PPN_DROME
ID PPN_DROME Reviewed; 2898 AA.
AC Q868Z9; E1JJ05; E1JJ06; Q6NP04; Q7KRX2; Q869A0; Q9GQR0; Q9VAV3; Q9VAV4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Papilin;
DE Flags: Precursor;
GN Name=Ppn; ORFNames=CG33103;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), PROTEIN SEQUENCE OF 27-39; 224-244;
RP 554-572; 696-700 AND 2410-2443, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [MRNA] (ISOFORMS E AND F), AND TISSUE SPECIFICITY.
RX PubMed=12666201; DOI=10.1002/dvdy.10265;
RA Kramerova I.A., Kramerov A.A., Fessler J.H.;
RT "Alternative splicing of papilin and the diversity of Drosophila
RT extracellular matrix during embryonic morphogenesis.";
RL Dev. Dyn. 226:634-642(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2186-2898 (ISOFORM F).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, SUBUNIT, SULFATION, AND GLYCOSYLATION.
RX PubMed=3320045; DOI=10.1016/s0021-9258(18)45424-5;
RA Campbell A.G., Fessler L.I., Salo T., Fessler J.H.;
RT "Papilin: a Drosophila proteoglycan-like sulfated glycoprotein from
RT basement membranes.";
RL J. Biol. Chem. 262:17605-17612(1987).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-669, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
CC -!- FUNCTION: Essential extracellular matrix (ECM) protein that influences
CC cell rearrangements. May act by modulating metalloproteinases action
CC during organogenesis. Able to non-competitively inhibit procollagen N-
CC proteinase, an ADAMTS metalloproteinase. {ECO:0000269|PubMed:11076767}.
CC -!- SUBUNIT: Homooligomer; disulfide-linked. {ECO:0000269|PubMed:3320045}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:11076767,
CC ECO:0000269|PubMed:3320045}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=E; Synonyms=Papilin-3;
CC IsoId=Q868Z9-1; Sequence=Displayed;
CC Name=F; Synonyms=Papilin-2;
CC IsoId=Q868Z9-2; Sequence=VSP_020304;
CC Name=C; Synonyms=Papilin-1;
CC IsoId=Q868Z9-5; Sequence=VSP_041751, VSP_041752, VSP_041753;
CC Name=G;
CC IsoId=Q868Z9-6; Sequence=VSP_041750;
CC -!- TISSUE SPECIFICITY: During embryogenesis it first appears in the
CC extracellular matrix during gastrulation and early mesoderm development
CC at sites where basement membranes do not subsequently form. Later,
CC migrating hemocytes prominently produce it together with other ECM
CC components, in basement membranes that underlie epithelia and envelop
CC muscles and emerging organs. At various life stages, it can be
CC synthesized by other cells, such as those of the fat body, and it also
CC occurs in a few, circumscribed regions of relatively amorphous ECM.
CC Isoform E is specifically expressed in ECM of heart and proventriculus.
CC Isoform C is a major component of transitory ECM deposit in the early
CC embryo. Isoform F is a major component of the basement membrane during
CC embryogenesis. {ECO:0000269|PubMed:11076767,
CC ECO:0000269|PubMed:12666201}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development and is prominent
CC in adult basement membranes. Appears after 4 hours of embryogenesis,
CC peaks at 8-12 hours and remains thereafter.
CC {ECO:0000269|PubMed:11076767}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17893096,
CC ECO:0000269|PubMed:3320045}.
CC -!- PTM: Sulfated. {ECO:0000269|PubMed:3320045}.
CC -!- SIMILARITY: Belongs to the papilin family. {ECO:0000305}.
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DR EMBL; AF205357; AAG37995.1; -; mRNA.
DR EMBL; AF529179; AAO84907.1; -; mRNA.
DR EMBL; AF529180; AAO84908.1; -; mRNA.
DR EMBL; AE014297; AAF56794.4; -; Genomic_DNA.
DR EMBL; AE014297; AAF56795.4; -; Genomic_DNA.
DR EMBL; AE014297; ACZ95054.1; -; Genomic_DNA.
DR EMBL; AE014297; ACZ95055.1; -; Genomic_DNA.
DR EMBL; BT011127; AAR82794.1; -; mRNA.
DR RefSeq; NP_001163760.1; NM_001170289.2. [Q868Z9-5]
DR RefSeq; NP_001163761.1; NM_001170290.2. [Q868Z9-6]
DR RefSeq; NP_788751.2; NM_176574.3. [Q868Z9-2]
DR RefSeq; NP_788752.2; NM_176575.3. [Q868Z9-1]
DR SMR; Q868Z9; -.
DR BioGRID; 68683; 26.
DR IntAct; Q868Z9; 4.
DR STRING; 7227.FBpp0291051; -.
DR MEROPS; I02.955; -.
DR MEROPS; I02.964; -.
DR MEROPS; I02.968; -.
DR MEROPS; I02.978; -.
DR GlyGen; Q868Z9; 20 sites.
DR iPTMnet; Q868Z9; -.
DR PaxDb; Q868Z9; -.
DR PRIDE; Q868Z9; -.
DR EnsemblMetazoa; FBtr0300337; FBpp0289566; FBgn0003137. [Q868Z9-5]
DR EnsemblMetazoa; FBtr0301837; FBpp0291051; FBgn0003137. [Q868Z9-1]
DR EnsemblMetazoa; FBtr0301838; FBpp0291052; FBgn0003137. [Q868Z9-2]
DR EnsemblMetazoa; FBtr0301839; FBpp0291053; FBgn0003137. [Q868Z9-6]
DR GeneID; 43872; -.
DR KEGG; dme:Dmel_CG33103; -.
DR UCSC; CG33103-RA; d. melanogaster. [Q868Z9-1]
DR CTD; 43872; -.
DR FlyBase; FBgn0003137; Ppn.
DR VEuPathDB; VectorBase:FBgn0003137; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4295; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000171211; -.
DR InParanoid; Q868Z9; -.
DR OMA; KHGCCPD; -.
DR PhylomeDB; Q868Z9; -.
DR SignaLink; Q868Z9; -.
DR BioGRID-ORCS; 43872; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43872; -.
DR PRO; PR:Q868Z9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003137; Expressed in embryonic/larval hemocyte (Drosophila) and 34 other tissues.
DR ExpressionAtlas; Q868Z9; baseline and differential.
DR Genevisible; Q868Z9; DM.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IMP:UniProtKB.
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; IMP:UniProtKB.
DR CDD; cd00109; KU; 12.
DR Gene3D; 2.20.100.10; -; 5.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 4.10.410.10; -; 12.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR036645; Elafin-like_sf.
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 InterPro; IPR008197; WAP_dom.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00014; Kunitz_BPTI; 12.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF00090; TSP_1; 1.
DR Pfam; PF00095; WAP; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00131; KU; 12.
DR SMART; SM00209; TSP1; 7.
DR SMART; SM00217; WAP; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF57256; SSF57256; 1.
DR SUPFAM; SSF57362; SSF57362; 12.
DR SUPFAM; SSF82895; SSF82895; 7.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 11.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 12.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
DR PROSITE; PS51390; WAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Developmental protein;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Immunoglobulin domain; Protease inhibitor; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal;
KW Sulfation.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:11076767"
FT CHAIN 27..2898
FT /note="Papilin"
FT /id="PRO_0000248544"
FT DOMAIN 57..111
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 338..397
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 461..521
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 522..575
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 576..633
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 639..694
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1612..1662
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1671..1721
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1730..1780
FT /note="BPTI/Kunitz inhibitor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1790..1840
FT /note="BPTI/Kunitz inhibitor 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1849..1899
FT /note="BPTI/Kunitz inhibitor 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1922..1972
FT /note="BPTI/Kunitz inhibitor 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 2001..2051
FT /note="BPTI/Kunitz inhibitor 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 2071..2121
FT /note="BPTI/Kunitz inhibitor 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 2128..2178
FT /note="BPTI/Kunitz inhibitor 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 2194..2244
FT /note="BPTI/Kunitz inhibitor 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 2253..2303
FT /note="BPTI/Kunitz inhibitor 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 2318..2371
FT /note="BPTI/Kunitz inhibitor 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 2452..2498
FT /note="WAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 2523..2607
FT /note="Ig-like C2-type 1"
FT DOMAIN 2617..2697
FT /note="Ig-like C2-type 2"
FT DOMAIN 2749..2840
FT /note="Ig-like C2-type 3"
FT DOMAIN 2847..2886
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 43..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1323..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1902..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1972..2004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..724
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..1212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1976..1993
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 917
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 950
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1064
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1750
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2020
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2838
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..105
FT /evidence="ECO:0000250"
FT DISULFID 73..110
FT /evidence="ECO:0000250"
FT DISULFID 84..95
FT /evidence="ECO:0000250"
FT DISULFID 462..504
FT /evidence="ECO:0000250"
FT DISULFID 473..515
FT /evidence="ECO:0000250"
FT DISULFID 477..520
FT /evidence="ECO:0000250"
FT DISULFID 1612..1662
FT /evidence="ECO:0000250"
FT DISULFID 1621..1645
FT /evidence="ECO:0000250"
FT DISULFID 1637..1658
FT /evidence="ECO:0000250"
FT DISULFID 1671..1721
FT /evidence="ECO:0000250"
FT DISULFID 1680..1704
FT /evidence="ECO:0000250"
FT DISULFID 1696..1717
FT /evidence="ECO:0000250"
FT DISULFID 1730..1780
FT /evidence="ECO:0000250"
FT DISULFID 1739..1763
FT /evidence="ECO:0000250"
FT DISULFID 1755..1776
FT /evidence="ECO:0000250"
FT DISULFID 1790..1840
FT /evidence="ECO:0000250"
FT DISULFID 1799..1823
FT /evidence="ECO:0000250"
FT DISULFID 1815..1836
FT /evidence="ECO:0000250"
FT DISULFID 1849..1899
FT /evidence="ECO:0000250"
FT DISULFID 1858..1882
FT /evidence="ECO:0000250"
FT DISULFID 1874..1895
FT /evidence="ECO:0000250"
FT DISULFID 1922..1972
FT /evidence="ECO:0000250"
FT DISULFID 1931..1955
FT /evidence="ECO:0000250"
FT DISULFID 1947..1968
FT /evidence="ECO:0000250"
FT DISULFID 2001..2051
FT /evidence="ECO:0000250"
FT DISULFID 2010..2034
FT /evidence="ECO:0000250"
FT DISULFID 2026..2047
FT /evidence="ECO:0000250"
FT DISULFID 2071..2121
FT /evidence="ECO:0000250"
FT DISULFID 2080..2104
FT /evidence="ECO:0000250"
FT DISULFID 2096..2117
FT /evidence="ECO:0000250"
FT DISULFID 2128..2178
FT /evidence="ECO:0000250"
FT DISULFID 2137..2161
FT /evidence="ECO:0000250"
FT DISULFID 2153..2174
FT /evidence="ECO:0000250"
FT DISULFID 2194..2244
FT /evidence="ECO:0000250"
FT DISULFID 2203..2227
FT /evidence="ECO:0000250"
FT DISULFID 2219..2240
FT /evidence="ECO:0000250"
FT DISULFID 2253..2303
FT /evidence="ECO:0000250"
FT DISULFID 2262..2286
FT /evidence="ECO:0000250"
FT DISULFID 2278..2299
FT /evidence="ECO:0000250"
FT DISULFID 2318..2371
FT /evidence="ECO:0000250"
FT DISULFID 2327..2354
FT /evidence="ECO:0000250"
FT DISULFID 2346..2367
FT /evidence="ECO:0000250"
FT DISULFID 2543..2592
FT /evidence="ECO:0000250"
FT DISULFID 2640..2687
FT /evidence="ECO:0000250"
FT DISULFID 2775..2824
FT /evidence="ECO:0000250"
FT VAR_SEQ 1788..2372
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:11076767"
FT /id="VSP_041751"
FT VAR_SEQ 1788..1844
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_041750"
FT VAR_SEQ 2251..2373
FT /note="DVCNEPVTTGPCTDWQTKYYFNTASQACEPFTYGGCDGTGNRFSDLFECQTV
FT CLAGREPRVGSAKEICLLPVATGRCNGPSVHERRWYYDDEAGNCVSFIYAGCSGNQNNF
FT RSFEACTNQCRP -> A (in isoform F)"
FT /evidence="ECO:0000303|PubMed:12666201, ECO:0000303|Ref.5"
FT /id="VSP_020304"
FT VAR_SEQ 2373
FT /note="P -> A (in isoform C)"
FT /evidence="ECO:0000303|PubMed:11076767"
FT /id="VSP_041752"
FT VAR_SEQ 2612..2750
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:11076767"
FT /id="VSP_041753"
FT CONFLICT 224
FT /note="D -> N (in Ref. 1; AAG37995 and 2; AAO84907/
FT AAO84908)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="S -> N (in Ref. 1; AAG37995 and 2; AAO84907/
FT AAO84908)"
FT /evidence="ECO:0000305"
FT CONFLICT 852
FT /note="T -> P (in Ref. 1; AAG37995 and 2; AAO84907/
FT AAO84908)"
FT /evidence="ECO:0000305"
FT CONFLICT 934
FT /note="N -> S (in Ref. 1; AAG37995 and 2; AAO84907/
FT AAO84908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="G -> W (in Ref. 1; AAG37995 and 2; AAO84907/
FT AAO84908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1344
FT /note="T -> S (in Ref. 1; AAG37995 and 2; AAO84907/
FT AAO84908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1484
FT /note="G -> S (in Ref. 1; AAG37995 and 2; AAO84907/
FT AAO84908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1574
FT /note="D -> E (in Ref. 1; AAG37995 and 2; AAO84907/
FT AAO84908)"
FT /evidence="ECO:0000305"
FT CONFLICT 2566
FT /note="K -> R (in Ref. 1; AAG37995)"
FT /evidence="ECO:0000305"
FT CONFLICT 2764
FT /note="S -> R (in Ref. 2; AAO84907/AAO84908)"
FT /evidence="ECO:0000305"
FT CONFLICT 2788
FT /note="I -> T (in Ref. 1; AAG37995)"
FT /evidence="ECO:0000305"
FT CONFLICT 2811
FT /note="L -> V (in Ref. 2; AAO84907/AAO84908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2898 AA; 313035 MW; 5FFF75A4155D49A4 CRC64;
MDLSRRLCST ALVAFIVLAS IHDSQSRFPG LRQKRQYGAN MYLPESSVTP GGEGNDPDEW
TPWSSPSDCS RTCGGGVSYQ TRECLRRDDR GEAVCSGGSR RYFSCNTQDC PEEESDFRAQ
QCSRFDRQQF DGVFYEWVPY TNAPNPCELN CMPKGERFYY RQREKVVDGT RCNDKDLDVC
VNGECMPVGC DMMLGSDAKE DKCRKCGGDG STCKTIRNTI TTKDLAPGYN DLLLLPEGAT
NIRIEETVPS SNYLACRNHS GHYYLNGDWR IDFPRPMFFA NSWWNYQRKP MGFAAPDQLT
CSGPISESLF IVMLVQEKNI SLDYEYSIPE SLSHSQQDTH TWTHHQFNAC SASCGGGSQS
RKVTCNNRIT LAEVNPSLCD QKSKPVEEQA CGTEPCAPHW VEGEWSKCSK GCGSDGFQNR
SITCERISSS GEHTVEEDAV CLKEVGNKPA TKQECNRDVK NCPKYHLGPW TPCDKLCGDG
KQTRKVTCFI EENGHKRVLP EEDCVEEKPE TEKSCLLTPC EGVDWIISQW SGCNACGQNT
ETRTAICGNK EGKVYPEEFC EPEVPTLSRP CKSPKCEAQW FSSEWSKCSA PCGKGVKSRI
VICGEFDGKT VTPADDDSKC NKETKPESEQ DCEGEEKVCP GEWFTGPWGK CSKPCGGGER
VREVLCLSNG TKSVNCDEEK VEPLSEKCNS EACTEDEILP LTSTDKPIED DEEDCDEDGI
ELISDGLSDD EKSEDVIDLE GTAKTETTPE AEDLMQSDSP TPYDEFESTG TTFEGSGYDS
ESTTDSGIST EGSGDDEETS EASTDLSSST DSGSTSSDST SSDSSSSISS DATSEAPASS
VSDSSDSTDA STETTGVSDD STDVSSSTEA SASESTDVSG ASDSTGSTNA SDSTPESSTE
ASSSTDDSTD SSDNSSNVSE SSTEASSSSV SDSNDSSDGS TDGVSSTTEN SSDSTSDATS
DSTASSDSTD STSDQTTETT PESSTDSTES STLDASSTTD ASSTSESSSE SSTDGSSTTS
NSASSETTGL SSDGSTTDAT TAASDNTDIT TDGSTDESTD GSSNASTEGS TEGASEDTTI
STESSGSTES TDAIASDGST TEGSTVEDLS SSTSSDVTSD STITDSSPST EVSGSTDSSS
STDGSSTDAS STEASSTDVT ESTDSTVSGG TSDTTESGPT EESTTEGSTE STTEGSTDST
QSTDLDSTTS DIWSTSDKDD ESESSTPYSF DSEVTKSKPR KCKPKKSTCA KSEYGCCPDG
KSTPKGPFDE GCPIAKTCAD TKYGCCLDGV SPAKGKNNKG CPKSQCAETL FGCCPDKFTA
ADGENDEGCP ETTTVPPTTT TEETQPETTT EIEGSGQDST TSEPDTKKSC SFSEFGCCPD
AETSAKGPDF EGCGLASPVA KGCAESENGC CPDGQTPASG PNGEGCSGCT RERFGCCPDS
QTPAHGPNKE GCCLDTQFGC CPDNILAARG PNNEGCECHY TPYGCCPDNK SAATGYNQEG
CACETTQYGC CPDKITAAKG PKHEGCPCET TQFGCCPDGL TFAKGPHHHG CHCTQTEFKC
CDDEKTPAKG PNGDGCTCVE SKFGCCPDGV TKATDEKFGG CENVQEPPQK ACGLPKETGT
CNNYSVKYYF DTSYGGCARF WYGGCDGNDN RFESEAECKD TCQDYTGKHV CLLPKSAGPC
TGFTKKWYFD VDRNRCEEFQ YGGCYGTNNR FDSLEQCQGT CAASENLPTC EQPVESGPCA
GNFERWYYDN ETDICRPFTY GGCKGNKNNY PTEHACNYNC RQPGVLKDRC ALPKQTGDCS
EKLAKWHFSE SEKRCVPFYY SGCGGNKNNF PTLESCEDHC PRQVAKDICE IPAEVGECAN
YVTSWYYDTQ DQACRQFYYG GCGGNENRFP TEESCLARCD RKPEPTTTTP ATRPQPSRQD
VCDEEPAPGE CSTWVLKWHF DRKIGACRQF YYGNCGGNGN RFETENDCQQ RCLSQEPPAP
TPPRAPAPTR QPDPAPTVAQ CSQPADPGQC DKWALHWNYN ETEGRCQSFY YGGCGGNDNR
FATEEECSAR CSVNIDIRIG ADPVEHDTSK CFLAFEPGNC YNNVTRWFYN SAEGLCDEFV
YTGCGGNANN YATEEECQNE CNDAQTTCAL PPVRGRCSDL SRRWYFDERS GECHEFEFTG
CRGNRNNFVS QSDCLNFCIG EPVVEPSAPT YSVCAEPPEA GECDNRTTAW FYDSENMACT
AFTYTGCGGN GNRFETRDQC ERQCGEFKGV DVCNEPVTTG PCTDWQTKYY FNTASQACEP
FTYGGCDGTG NRFSDLFECQ TVCLAGREPR VGSAKEICLL PVATGRCNGP SVHERRWYYD
DEAGNCVSFI YAGCSGNQNN FRSFEACTNQ CRPEPNKQDN EIGQNPCDTF DAECQELRCP
YGVRRVAARS QPECTQCICE NPCEGYSCPE GQQCAIDVAS SDDRQFAPVC RDIYKPGECP
ALSANASGCA RECYTDADCR GDNKCCSDGC GQLCVHPARP TQPPRTQAPV VSYPGDARAA
LEPKEAHELD VQTAIGGIAV LRCFATGNPA PNITWSLKNL VINTNKGRYV LTANGDLTIV
QVRQTDDGTY VCVASNGLGE PVRREVALQV TEPVSQPAYI YGDKNVTQIV ELNRPAVIRC
PAGGFPEPHV SWWRNGQMFG LKNNLMARDY SLVFNSIQLS DLGLYTCEVY NQRRPVSLRV
TLKAVGPVRP LSPEEEQYMQ YVLNPATRPV TQRPSYPYRP TRPAYVPEPT VNVHAVLALE
PKNSYTPGST IVMSCSVQGY PEPNVTWIKD DVPLYNNERV QITYQPHRLV LSDVTSADSG
KYTCRASNAY TYANGEANVS IQSVVPVSPE CVDNPYFANC KLIVKGRYCS NPYYTQFCCR
SCTLAGQVAS PPLHPNAV
