GenomeNet

Database: UniProt
Entry: Q06561
LinkDB: Q06561
Original site: Q06561 
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   13-FEB-2019, entry version 175.
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
RT   to 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
RT   investigating 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
RT   temporal 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
RT   unc-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
RP   BY 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
RT   to 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
RT   the Caenorhabditis elegans gonadal myoepithelial sheath and their
RT   essential roles for ovulation.";
RL   Dev. Dyn. 236:1093-1105(2007).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1422, AND IDENTIFICATION
RP   BY 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
RT   muscle in Caenorhabditis elegans.";
RL   PLoS Genet. 8:E1002471-E1002471(2012).
CC   -!- FUNCTION: Component of an integrin containing attachment complex,
CC       which is required for muscle development and maintenance
CC       (PubMed:22253611). Probable structural role in myofilament
CC       assembly and/or attachment of the myofilament lattice to the cell
CC       membrane (PubMed:8393416, PubMed:11438655, PubMed:17326220). May
CC       be an extracellular anchor for integrin receptors in body wall
CC       muscles and myoepithelial sheath cells (PubMed:8393416,
CC       PubMed:17326220). During the formation of neuromuscular junctions
CC       at the larval stage, negatively regulates membrane protrusion from
CC       body wall muscles, probably downstream of the integrin complex
CC       formed by pat-2 and pat-3 (PubMed:16495308). Involved in ovulation
CC       (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
CC       and unc-112. {ECO:0000305|PubMed:22253611}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000269|PubMed:10512861}.
CC       Cytoplasm, myofibril, sarcomere, M line
CC       {ECO:0000269|PubMed:10512861}. Note=In body wall muscles,
CC       colocalizes to dense bodies and M lines with beta-integrin pat-3
CC       (PubMed:10512861). In myoepithelial sheath cells, colocalizes in
CC       dense body-like structures with actin thin filaments and pat-3
CC       (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         Note=No experimental confirmation available.;
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         Note=No experimental confirmation available.;
CC       Name=c {ECO:0000312|WormBase:ZC101.2c};
CC         IsoId=Q06561-4; Sequence=VSP_007193, VSP_007194, VSP_007195,
CC                                  VSP_007196;
CC         Note=No experimental confirmation available.;
CC       Name=f {ECO:0000312|WormBase:ZC101.2f};
CC         IsoId=Q06561-5; Sequence=VSP_020104, VSP_007195, VSP_020105;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Detected on embryonic and adult body wall
CC       muscle cells (at protein level) (PubMed:8393416, PubMed:10512861).
CC       Found in the basement membrane of all contractile tissues (at
CC       protein level) (PubMed:10512861). Expressed in gonadal sheath
CC       cells and spermatheca (PubMed:17326220).
CC       {ECO:0000269|PubMed:10512861, ECO:0000269|PubMed:17326220,
CC       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
CC       wall muscles (PubMed:16495308). RNAi-mediated knockdown causes an
CC       accumulation in the proximal gonad of endomitotic mature oocytes
CC       in 30 percent of animals (PubMed:17326220). RNAi-mediated
CC       knockdown results in impaired mobility, mitochondrial
CC       fragmentation, and disrupted integrin attachment complexes in
CC       muscle (PubMed:22253611). This leads to degradation of muscle
CC       proteins in the cytosol, myofibrillar defects and disruption of
CC       sarcomere organization (PubMed:22253611).
CC       {ECO:0000269|PubMed:16495308, ECO:0000269|PubMed:17326220,
CC       ECO:0000269|PubMed:22253611}.
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   UniGene; Cel.13832; -.
DR   ProteinModelPortal; Q06561; -.
DR   SMR; Q06561; -.
DR   BioGrid; 40407; 13.
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; ZC101.2a; WBGene00006787. [Q06561-2]
DR   EnsemblMetazoa; ZC101.2b; ZC101.2b; WBGene00006787. [Q06561-3]
DR   EnsemblMetazoa; ZC101.2c; ZC101.2c; WBGene00006787. [Q06561-4]
DR   EnsemblMetazoa; ZC101.2e; ZC101.2e; WBGene00006787. [Q06561-1]
DR   GeneID; 175126; -.
DR   KEGG; cel:CELE_ZC101.2; -.
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   eggNOG; ENOG410XTD2; LUCA.
DR   InParanoid; Q06561; -.
DR   OMA; QAQYLCR; -.
DR   OrthoDB; 414294at2759; -.
DR   PhylomeDB; Q06561; -.
DR   PRO; PR:Q06561; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00006787; Expressed in 4 organ(s), highest expression level in material anatomical entity.
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: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:0005198; F:structural molecule activity; IMP:WormBase.
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   CDD; cd00112; LDLa; 2.
DR   Gene3D; 2.60.40.10; -; 17.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; IPR002049; Laminin_EGF.
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   Pfam; PF07679; I-set; 1.
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; Complete proteome; Cytoplasm;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Immunoglobulin domain; Laminin EGF-like domain; Proteoglycan;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23   3375       Basement membrane proteoglycan.
FT                                /FTId=PRO_0000026698.
FT   DOMAIN       45    130       Ig-like C2-type 1.
FT   DOMAIN      148    184       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      189    225       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      232    269       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      271    355       Ig-like C2-type 2.
FT   DOMAIN      384    431       Laminin EGF-like 1; truncated.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      432    441       Laminin EGF-like 2; first part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      450    633       Laminin IV type A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00458}.
FT   DOMAIN      634    666       Laminin EGF-like 2; second part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      674    720       Laminin EGF-like 3; truncated.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      721    730       Laminin EGF-like 4; first part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      740    921       Laminin IV type A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00458}.
FT   DOMAIN      922    954       Laminin EGF-like 4; second part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN      955   1004       Laminin EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1011   1060       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1061   1111       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1126   1222       Ig-like C2-type 3.
FT   DOMAIN     1226   1311       Ig-like C2-type 4.
FT   DOMAIN     1319   1401       Ig-like C2-type 5.
FT   DOMAIN     1410   1499       Ig-like C2-type 6.
FT   DOMAIN     1503   1585       Ig-like C2-type 7.
FT   DOMAIN     1588   1680       Ig-like C2-type 8.
FT   DOMAIN     1690   1785       Ig-like C2-type 9.
FT   DOMAIN     1793   1878       Ig-like C2-type 10.
FT   DOMAIN     1886   1970       Ig-like C2-type 11.
FT   DOMAIN     1973   2069       Ig-like C2-type 12.
FT   DOMAIN     2073   2163       Ig-like C2-type 13.
FT   DOMAIN     2173   2260       Ig-like C2-type 14.
FT   DOMAIN     2263   2343       Ig-like C2-type 15.
FT   DOMAIN     2349   2435       Ig-like C2-type 16.
FT   DOMAIN     2446   2530       Ig-like C2-type 17.
FT   DOMAIN     2532   2713       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     2793   2960       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     3180   3359       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   COMPBIAS   2961   3093       Glu-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00007}.
FT   COMPBIAS   2972   3066       Thr-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00017}.
FT   CARBOHYD   1422   1422       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12754521,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   2476   2476       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2950   2950       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3143   3143       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3156   3156       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     66    114       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    149    161       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    156    174       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    168    183       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    190    202       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    197    215       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    209    224       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    233    246       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    240    259       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    253    268       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    293    344       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    384    400       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    402    411       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    414    429       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    634    648       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    636    689       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    691    700       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    703    718       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    955    964       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    957    971       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    974    983       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    986   1002       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1011   1021       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1013   1027       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1030   1039       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1042   1058       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1061   1069       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1063   1079       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1082   1091       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1094   1109       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1152   1200       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   1247   1294       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   1338   1384       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   1435   1481       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   1527   1573       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   1618   1663       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   1719   1767       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   1814   1861       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   1907   1954       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   1998   2053       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   2099   2147       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   2195   2242       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   2284   2329       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   2374   2420       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   2467   2514       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID   2713   2725       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2719   2736       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2738   2747       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2754   2764       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2759   2773       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2775   2784       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2935   2960       {ECO:0000255|PROSITE-ProRule:PRU00122}.
FT   DISULFID   3141   3152       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3146   3162       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3164   3173       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   3333   3359       {ECO:0000255|PROSITE-ProRule:PRU00122}.
FT   VAR_SEQ    1129   1222       VLRVRIMEPKRQIALPGDRVHWICQVTGYTTEKIHVEWTKV
FT                                GEMSLPPNAKAYDGYLVLKGVEAENAGQYRCTATTITQYAT
FT                                DDALLTISKRIS -> G (in isoform f).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_020104.
FT   VAR_SEQ    1129   1160       VLRVRIMEPKRQIALPGDRVHWICQVTGYTTE -> GDFAR
FT                                NSPSQNSSGQRRHRRRRIRVRSRFYHH (in isoform
FT                                b). {ECO:0000305}.
FT                                /FTId=VSP_007191.
FT   VAR_SEQ    1161   3375       Missing (in isoform b). {ECO:0000305}.
FT                                /FTId=VSP_007192.
FT   VAR_SEQ    1695   1695       R -> H (in isoform c). {ECO:0000305}.
FT                                /FTId=VSP_007193.
FT   VAR_SEQ    1696   1882       Missing (in isoform c). {ECO:0000305}.
FT                                /FTId=VSP_007194.
FT   VAR_SEQ    2442   2482       QDQVTFTVADSLPVVYTVGQPAYLSCIGKTETKPNQSVVWT
FT                                -> RKRKHLGNRRGRRLRHRRRNAQNGPLSRKTRTTTKLFG
FT                                SWF (in isoform a, isoform c and isoform
FT                                f). {ECO:0000305}.
FT                                /FTId=VSP_007195.
FT   VAR_SEQ    2483   3375       Missing (in isoform a and isoform c).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_007196.
FT   VAR_SEQ    2485   3375       Missing (in isoform f). {ECO:0000305}.
FT                                /FTId=VSP_020105.
FT   CONFLICT    512    512       Missing (in Ref. 1; AAA28156).
FT                                {ECO:0000305}.
FT   CONFLICT    547    547       R -> P (in Ref. 1; AAA28156).
FT                                {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
//
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