UNC52_CAEEL
ID UNC52_CAEEL Reviewed; 3375 AA.
AC Q06561; O18261; O18263; Q6BEQ6; Q9U7E8; Q9XTD2; Q9XTI5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Basement membrane proteoglycan {ECO:0000303|PubMed:8393416};
DE AltName: Full=Perlecan homolog {ECO:0000303|PubMed:10512861};
DE AltName: Full=Uncoordinated protein 52;
DE Short=Protein unc-52 {ECO:0000303|PubMed:10512861, ECO:0000303|PubMed:8393416};
DE Flags: Precursor;
GN Name=unc-52 {ECO:0000312|WormBase:ZC101.2e};
GN ORFNames=ZC101.2 {ECO:0000312|WormBase:ZC101.2e};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), FUNCTION, ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=8393416; DOI=10.1101/gad.7.8.1471;
RA Rogalski T.M., Williams B.D., Mullen G.P., Moerman D.G.;
RT "Products of the unc-52 gene in Caenorhabditis elegans are homologous to
RT the core protein of the mammalian basement membrane heparan sulfate
RT proteoglycan.";
RL Genes Dev. 7:1471-1484(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2451-3375 (ISOFORMS C/E), ALTERNATIVE
RP SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=10512861; DOI=10.1091/mbc.10.10.3205;
RA Mullen G.P., Rogalski T.M., Bush J.A., Gorji P.R., Moerman D.G.;
RT "Complex patterns of alternative splicing mediate the spatial and temporal
RT distribution of perlecan/UNC-52 in Caenorhabditis elegans.";
RL Mol. Biol. Cell 10:3205-3221(1999).
RN [4]
RP ALTERNATIVE SPLICING, AND FUNCTION.
RX PubMed=11438655; DOI=10.1128/mcb.21.15.4985-4995.2001;
RA Spike C.A., Shaw J.E., Herman R.K.;
RT "Analysis of smu-1, a gene that regulates the alternative splicing of unc-
RT 52 pre-mRNA in Caenorhabditis elegans.";
RL Mol. Cell. Biol. 21:4985-4995(2001).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1422, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17326220; DOI=10.1002/dvdy.21091;
RA Ono K., Yu R., Ono S.;
RT "Structural components of the nonstriated contractile apparatuses in the
RT Caenorhabditis elegans gonadal myoepithelial sheath and their essential
RT roles for ovulation.";
RL Dev. Dyn. 236:1093-1105(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1422, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [9]
RP FUNCTION, COMPONENT OF AN INTEGRIN CONTAINING ATTACHMENT COMPLEX, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22253611; DOI=10.1371/journal.pgen.1002471;
RA Etheridge T., Oczypok E.A., Lehmann S., Fields B.D., Shephard F.,
RA Jacobson L.A., Szewczyk N.J.;
RT "Calpains mediate integrin attachment complex maintenance of adult muscle
RT in Caenorhabditis elegans.";
RL PLoS Genet. 8:E1002471-E1002471(2012).
CC -!- FUNCTION: Component of an integrin containing attachment complex, which
CC is required for muscle development and maintenance (PubMed:22253611).
CC Probable structural role in myofilament assembly and/or attachment of
CC the myofilament lattice to the cell membrane (PubMed:8393416,
CC PubMed:11438655, PubMed:17326220). May be an extracellular anchor for
CC integrin receptors in body wall muscles and myoepithelial sheath cells
CC (PubMed:8393416, PubMed:17326220). During the formation of
CC neuromuscular junctions at the larval stage, negatively regulates
CC membrane protrusion from body wall muscles, probably downstream of the
CC integrin complex formed by pat-2 and pat-3 (PubMed:16495308). Involved
CC in ovulation (PubMed:17326220). {ECO:0000269|PubMed:11438655,
CC ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:17326220,
CC ECO:0000269|PubMed:22253611, ECO:0000269|PubMed:8393416}.
CC -!- SUBUNIT: Component of an integrin containing attachment complex,
CC composed of at least pat-2, pat-3, pat-4, pat-6, unc-52, unc-97 and
CC unc-112. {ECO:0000305|PubMed:22253611}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:10512861}. Cytoplasm,
CC myofibril, sarcomere, M line {ECO:0000269|PubMed:10512861}. Note=In
CC body wall muscles, colocalizes to dense bodies and M lines with beta-
CC integrin pat-3 (PubMed:10512861). In myoepithelial sheath cells,
CC colocalizes in dense body-like structures with actin thin filaments and
CC pat-3 (PubMed:17326220). {ECO:0000269|PubMed:10512861,
CC ECO:0000269|PubMed:17326220}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=e {ECO:0000312|WormBase:ZC101.2e};
CC IsoId=Q06561-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:ZC101.2a};
CC IsoId=Q06561-2; Sequence=VSP_007195, VSP_007196;
CC Name=b {ECO:0000312|WormBase:ZC101.2b};
CC IsoId=Q06561-3; Sequence=VSP_007191, VSP_007192;
CC Name=c {ECO:0000312|WormBase:ZC101.2c};
CC IsoId=Q06561-4; Sequence=VSP_007193, VSP_007194, VSP_007195,
CC VSP_007196;
CC Name=f {ECO:0000312|WormBase:ZC101.2f};
CC IsoId=Q06561-5; Sequence=VSP_020104, VSP_007195, VSP_020105;
CC -!- TISSUE SPECIFICITY: Detected on embryonic and adult body wall muscle
CC cells (at protein level) (PubMed:8393416, PubMed:10512861). Found in
CC the basement membrane of all contractile tissues (at protein level)
CC (PubMed:10512861). Expressed in gonadal sheath cells and spermatheca
CC (PubMed:17326220). {ECO:0000269|PubMed:10512861,
CC ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:8393416}.
CC -!- DEVELOPMENTAL STAGE: Synthesized early in embryogenesis.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in L4 larval stage,
CC causes a small increase in ectopic membrane extensions from body wall
CC muscles (PubMed:16495308). RNAi-mediated knockdown causes an
CC accumulation in the proximal gonad of endomitotic mature oocytes in 30
CC percent of animals (PubMed:17326220). RNAi-mediated knockdown results
CC in impaired mobility, mitochondrial fragmentation, and disrupted
CC integrin attachment complexes in muscle (PubMed:22253611). This leads
CC to degradation of muscle proteins in the cytosol, myofibrillar defects
CC and disruption of sarcomere organization (PubMed:22253611).
CC {ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:17326220,
CC ECO:0000269|PubMed:22253611}.
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DR EMBL; L13458; AAA28156.1; -; Genomic_DNA.
DR EMBL; BX284602; CAB07704.1; -; Genomic_DNA.
DR EMBL; BX284602; CAB07706.1; -; Genomic_DNA.
DR EMBL; Z93375; CAB07706.1; JOINED; Genomic_DNA.
DR EMBL; BX284602; CAB07707.1; -; Genomic_DNA.
DR EMBL; Z93375; CAB07707.1; JOINED; Genomic_DNA.
DR EMBL; BX284602; CAB07708.1; -; Genomic_DNA.
DR EMBL; Z93375; CAB07708.1; JOINED; Genomic_DNA.
DR EMBL; BX284602; CAH04744.1; -; Genomic_DNA.
DR EMBL; Z93375; CAH04744.1; JOINED; Genomic_DNA.
DR EMBL; AF132883; AAD25092.1; -; mRNA.
DR PIR; C88369; C88369.
DR PIR; F88369; F88369.
DR PIR; T19821; T19821.
DR RefSeq; NP_001022488.1; NM_001027317.5.
DR RefSeq; NP_497044.3; NM_064643.8. [Q06561-1]
DR RefSeq; NP_497045.1; NM_064644.3. [Q06561-4]
DR RefSeq; NP_497046.1; NM_064645.4. [Q06561-2]
DR RefSeq; NP_497047.1; NM_064646.4. [Q06561-3]
DR BioGRID; 40407; 19.
DR IntAct; Q06561; 1.
DR STRING; 6239.ZC101.2e; -.
DR iPTMnet; Q06561; -.
DR EPD; Q06561; -.
DR PaxDb; Q06561; -.
DR PeptideAtlas; Q06561; -.
DR PRIDE; Q06561; -.
DR EnsemblMetazoa; ZC101.2a.1; ZC101.2a.1; WBGene00006787. [Q06561-2]
DR EnsemblMetazoa; ZC101.2b.1; ZC101.2b.1; WBGene00006787. [Q06561-3]
DR EnsemblMetazoa; ZC101.2c.1; ZC101.2c.1; WBGene00006787. [Q06561-4]
DR EnsemblMetazoa; ZC101.2e.1; ZC101.2e.1; WBGene00006787. [Q06561-1]
DR EnsemblMetazoa; ZC101.2f.1; ZC101.2f.1; WBGene00006787.
DR GeneID; 175126; -.
DR UCSC; ZC101.2e; c. elegans. [Q06561-1]
DR CTD; 175126; -.
DR WormBase; ZC101.2a; CE15028; WBGene00006787; unc-52. [Q06561-2]
DR WormBase; ZC101.2b; CE15030; WBGene00006787; unc-52. [Q06561-3]
DR WormBase; ZC101.2c; CE15034; WBGene00006787; unc-52. [Q06561-4]
DR WormBase; ZC101.2e; CE18424; WBGene00006787; unc-52. [Q06561-1]
DR WormBase; ZC101.2f; CE37074; WBGene00006787; unc-52. [Q06561-5]
DR eggNOG; KOG3509; Eukaryota.
DR HOGENOM; CLU_000078_0_0_1; -.
DR InParanoid; Q06561; -.
DR OMA; PGHDQSY; -.
DR OrthoDB; 414294at2759; -.
DR PhylomeDB; Q06561; -.
DR Reactome; R-CEL-1474228; Degradation of the extracellular matrix.
DR Reactome; R-CEL-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-CEL-2022928; HS-GAG biosynthesis.
DR Reactome; R-CEL-2024096; HS-GAG degradation.
DR Reactome; R-CEL-3000157; Laminin interactions.
DR Reactome; R-CEL-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-CEL-3000178; ECM proteoglycans.
DR PRO; PR:Q06561; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006787; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q06561; baseline and differential.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0055120; C:striated muscle dense body; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IMP:WormBase.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IGI:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:WormBase.
DR GO; GO:0031581; P:hemidesmosome assembly; IGI:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IMP:WormBase.
DR GO; GO:0048644; P:muscle organ morphogenesis; IGI:WormBase.
DR GO; GO:0030239; P:myofibril assembly; IEP:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
DR GO; GO:1905905; P:pharyngeal gland morphogenesis; IMP:UniProtKB.
DR GO; GO:0060465; P:pharynx development; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:UniProtKB.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:UniProtKB.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 6.
DR CDD; cd00110; LamG; 3.
DR CDD; cd00112; LDLa; 2.
DR Gene3D; 2.60.40.10; -; 17.
DR Gene3D; 4.10.400.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_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; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13895; Ig_2; 2.
DR Pfam; PF00052; Laminin_B; 2.
DR Pfam; PF00053; Laminin_EGF; 7.
DR Pfam; PF02210; Laminin_G_2; 3.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00180; EGF_Lam; 6.
DR SMART; SM00409; IG; 17.
DR SMART; SM00408; IGc2; 17.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00282; LamG; 3.
DR SMART; SM00192; LDLa; 3.
DR SUPFAM; SSF48726; SSF48726; 15.
DR SUPFAM; SSF49899; SSF49899; 3.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57424; SSF57424; 3.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01248; EGF_LAM_1; 7.
DR PROSITE; PS50027; EGF_LAM_2; 5.
DR PROSITE; PS50835; IG_LIKE; 17.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR PROSITE; PS51115; LAMININ_IVA; 2.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Cytoplasm; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Immunoglobulin domain;
KW Laminin EGF-like domain; Proteoglycan; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..3375
FT /note="Basement membrane proteoglycan"
FT /id="PRO_0000026698"
FT DOMAIN 45..130
FT /note="Ig-like C2-type 1"
FT DOMAIN 148..184
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 189..225
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 232..269
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 271..355
FT /note="Ig-like C2-type 2"
FT DOMAIN 384..431
FT /note="Laminin EGF-like 1; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 432..441
FT /note="Laminin EGF-like 2; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 450..633
FT /note="Laminin IV type A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 634..666
FT /note="Laminin EGF-like 2; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 674..720
FT /note="Laminin EGF-like 3; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 721..730
FT /note="Laminin EGF-like 4; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 740..921
FT /note="Laminin IV type A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 922..954
FT /note="Laminin EGF-like 4; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 955..1004
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1011..1060
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1061..1111
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1126..1222
FT /note="Ig-like C2-type 3"
FT DOMAIN 1226..1311
FT /note="Ig-like C2-type 4"
FT DOMAIN 1319..1401
FT /note="Ig-like C2-type 5"
FT DOMAIN 1410..1499
FT /note="Ig-like C2-type 6"
FT DOMAIN 1503..1585
FT /note="Ig-like C2-type 7"
FT DOMAIN 1588..1680
FT /note="Ig-like C2-type 8"
FT DOMAIN 1690..1785
FT /note="Ig-like C2-type 9"
FT DOMAIN 1793..1878
FT /note="Ig-like C2-type 10"
FT DOMAIN 1886..1970
FT /note="Ig-like C2-type 11"
FT DOMAIN 1973..2069
FT /note="Ig-like C2-type 12"
FT DOMAIN 2073..2163
FT /note="Ig-like C2-type 13"
FT DOMAIN 2173..2260
FT /note="Ig-like C2-type 14"
FT DOMAIN 2263..2343
FT /note="Ig-like C2-type 15"
FT DOMAIN 2349..2435
FT /note="Ig-like C2-type 16"
FT DOMAIN 2446..2530
FT /note="Ig-like C2-type 17"
FT DOMAIN 2532..2713
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2793..2960
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3180..3359
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 364..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1478..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1880..1918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2952..3124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1773..1789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2984..3013
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3014..3036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3052..3069
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3094..3120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 2476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2950
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 66..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 149..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 156..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 168..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 190..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 197..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 209..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 233..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 240..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 253..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 293..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 384..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 402..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 414..429
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 634..648
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 636..689
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 691..700
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 703..718
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 955..964
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 957..971
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 974..983
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 986..1002
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1011..1021
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1013..1027
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1030..1039
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1042..1058
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1061..1069
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1063..1079
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1082..1091
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1094..1109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1152..1200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1247..1294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1338..1384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1435..1481
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1527..1573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1618..1663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1719..1767
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1814..1861
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1907..1954
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1998..2053
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2099..2147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2195..2242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2284..2329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2374..2420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2467..2514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2713..2725
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2719..2736
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2738..2747
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2754..2764
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2759..2773
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2775..2784
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2935..2960
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 3141..3152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3146..3162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3164..3173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3333..3359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT VAR_SEQ 1129..1222
FT /note="VLRVRIMEPKRQIALPGDRVHWICQVTGYTTEKIHVEWTKVGEMSLPPNAKA
FT YDGYLVLKGVEAENAGQYRCTATTITQYATDDALLTISKRIS -> G (in isoform
FT f)"
FT /evidence="ECO:0000305"
FT /id="VSP_020104"
FT VAR_SEQ 1129..1160
FT /note="VLRVRIMEPKRQIALPGDRVHWICQVTGYTTE -> GDFARNSPSQNSSGQR
FT RHRRRRIRVRSRFYHH (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_007191"
FT VAR_SEQ 1161..3375
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_007192"
FT VAR_SEQ 1695
FT /note="R -> H (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_007193"
FT VAR_SEQ 1696..1882
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_007194"
FT VAR_SEQ 2442..2482
FT /note="QDQVTFTVADSLPVVYTVGQPAYLSCIGKTETKPNQSVVWT -> RKRKHLG
FT NRRGRRLRHRRRNAQNGPLSRKTRTTTKLFGSWF (in isoform a, isoform c
FT and isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_007195"
FT VAR_SEQ 2483..3375
FT /note="Missing (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_007196"
FT VAR_SEQ 2485..3375
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_020105"
FT CONFLICT 512
FT /note="Missing (in Ref. 1; AAA28156)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="R -> P (in Ref. 1; AAA28156)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3375 AA; 369052 MW; 1AA418BB4E5D67AA CRC64;
MKRSSTVLAA LLALLLVATN DAARHRKYRQ TYQDIDSDDD DTSDVQITVF PSEKEVRDGR
DVSFECRART SDNSVYPTVR WARVGGPLPS SAHDSGGRLT INPVQLSDAG TYICVSDYNG
NTVEARATLS VVSYGPQEVS NGLRQAGQCM ADEKACGNNE CVKNDYVCDG EPDCRDRSDE
ANCPAISRTC EPNEFKCNNN KCVQKMWLCD GDDDCGDNSD ELNCNAKPSS SDCKPTEFQC
HDRRQCVPSS FHCDGTNDCH DGSDEVGCVQ PTVVDPPQTN LQVPRGTTFS LTCKAVAVPE
PYINWRLNWG PVCEPPRCLQ TSEGGYGTLT IHDAQPVDQG AYTCEAINVK GRVLATPDCI
VRVVDDPRPQ PPQPPTAPPQ RASCDTRGAV TPYPNNYGTC ECKSQVTGPN CDQCKPGAFH
LSEKSPEGCL KCFCFGVSND CRSSGHYRTK DRLMFAGDAE GVTISDIEER TIDRNTPFSF
FKTGYLTFDG TTDGVAKYWR LPQRFLGDKV TAYGGKMEFE IEFSGSGHHS SEPMVVLKGN
QNILVHRVRN QEHVLRSDSP VRITVETYET NYEQLNGAAA TREDLLMVLA DLDAFLIRAT
HVAHQTSTSL GDVSWEIAVD RYTPDGLALE VEQCVCPPGY LGTSCEDCAP GYERSGYGPY
LGTCVPIQPR HQQCGPGAVA PTAPAQGQCQ CKASVIGPNC DRCAPNSFGL APTNPQGCIP
CFCSGVTQQC SASSYRRTSV SIDYARGDRD QLELTTSDSR QPYSPQTRAE LSGQAIEFRS
FEEARGQTLY WKLPEKFLGD KVTSYGGTLE YTFKFSGNGN SDQSADVILR GNDIALQYKH
REPFYADREN KVQIKIIETS WQRVDGQQAT REHLLMTLAD LDTLLIKSTY NDDCTDSQLL
SANLEFAEPY GQGLTAAEVE QCICPPGYVG TSCEDCAPGY SRTGGGLYLG LCEKCECNGH
ASQCDKEYGY CLDCQHNTEG DQCERCKPGF VGDARRGTPN DCQPEATRAP CHCNNHSPRG
CDSFGRCLLC EHNTEGTHCE RCKKGYYGDA TKGSPYDCTP CPCPGASDCY LDNEGQVACR
ICPAGLQGRL CNECAPGYTR SNKPAGRVCE PIGQVTNEDI TFVQKPHEVL RVRIMEPKRQ
IALPGDRVHW ICQVTGYTTE KIHVEWTKVG EMSLPPNAKA YDGYLVLKGV EAENAGQYRC
TATTITQYAT DDALLTISKR ISGRPPQPVI DPPHLVVNEG EPAAFRCWVP GIPDCQITWH
REQLGGPLPH GVYQTGNALK IPQSQLHHAG RYICSAANQY GTGQSPPAVL EVKKPVIPPK
VDPIRQTVDR DQPARFKCWV PGNSNVQLRW SRPGGAPLPS GVQEQQGILH IPRASDQEVG
QYVCTATDPS DNTPLQSEPV QLNIRDPAPP QRGAAPQIDP PNQTVNVNDP AQFRCWVPGQ
PRAQLKWSRK DGRPLPNGIL ERDGFLRIDK SQLHDAGEYE CTSTEPDGST QLSPPARLNV
NQPQAIQPQV DPPVQTVNEG EPSRIRCWVP GHPNIQLQFV KRGRRPLPAH ARFSQGNLEI
PRTLKSDEDE YICIATDPTT NRPVESNPAR VIVKSPIRPI IDPAEQTVPE GSPFKIRCYV
PGHPSVQLTF RRVSGQLNED ADENNGLLAV QRAELTDEGD YICTARDPDT GAPIDSTPAT
VHVTNAAAPP QVEARPPQHP VITPQTQTIP EGDPARIQCT VPGNPSAAQH LSFERVDGKG
LPFGSSDDRG VLTIPSTQLQ DAGEYVCLYS PENSPPVKTN PSTLNVTPEG TPPRPVATPP
LLSVAPGSPA RFNCVAHSDT PARIRWGFRE ENGPLPEHVN QDGDDIVISE AGDRNVGEYV
CSATNDFGTG VADPVRLEVT EDQEPPTAVV EPRTWNGKPG ERHQFRCITT GSPTPKITWT
GPNGSPLPHD VTPLEPNILD FSNGRSELNG DYTCTASNPI GEASDHGNVN IGPSLTVKTN
PPGPKLIVTV GEPLQVKCEA FGAPGDPEPE VEWLHDPGPE RGDLPDDFKP VTISEQFIRH
PNVGLGNAGV YTCKGSSAHA TATKNIYIEV VEPSRIATVS ILGGSSQWFD QGEKGELICT
ATGSSLVDRL EWEKVDDQLP TDVEEHNEPG LLHFPSFKNS YAGEYRCNGY RNNEIIASAA
VHVHSSANAD DEPKVEIEPP RVRVVSQGDN IVLKCSVQGA ENGEHFKWAL LRGGSLVRQL
GTEPTLEITK ADPSNDFGVY RCNVEDNNGL VIGSAFTAVS VGQQDKSHAQ IVKFDDKSDA
SFTCPIYSVP GSKVDWTYEN GDLPSKAVPN GNKIEIKEFD DASAGTYVCK VSFDGNVVEG
FVTAQMFVPD TIIQVLLEVS SESPQIGDRA WFDCKVTGDP SAVISWTKEG NDDLPPNAQV
TGGRLLFTDL KEDNAGVYRC VAKTKAGPLQ TRTVLNVGSG KQDQVTFTVA DSLPVVYTVG
QPAYLSCIGK TETKPNQSVV WTKEEGDLPS GSRVEQGVLM LPSVHRDDEG SYTCEIVKEE
NPVFSTVDLQ IDDFIPVIDG EPIELPPLSD EEIVNLDIEI TLNTANPKGI IFETKRINSG
DLLATPYDTI HHEAKITDYG TVLYEFDIGN GRQIVETTNP INPNEWNVIK IKNDKNQVTI
QLNDESATIR QHTNPLPSLS TGVNRPVFIG GRHEPTNEAN DFRGIISQVV LSGHNVGLGD
ARIPSSVVKY DACASTNLCL NGANCRNANN HHGFSCECAE EFHGEYCQWR SNSCHDESCN
TGICLDNEES WQCVCPLGTT GLRCEEKTEI PQPLGFTSDT SFLAVKRPVK FESIKMKLRP
QADSDEHILM YFASDYGSNT KQYTSLSLIA NQVVLTVRRP DKEVQKIRSE TLEAGELIDV
AVRQAGNALV MTVDGNQVST IETDTLKPGT EIFIGGLPPG LNSPDDVVEQ SFQGCVYEIL
INSQDVDLQN LSSSGDISSC EESQFPVEED DTTTTTTTEE PEAVIEEPTT EEPTTTEEPI
TEEPTEEPTT TEEPTTTEEP TTTTEEPTTT TTEEPYHIYE TSRDDDPEII IPVETTTTST
TTTSTTEEPE AEPALVLPTD PVEENDVSDE EEEISTISTV SPDNGLDSDS DYSEGTLPPD
SSSEEIVVGD VYSTQEPNNI CANSTCGMNG QCVPRNMTHY TCECKLYYDG PTCSLFKPIE
HAARFDGDAF IELSSDEFPH LTSEKDEIVA FKFKTEQQNG VLLWQGQRPT VQQMEDYISV
GIVNGHLHFS YELGGGAAHL ISEERVDDGK EHSVRFERKG REGQMRIDNY REVDGRSTGI
LAMLNVDGNI FVGGVPDISK ATGGLFSNNF VGCIADVELN GVKLDLMATA IDGKNVKPCD
EWMHRKRWLY RRRVR
