. Translation: ACZ95054.1.
AE014297 Genomic DNA. Translation: ACZ95055.1.
BT011127 mRNA. Translation: AAR82794.1.
RefSeqiNP_001163760.1. NM_001170289.2. [Q868Z9-5]
NP_001163761.1. NM_001170290.2. [Q868Z9-6]
NP_788751.2. NM_176574.3. [Q868Z9-2]
NP_788752.2. NM_176575.3. [Q868Z9-1]
UniGeneiDm.7007.

3D structure databases

ProteinModelPortaliQ868Z9.
SMRiQ868Z9. Positions 60-271, 733-1226, 1611-1899, 1921-2372, 2510-2842.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68683. 26 interactions.
IntActiQ868Z9. 4 interactions.
MINTiMINT-330923.
STRINGi7227.FBpp0291051.

Protein family/group databases

MEROPSiI02.955.

Proteomic databases

PaxDbiQ868Z9.
PRIDEiQ868Z9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0301837; FBpp0291051; FBgn0003137. [Q868Z9-1]
GeneIDi43872.
KEGGidme:Dmel_CG33103.
UCSCiCG33103-RA. d. melanogaster. [Q868Z9-1]

Organism-specific databases

CTDi43872.
FlyBaseiFBgn0003137. Ppn.

Phylogenomic databases

eggNOGiKOG4295. Eukaryota.
KOG4475. Eukaryota.
KOG4597. Eukaryota.
ENOG410XQNP. LUCA.
GeneTreeiENSGT00760000118885.
InParanoidiQ868Z9.
OMAiEGCACET.
OrthoDBiEOG73FQKT.
PhylomeDBiQ868Z9.

Miscellaneous databases

GenomeRNAii43872.
PROiQ868Z9.

Gene expression databases

BgeeiQ868Z9.
ExpressionAtlasiQ868Z9. differential.
GenevisibleiQ868Z9. DM.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
4.10.410.10. 12 hits.
InterProiIPR010294. ADAM_spacer1.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR002223. Kunitz_BPTI.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR010909. PLAC.
IPR020901. Prtase_inh_Kunz-CS.
IPR000884. TSP1_rpt.
IPR008197. WAP_dom.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF07679. I-set. 1 hit.
PF00014. Kunitz_BPTI. 12 hits.
PF08686. PLAC. 1 hit.
PF00090. TSP_1. 6 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
PR00759. BASICPTASE.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00131. KU. 12 hits.
SM00209. TSP1. 7 hits.
SM00217. WAP. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF57256. SSF57256. 1 hit.
SSF57362. SSF57362. 12 hits.
SSF82895. SSF82895. 7 hits.
PROSITEiPS00280. BPTI_KUNITZ_1. 11 hits.
PS50279. BPTI_KUNITZ_2. 12 hits.
PS50835. IG_LIKE. 3 hits.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 5 hits.
PS51390. WAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases."
    Kramerova I.A., Kawaguchi N., Fessler L.I., Nelson R.E., Chen Y., Kramerov A.A., Kusche-Gullberg M., Kramer J.M., Ackley B.D., Sieron A.L., Prockop D.J., Fessler J.H.
    Development 127:5475-5485(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), PROTEIN SEQUENCE OF 27-39; 224-244; 554-572; 696-700 AND 2410-2443, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "Alternative splicing of papilin and the diversity of Drosophila extracellular matrix during embryonic morphogenesis."
    Kramerova I.A., Kramerov A.A., Fessler J.H.
    Dev. Dyn. 226:634-642(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS E AND F), TISSUE SPECIFICITY.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2186-2898 (ISOFORM F).
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Papilin: a Drosophila proteoglycan-like sulfated glycoprotein from basement membranes."
    Campbell A.G., Fessler L.I., Salo T., Fessler J.H.
    J. Biol. Chem. 262:17605-17612(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT, SULFATION, GLYCOSYLATION.
  7. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
    Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
    Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-669, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Oregon-R.
    Tissue: Head.

Entry informationi

Entry nameiPPN_DROME
AccessioniPrimary (citable) accession number: Q868Z9
Secondary accession number(s): E1JJ05
, E1JJ06, Q6NP04, Q7KRX2, Q869A0, Q9GQR0, Q9VAV3, Q9VAV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: June 8, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.