CRUM2_MOUSE
ID CRUM2_MOUSE Reviewed; 1282 AA.
AC Q80YA8; A2ALU1; Q6P6N1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein crumbs homolog 2 {ECO:0000305};
DE Short=crumbs2 {ECO:0000303|PubMed:26496195};
DE AltName: Full=Crumbs-like protein 2;
DE Flags: Precursor;
GN Name=Crb2 {ECO:0000312|MGI:MGI:2679260};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-1282.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=15851977;
RA van den Hurk J.A.J.M., Rashbass P., Roepman R., Davis J., Voesenek K.E.J.,
RA Arends M.L., Zonneveld M.N., van Roekel M.H.G., Cameron K.,
RA Rohrschneider K., Heckenlively J.R., Koenekoop R.K., Hoyng C.B.,
RA Cremers F.P.M., den Hollander A.I.;
RT "Characterization of the crumbs homolog 2 (CRB2) gene and analysis of its
RT role in retinitis pigmentosa and Leber congenital amaurosis.";
RL Mol. Vis. 11:263-273(2005).
RN [4]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=17920587; DOI=10.1016/j.yexcr.2007.08.025;
RA Gosens I., Sessa A., den Hollander A.I., Letteboer S.J.F., Belloni V.,
RA Arends M.L., Le Bivic A., Cremers F.P.M., Broccoli V., Roepman R.;
RT "FERM protein EPB41L5 is a novel member of the mammalian CRB-MPP5 polarity
RT complex.";
RL Exp. Cell Res. 313:3959-3970(2007).
RN [5]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=22072575; DOI=10.1002/dvdy.22778;
RA Xiao Z., Patrakka J., Nukui M., Chi L., Niu D., Betsholtz C.,
RA Pikkarainen T., Pikkarainan T., Vainio S., Tryggvason K.;
RT "Deficiency in Crumbs homolog 2 (Crb2) affects gastrulation and results in
RT embryonic lethality in mice.";
RL Dev. Dyn. 240:2646-2656(2011).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=23001562; DOI=10.1093/hmg/dds398;
RA Alves C.H., Sanz A.S., Park B., Pellissier L.P., Tanimoto N., Beck S.C.,
RA Huber G., Murtaza M., Richard F., Sridevi Gurubaran I., Garcia Garrido M.,
RA Levelt C.N., Rashbass P., Le Bivic A., Seeliger M.W., Wijnholds J.;
RT "Loss of CRB2 in the mouse retina mimics human retinitis pigmentosa due to
RT mutations in the CRB1 gene.";
RL Hum. Mol. Genet. 22:35-50(2013).
RN [7]
RP GLYCOSYLATION AT SER-271, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=26496195; DOI=10.1371/journal.pgen.1005551;
RA Ramkumar N., Harvey B.M., Lee J.D., Alcorn H.L., Silva-Gagliardi N.F.,
RA McGlade C.J., Bestor T.H., Wijnholds J., Haltiwanger R.S., Anderson K.V.;
RT "Protein O-glucosyltransferase 1 (POGLUT1) promotes mouse gastrulation
RT through modification of the apical polarity protein CRUMBS2.";
RL PLoS Genet. 11:E1005551-E1005551(2015).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27870829; DOI=10.1038/ncb3442;
RA Ramkumar N., Omelchenko T., Silva-Gagliardi N.F., McGlade C.J.,
RA Wijnholds J., Anderson K.V.;
RT "Crumbs2 promotes cell ingression during the epithelial-to-mesenchymal
RT transition at gastrulation.";
RL Nat. Cell Biol. 18:1281-1291(2016).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26802325; DOI=10.1016/j.neures.2016.01.001;
RA Dudok J.J., Murtaza M., Henrique Alves C., Rashbass P., Wijnholds J.;
RT "Crumbs 2 prevents cortical abnormalities in mouse dorsal telencephalon.";
RL Neurosci. Res. 108:12-23(2016).
CC -!- FUNCTION: Apical polarity protein that plays a central role during the
CC epithelial-to-mesenchymal transition (EMT) at gastrulation, when newly
CC specified mesodermal cells move inside the embryo (PubMed:26496195,
CC PubMed:27870829). Acts by promoting cell ingression, the process by
CC which cells leave the epithelial epiblast and move inside the embryo to
CC form a new tissue layer (PubMed:27870829). The anisotropic distribution
CC of CRB2 and MYH10/myosin-IIB at cell edges define which cells will
CC ingress: cells with high apical CRB2 are probably extruded from the
CC epiblast by neighboring cells with high levels of apical MYH10/myosin-
CC IIB (PubMed:27870829). Also required for maintenance of the apical
CC polarity complex during development of the cortex.
CC {ECO:0000269|PubMed:26496195, ECO:0000269|PubMed:26802325,
CC ECO:0000269|PubMed:27870829}.
CC -!- SUBUNIT: Interacts (via intracellular domain) with EPB41L5.
CC {ECO:0000250|UniProtKB:Q5IJ48}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:17920587, ECO:0000269|PubMed:26496195,
CC ECO:0000269|PubMed:27870829}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=O-glucosylation is required for localization at the
CC apical plasma membrane (PubMed:26496195). Distributed in a complex
CC anisotropic pattern on apical cell edges: the level of CRB2 on a cell
CC edge is inversely correlated with the level of MYH10/myosin-IIB
CC (PubMed:27870829). {ECO:0000269|PubMed:26496195,
CC ECO:0000269|PubMed:27870829}.
CC -!- TISSUE SPECIFICITY: In the adult eye, strongly expressed in the outer
CC nuclear layer, containing the cell bodies of the photoreceptor cells,
CC and in the inner nuclear layer, containing the cell bodies of the
CC horizontal, bipolar, amacrine, and Mueller glial cells
CC (PubMed:15851977). Also expressed in some cells in the ganglion cell
CC layer (or may be displaced amacrine cells rather than ganglion cells)
CC (PubMed:15851977). {ECO:0000269|PubMed:15851977}.
CC -!- DEVELOPMENTAL STAGE: Expressed in early embryonic cells, more
CC specifically in embryonic regions undergoing dramatic rearrangement,
CC such as the developing neuroepithelium which proceeds with neural tube
CC closure, the anterior splitting lateral plate mesoderm that wraps the
CC pericardial cavity and the differentiating somite epithelium
CC (PubMed:22072575). Widely expressed throughout the epiblast and the
CC lateral plate mesoderm at 7 dpc. At 7.5 dpc-7.75 dpc, continues to be
CC expressed in these regions, and expression is also found on the apical
CC side of the embryonic endoderm, and extraembryonic amnion and allantois
CC (PubMed:22072575). At 8-8.5 dpc, expression is also detected in the
CC heart tube, foregut and the apical side of the somite epithelium
CC (PubMed:22072575). Stronger expression is detected on the apical sides
CC of the splitting lateral plate mesoderm, and the apical side of the
CC neural ectoderm at trunk region (PubMed:22072575). Not expressed in the
CC notochord plate or the extra-embryonic endoderm (PubMed:22072575).
CC Expressed in the developing spinal cord, eye, and forebrain at 10.5 dpc
CC (PubMed:17920587). Expressed in the ventricular layers of the
CC developing neural tube along the entire cranial-caudal length,
CC including the anterior forebrain and the posterior spinal cord at 11.5
CC dpc (PubMed:17920587). Expressed in apical epithelial kidney cells at
CC 15.5 dpc (PubMed:17920587). {ECO:0000269|PubMed:17920587,
CC ECO:0000269|PubMed:22072575}.
CC -!- PTM: O-glucosylated by POGLUT1 at Ser-271; consists of an O-glucose
CC trisaccharide, in which the O-glucose is elongated by the addition of
CC two xylose residues (PubMed:26496195). O-glucosylation is required for
CC localization at the plasma membrane (PubMed:26496195).
CC {ECO:0000269|PubMed:26496195}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality due impaired gastrulation
CC (PubMed:22072575, PubMed:27870829). Mesoderm formation is disrupted,
CC and cells do not ingress (PubMed:27870829). Instead, a single layer
CC forms, and the embryo fails to properly establish its body plan,
CC leading to embryonic arrest (PubMed:27870829). Conditional deletion in
CC the developing retina leads to progressive disorganization during late
CC retinal development: retina show progressive thinning of the
CC photoreceptor layer and sites of cellular mislocalization
CC (PubMed:23001562). Conditional deletion in the dorsal telencephalon
CC leads to defects in the maintenance of the apical complex
CC (PubMed:26802325). {ECO:0000269|PubMed:22072575,
CC ECO:0000269|PubMed:23001562, ECO:0000269|PubMed:26802325,
CC ECO:0000269|PubMed:27870829}.
CC -!- SIMILARITY: Belongs to the Crumbs protein family. {ECO:0000305}.
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DR EMBL; AL805959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043114; AAH43114.1; -; mRNA.
DR EMBL; BC062128; AAH62128.1; -; mRNA.
DR CCDS; CCDS50580.1; -.
DR RefSeq; NP_001157038.1; NM_001163566.1.
DR AlphaFoldDB; Q80YA8; -.
DR SMR; Q80YA8; -.
DR STRING; 10090.ENSMUSP00000058007; -.
DR GlyGen; Q80YA8; 13 sites.
DR iPTMnet; Q80YA8; -.
DR PhosphoSitePlus; Q80YA8; -.
DR MaxQB; Q80YA8; -.
DR PaxDb; Q80YA8; -.
DR PeptideAtlas; Q80YA8; -.
DR PRIDE; Q80YA8; -.
DR ProteomicsDB; 285369; -.
DR Antibodypedia; 48144; 132 antibodies from 22 providers.
DR Ensembl; ENSMUST00000050372; ENSMUSP00000058007; ENSMUSG00000035403.
DR GeneID; 241324; -.
DR KEGG; mmu:241324; -.
DR UCSC; uc008jnf.2; mouse.
DR CTD; 286204; -.
DR MGI; MGI:2679260; Crb2.
DR VEuPathDB; HostDB:ENSMUSG00000035403; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00950000183101; -.
DR HOGENOM; CLU_000827_2_0_1; -.
DR InParanoid; Q80YA8; -.
DR OMA; APCEDCT; -.
DR OrthoDB; 111153at2759; -.
DR PhylomeDB; Q80YA8; -.
DR TreeFam; TF316224; -.
DR BioGRID-ORCS; 241324; 5 hits in 74 CRISPR screens.
DR PRO; PR:Q80YA8; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80YA8; protein.
DR Bgee; ENSMUSG00000035403; Expressed in retinal neural layer and 45 other tissues.
DR ExpressionAtlas; Q80YA8; baseline and differential.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0035003; C:subapical complex; IDA:MGI.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0072359; P:circulatory system development; IMP:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0055111; P:ingression involved in gastrulation with mouth forming second; IMP:UniProtKB.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:UniProtKB.
DR GO; GO:0001707; P:mesoderm formation; IMP:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; ISO:MGI.
DR GO; GO:0014028; P:notochord formation; IMP:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB.
DR GO; GO:0001895; P:retina homeostasis; IMP:UniProtKB.
DR GO; GO:0046549; P:retinal cone cell development; IMP:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; IMP:UniProtKB.
DR CDD; cd00110; LamG; 3.
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; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00008; EGF; 9.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00179; EGF_CA; 13.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; SSF49899; 3.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 8.
DR PROSITE; PS00022; EGF_1; 14.
DR PROSITE; PS01186; EGF_2; 9.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 5.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Developmental protein; Disulfide bond;
KW EGF-like domain; Gastrulation; Glycoprotein; Membrane; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1282
FT /note="Protein crumbs homolog 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000055626"
FT TOPO_DOM 36..1221
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1222..1242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1243..1282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 71..110
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 112..148
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 150..186
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 188..225
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 227..263
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 265..322
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 324..360
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 362..398
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 400..440
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 444..607
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 609..645
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 649..808
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 810..846
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 872..1051
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1053..1089
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1091..1127
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1131..1168
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1170..1206
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1246..1282
FT /note="Interaction with EPB41L5"
FT /evidence="ECO:0000250|UniProtKB:Q5IJ48"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000305|PubMed:26496195"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 80..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 100..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 116..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 121..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 138..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 154..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 159..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 176..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 192..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 197..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 214..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 231..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 236..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 253..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 269..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 274..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 312..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 328..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 333..348
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 350..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 366..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 371..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 388..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 404..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 409..428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 430..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 583..607
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 613..624
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 618..633
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 635..644
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 769..808
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 814..825
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 819..834
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 836..845
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1010..1051
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1057..1068
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1062..1077
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1079..1088
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1095..1105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1100..1115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1117..1126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1135..1147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1141..1156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1158..1167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1174..1185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1179..1194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1196..1205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 842
FT /note="G -> E (in Ref. 2; AAH62128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1282 AA; 134760 MW; 9099A9AAD1FEC403 CRC64;
MALVGPRIWG PRRDIYPLLL LLLLLLLLLL PWVPAGLVPP ETPSVCASDP CAPGTKCQAT
ESGGYTCEPS ELGGCATQPC HHGALCVPQG PDPNSFRCYC VPGFQGPHCE LDIDECASRP
CQHGGTCQNL ADHYECHCPL GYAGVTCEAE VDECSSAPCL HGGSCLDGVG SYRCVCAPGY
AGANCQLDVD ECQSQPCAHG GVCHDLVNGF RCDCADTGYE GARCEQEVLE CASAPCAHNA
SCLDGFRSFR CLCWPGFSGE RCEVDEDECA SGPCQNGGQC LQRSDPTLYG GVQAIFPGAF
SFSHAAGFLC SCPLGFAGND CSMDVDECAS GPCLNGGSCQ DLPNGFQCYC QDGYTGLTCQ
EDMDECQSEP CLHGGTCSDT VAGYICQCPE AWGGHDCSVQ LTGCQGHTCP LAATCIPTFK
SGLHGYFCRC PPGTYGPFCG QNTTFSVVSG SSVWGLVPAA ASLGLALRFR TTLLAGTLAT
LKDTRDSLEL VLVGAVLQAT LSRHGTAVLI LTLPDLALND GHWHQVEVTL HLGTLELRLW
HEGCPGQLCV ASGPVATGPT ASVASGPPGS YSIYLGGGVF AGCFQDVRVE GHLLLPEELK
GTVLLGCERR EPCQPLPCAH GGACVDLWTH FRCDCPRPYR GATCTDEVPA ATFGLGGATS
SASFLLHQLG PNLTVSFFLR TREPAGLLLQ FANDSVASLT VFLSEGQIRA EGLGHPAVVL
PGRWDDGLPH LVMLSFGPDQ LQDLGQRLYV GGRFYPDDTQ LWGGPFRGCL QDLQLNSIHL
PFFSSPMENS SWPSELEAGQ SSNLTQGCVS EDTCNPNPCF NGGTCHVTWN DFYCTCSENF
TGPTCAQQRW CPRQPCLPPA TCEEVPDGFV CVAEATFREG PPAVFTGHNV SSSLSGLTLA
FRTRDSEAGL LRAVSAAGAH SNIWLAVRNG SLAGDVAGSV LPAPGPRVAD GAWHRVRLAR
EFPQAAASRW LLWLDGAATP VALHGLGGDL GFLQGPGAVP LLLAENFTGC LGRVALGDFP
LPLAPPRSGT VSGAREHFVA WPGSPAVSLG CRGGPVCSPS PCLHGGACRD LFDAFACSCG
PAWEGPRCEI RADPCRSTPC VRGQCHARPD GRFECRCPPG FSGPRCRLPV LPQGCNLNST
CKDGAPCEGG PLGTNCSCQE GLAGLRCQSL DKPCEASPCL NGGTCRVASG IFECTCSAGF
SGQFCEVVKT LPLPLPFPLL EVAVPAACAC LLLLLLGLLS GILAARKRRQ SEGTYSPSQQ
EVAGARLEMD SVLKVPPEER LI
