MEG10_MOUSE
ID MEG10_MOUSE Reviewed; 1147 AA.
AC Q6DIB5; Q3TLU3; Q3UG73;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Multiple epidermal growth factor-like domains protein 10 {ECO:0000312|MGI:MGI:2685177};
DE Short=Multiple EGF-like domains protein 10;
DE Flags: Precursor;
GN Name=Megf10 {ECO:0000312|MGI:MGI:2685177};
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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, AND DEVELOPMENTAL STAGE.
RX PubMed=17205124; DOI=10.1371/journal.pone.0000120;
RA Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
RA Zhou Z., Chimini G.;
RT "Cooperation between engulfment receptors: the case of ABCA1 and MEGF10.";
RL PLoS ONE 1:E120-E120(2006).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17643423; DOI=10.1016/j.yexcr.2007.06.015;
RA Suzuki E., Nakayama M.;
RT "MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin
RT assembly protein complex 2 medium chain and induces large vacuole
RT formation.";
RL Exp. Cell Res. 313:3729-3742(2007).
RN [5]
RP FUNCTION IN MYOGENESIS, AND TISSUE SPECIFICITY.
RX PubMed=18056409; DOI=10.1083/jcb.200709083;
RA Holterman C.E., Le Grand F., Kuang S., Seale P., Rudnicki M.A.;
RT "Megf10 regulates the progression of the satellite cell myogenic program.";
RL J. Cell Biol. 179:911-922(2007).
RN [6]
RP FUNCTION IN ENDOCYTOSIS.
RX PubMed=20828568; DOI=10.1016/j.febslet.2010.08.050;
RA Singh T.D., Park S.Y., Bae J.S., Yun Y., Bae Y.C., Park R.W., Kim I.S.;
RT "MEGF10 functions as a receptor for the uptake of amyloid-beta.";
RL FEBS Lett. 584:3936-3942(2010).
RN [7]
RP FUNCTION IN NEURONAL MOSAIC SPACING.
RX PubMed=22407321; DOI=10.1038/nature10877;
RA Kay J.N., Chu M.W., Sanes J.R.;
RT "MEGF10 and MEGF11 mediate homotypic interactions required for mosaic
RT spacing of retinal neurons.";
RL Nature 483:465-469(2012).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27170117; DOI=10.1523/jneurosci.3850-15.2016;
RA Iram T., Ramirez-Ortiz Z., Byrne M.H., Coleman U.A., Kingery N.D.,
RA Means T.K., Frenkel D., El Khoury J.;
RT "Megf10 Is a Receptor for C1Q That Mediates Clearance of Apoptotic Cells by
RT Astrocytes.";
RL J. Neurosci. 36:5185-5192(2016).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP NOTCH1.
RX PubMed=28498977; DOI=10.1093/hmg/ddx189;
RA Saha M., Mitsuhashi S., Jones M.D., Manko K., Reddy H.M., Bruels C.,
RA Cho K.A., Pacak C.A., Draper I., Kang P.B.;
RT "Consequences of MEGF10 deficiency on myoblast function and Notch1
RT interactions.";
RL Hum. Mol. Genet. 26:2984-3000(2017).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX DOI=10.1093/hmg/ddz064;
RA Saha M., Rizzo S.A., Ramanathan M., Hightower R.M., Santostefano K.E.,
RA Terada N., Finkel R.S., Berg J.S., Chahin N., Pacak C.A., Wagner R.E.,
RA Alexander M.S., Draper I., Kang P.B.;
RT "Selective serotonin reuptake inhibitors ameliorate MEGF10 myopathy.";
RL Hum. Mol. Genet. 2019:0-0(2019).
CC -!- FUNCTION: Membrane receptor involved in phagocytosis by macrophages and
CC astrocytes of apoptotic cells. Receptor for C1q, an eat-me signal, that
CC binds phosphatidylserine expressed on the surface of apoptotic cells
CC (PubMed:27170117). Cooperates with ABCA1 within the process of
CC engulfment (By similarity). Promotes the formation of large
CC intracellular vacuoles and may be responsible for the uptake of
CC amyloid-beta peptides (PubMed:20828568). Necessary for astrocyte-
CC dependent apoptotic neuron clearance in the developing cerebellum
CC (PubMed:27170117). Plays role in muscle cell proliferation, adhesion
CC and motility. Is also an essential factor in the regulation of
CC myogenesis. Controls the balance between skeletal muscle satellite
CC cells proliferation and differentiation through regulation of the notch
CC signaling pathway (PubMed:28498977,Ref.10). May also function in the
CC mosaic spacing of specific neuron subtypes in the retina through
CC homotypic retinal neuron repulsion. Mosaics provide a mechanism to
CC distribute each cell type evenly across the retina, ensuring that all
CC parts of the visual field have access to a full set of processing
CC elements (PubMed:22407321). {ECO:0000250|UniProtKB:Q96KG7,
CC ECO:0000269|PubMed:18056409, ECO:0000269|PubMed:20828568,
CC ECO:0000269|PubMed:22407321, ECO:0000269|PubMed:27170117,
CC ECO:0000269|PubMed:28498977, ECO:0000269|Ref.10}.
CC -!- SUBUNIT: Homomer (Probable). Interacts with GULP1 and ABCA1. Interacts
CC with AP2M1. Does not interact with MEGF11 (By similarity). Binds with
CC high affinity to complement C1q (By similarity). Interacts (via the
CC cytoplasmic domain) with NOTCH1 (via NICD domain) (PubMed:28498977).
CC {ECO:0000250|UniProtKB:Q96KG7, ECO:0000269|PubMed:28498977,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17643423,
CC ECO:0000269|PubMed:28498977}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:17643423}. Cell projection, phagocytic cup
CC {ECO:0000250|UniProtKB:Q96KG7}. Note=Forms an irregular, mosaic-like
CC adhesion pattern in region of the cell surface that becomes firmely
CC fixed to the substrate. Expressed at the cell surface in clusters
CC around cell corpses during engulfment. During the engulfment of
CC apoptotic thymocytes, recruited at the bottom of the forming phagocytic
CC cup. Colocalizes with ABCA1 in absence of any phagocytic challenge.
CC Does not localize within lamellipodia. Does not localize with MEGF11
CC (By similarity). Enriched at the sites of contact with apoptotic
CC thymocyte cells. {ECO:0000250|UniProtKB:Q96KG7}.
CC -!- TISSUE SPECIFICITY: Expressed in cerebellum (at protein level).
CC Expressed in kidney, stellate cells of the cerebellum and macrophage
CC cell lines. {ECO:0000269|PubMed:17205124, ECO:0000269|PubMed:17643423,
CC ECO:0000269|PubMed:18056409}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 15 dpc (at protein level).
CC Expressed in embryo at 8, 10, 11, 13, 14 and 15 dpc.
CC {ECO:0000269|PubMed:17205124}.
CC -!- DOMAIN: The EMI and EGF-like domains work in concert to promote self-
CC assembly.
CC -!- PTM: Ubiquitinated; mono- and polyubiquitinated forms are detected.
CC {ECO:0000250|UniProtKB:Q96KG7}.
CC -!- PTM: Phosphorylated on tyrosine residues. Phosphorylation at Tyr-1030
CC may be important for muscle cell proliferation.
CC {ECO:0000250|UniProtKB:Q96KG7}.
CC -!- DISRUPTION PHENOTYPE: Mutants show at postnatal day 7 an increased
CC amount of apoptotic cells in the developing cerebellum. However, adult
CC brains do not show higher numbers of apoptotic cells in the cerebellum
CC compared to wild-type. Astrocytes from knockout mice as well as
CC heterozygous mice have a significant impairment in engulfment of
CC apoptotic cells (PubMed:27170117). Reduced proliferation of primary
CC myoblasts (Ref.10). Mutants have normal mobility and their skeletal
CC muscles show mildly increased endomysial connective tissue. They
CC display reduced motor activity after exercise and show slower muscle
CC regeneration (PubMed:28498977). MEGF10 and DMD double knockout animals
CC have pronounced fiber size variability and intracellular inclusions in
CC the quadriceps femoris with extensive endomysial connective tissue
CC infiltration. Mice develop muscle weakness, kyphosis and a waddling
CC gait. At 2 months of age, they have reduced contractile force compared
CC to wild-type mice. They display reduced motor activity after exercise
CC and they walk shorter distances than wild-type. They have a delayed
CC regeneration after muscle injury and an aberrant muscle fber typing and
CC cross-sectional areas (PubMed:28498977). {ECO:0000269|PubMed:27170117,
CC ECO:0000269|PubMed:28498977, ECO:0000269|Ref.10}.
CC -!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
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DR EMBL; AK147238; BAE27788.1; -; mRNA.
DR EMBL; AK148084; BAE28336.1; -; mRNA.
DR EMBL; AK166316; BAE38699.1; -; mRNA.
DR EMBL; BC075647; AAH75647.1; -; mRNA.
DR CCDS; CCDS29264.1; -.
DR RefSeq; NP_001001979.1; NM_001001979.2.
DR AlphaFoldDB; Q6DIB5; -.
DR BioGRID; 214036; 2.
DR STRING; 10090.ENSMUSP00000075174; -.
DR GlyGen; Q6DIB5; 2 sites.
DR iPTMnet; Q6DIB5; -.
DR PhosphoSitePlus; Q6DIB5; -.
DR MaxQB; Q6DIB5; -.
DR PaxDb; Q6DIB5; -.
DR PeptideAtlas; Q6DIB5; -.
DR PRIDE; Q6DIB5; -.
DR ProteomicsDB; 292292; -.
DR Antibodypedia; 14004; 92 antibodies from 14 providers.
DR DNASU; 70417; -.
DR Ensembl; ENSMUST00000075770; ENSMUSP00000075174; ENSMUSG00000024593.
DR GeneID; 70417; -.
DR KEGG; mmu:70417; -.
DR UCSC; uc008eyz.2; mouse.
DR CTD; 84466; -.
DR MGI; MGI:2685177; Megf10.
DR VEuPathDB; HostDB:ENSMUSG00000024593; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00940000157703; -.
DR HOGENOM; CLU_008281_1_0_1; -.
DR InParanoid; Q6DIB5; -.
DR OMA; SSHCGCK; -.
DR OrthoDB; 561378at2759; -.
DR PhylomeDB; Q6DIB5; -.
DR TreeFam; TF332598; -.
DR BioGRID-ORCS; 70417; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Megf10; mouse.
DR PRO; PR:Q6DIB5; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q6DIB5; protein.
DR Bgee; ENSMUSG00000024593; Expressed in otolith organ and 142 other tissues.
DR ExpressionAtlas; Q6DIB5; baseline and differential.
DR Genevisible; Q6DIB5; MM.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001891; C:phagocytic cup; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001849; F:complement component C1q complex binding; ISO:MGI.
DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; ISO:MGI.
DR GO; GO:0043277; P:apoptotic cell clearance; IBA:GO_Central.
DR GO; GO:1902742; P:apoptotic process involved in development; IMP:MGI.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IMP:MGI.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0055001; P:muscle cell development; ISS:UniProtKB.
DR GO; GO:0033002; P:muscle cell proliferation; ISO:MGI.
DR GO; GO:0048627; P:myoblast development; IMP:UniProtKB.
DR GO; GO:0051451; P:myoblast migration; IMP:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IMP:UniProtKB.
DR GO; GO:0043654; P:recognition of apoptotic cell; IDA:MGI.
DR GO; GO:0051147; P:regulation of muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0048641; P:regulation of skeletal muscle tissue development; ISO:MGI.
DR GO; GO:0014719; P:skeletal muscle satellite cell activation; IMP:UniProtKB.
DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IMP:UniProtKB.
DR GO; GO:0014841; P:skeletal muscle satellite cell proliferation; IDA:UniProtKB.
DR CDD; cd00055; EGF_Lam; 1.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF12661; hEGF; 7.
DR Pfam; PF00053; Laminin_EGF; 5.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 14.
DR PROSITE; PS00022; EGF_1; 17.
DR PROSITE; PS01186; EGF_2; 17.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS51041; EMI; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Cell projection; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Myogenesis; Phagocytosis;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1147
FT /note="Multiple epidermal growth factor-like domains
FT protein 10"
FT /id="PRO_0000309733"
FT TOPO_DOM 26..857
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 858..878
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 879..1147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..107
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 101..136
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 144..179
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 187..222
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 230..265
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 278..308
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 316..351
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 405..440
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 453..483
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 491..526
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 539..569
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 577..612
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 665..700
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 713..743
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 751..786
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 799..829
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1..857
FT /note="Necessary for interaction with AP2M1, self-assembly
FT and formation of the irregular, mosaic-like adhesion
FT pattern"
FT /evidence="ECO:0000250|UniProtKB:Q96KG7"
FT REGION 945..1147
FT /note="Necessary for formation of large intracellular
FT vacuoles"
FT /evidence="ECO:0000250|UniProtKB:Q96KG7"
FT REGION 1093..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1030
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q96KG7"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..95
FT /evidence="ECO:0000255"
FT DISULFID 60..69
FT /evidence="ECO:0000255"
FT DISULFID 94..105
FT /evidence="ECO:0000255"
FT DISULFID 109..124
FT /evidence="ECO:0000250"
FT DISULFID 126..135
FT /evidence="ECO:0000250"
FT DISULFID 148..160
FT /evidence="ECO:0000250"
FT DISULFID 154..167
FT /evidence="ECO:0000250"
FT DISULFID 169..178
FT /evidence="ECO:0000250"
FT DISULFID 191..203
FT /evidence="ECO:0000250"
FT DISULFID 197..210
FT /evidence="ECO:0000250"
FT DISULFID 212..221
FT /evidence="ECO:0000250"
FT DISULFID 234..246
FT /evidence="ECO:0000250"
FT DISULFID 240..253
FT /evidence="ECO:0000250"
FT DISULFID 255..264
FT /evidence="ECO:0000250"
FT DISULFID 281..289
FT /evidence="ECO:0000250"
FT DISULFID 283..296
FT /evidence="ECO:0000250"
FT DISULFID 298..307
FT /evidence="ECO:0000250"
FT DISULFID 320..332
FT /evidence="ECO:0000250"
FT DISULFID 326..339
FT /evidence="ECO:0000250"
FT DISULFID 341..350
FT /evidence="ECO:0000250"
FT DISULFID 409..421
FT /evidence="ECO:0000250"
FT DISULFID 415..428
FT /evidence="ECO:0000250"
FT DISULFID 430..439
FT /evidence="ECO:0000250"
FT DISULFID 456..464
FT /evidence="ECO:0000250"
FT DISULFID 458..471
FT /evidence="ECO:0000250"
FT DISULFID 473..482
FT /evidence="ECO:0000250"
FT DISULFID 495..507
FT /evidence="ECO:0000250"
FT DISULFID 501..514
FT /evidence="ECO:0000250"
FT DISULFID 516..525
FT /evidence="ECO:0000250"
FT DISULFID 542..550
FT /evidence="ECO:0000250"
FT DISULFID 544..557
FT /evidence="ECO:0000250"
FT DISULFID 559..568
FT /evidence="ECO:0000250"
FT DISULFID 581..593
FT /evidence="ECO:0000250"
FT DISULFID 587..600
FT /evidence="ECO:0000250"
FT DISULFID 602..611
FT /evidence="ECO:0000250"
FT DISULFID 669..681
FT /evidence="ECO:0000250"
FT DISULFID 675..688
FT /evidence="ECO:0000250"
FT DISULFID 690..699
FT /evidence="ECO:0000250"
FT DISULFID 716..724
FT /evidence="ECO:0000250"
FT DISULFID 718..731
FT /evidence="ECO:0000250"
FT DISULFID 733..742
FT /evidence="ECO:0000250"
FT DISULFID 755..767
FT /evidence="ECO:0000250"
FT DISULFID 761..774
FT /evidence="ECO:0000250"
FT DISULFID 776..785
FT /evidence="ECO:0000250"
FT DISULFID 802..810
FT /evidence="ECO:0000250"
FT DISULFID 804..817
FT /evidence="ECO:0000250"
FT DISULFID 819..828
FT /evidence="ECO:0000250"
FT CONFLICT 323
FT /note="A -> T (in Ref. 1; BAE38699)"
FT /evidence="ECO:0000305"
FT CONFLICT 1092
FT /note="G -> S (in Ref. 1; BAE38699)"
FT /evidence="ECO:0000305"
FT CONFLICT 1137
FT /note="N -> S (in Ref. 1; BAE38699)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="S -> T (in Ref. 1; BAE38699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1147 AA; 122972 MW; FBC50896096181CC CRC64;
MAISSSSCLG LICSLLCHWV GTASSLNLED PNVCSHWESY SVTVQESYPH PFDQIYYTSC
TDILNWFKCT RHRISYRTAY RHGEKTMYRR KSQCCPGFYE SRDMCVPHCA DKCVHGRCIA
PNTCQCEPGW GGTNCSSACD GDHWGPHCSS RCQCKNRALC NPITGACHCA AGYRGWRCED
RCEQGTYGND CHQRCQCQNG ATCDHITGEC RCSPGYTGAF CEDLCPPGKH GPHCEQRCPC
QNGGVCHHVT GECSCPSGWM GTVCGQPCPE GRFGKNCSQE CQCHNGGTCD AATGQCHCSP
GYTGERCQDE CPVGSYGVRC AEACRCVNGG KCYHVSGTCL CEAGFSGELC EARLCPEGLY
GIKCDKRCPC HLDNTHSCHP MSGECGCKPG WSGLYCNETC SPGFYGEACQ QICSCQNGAD
CDSVTGRCAC APGFKGTDCS TPCPLGRYGI NCSSRCGCKN DAVCSPVDGS CICKAGWHGV
DCSIRCPSGT WGFGCNLTCQ CLNGGACNTL DGTCTCAPGW RGAKCEFPCQ DGTYGLNCAE
RCDCSHADGC HPTTGHCRCL PGWSGVHCDS VCAEGRWGPN CSLPCYCKNG ASCSPDDGIC
ECAPGFRGTT CQRICSPGFY GHRCSQTCPQ CVHSSGPCHH ITGLCDCLPG FTGALCNEVC
PSGRFGKNCA GVCTCTNNGT CNPIDRSCQC YPGWIGSDCS QPCPPAHWGP NCIHTCNCHN
GAFCSAYDGE CKCTPGWTGL YCTQRCPLGF YGKDCALICQ CQNGADCDHI SGQCTCRTGF
MGRHCEQKCP AGTYGYGCRQ ICDCLNNSTC DHITGTCYCS PGWKGARCDQ AGVIIVGNLN
SLSRTSTALP ADSYQIGAIA GIVVLVLVVL FLLALFIIYR HKQKRKESSM PAVTYTPAMR
VINADYTIAE TLPHSNGGNA NSHYFTNPSY HTLSQCATSP HVNNRDRMTI AKSKNNQLFV
NLKNVNPGKR GTLVDCTGTL PADWKQGGYL NELGAFGLDR SYMGKSLKDL GKNSEYNSST
CSLSSSENPY ATIKDPPALL PKSSECGYVE MKSPARRDSP YAEINNSTPA NRNVYEVEPT
VSVVQGVFSN SGHVTQDPYD LPKNSHIPCH YDLLPVRDSS SSPKREDGGG SNSTSSNSTS
SSSSSSE
