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   27-MAR-2024, entry version 156.
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 a 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   GlyCosmos; Q6DIB5; 2 sites, No reported glycans.
DR   GlyGen; Q6DIB5; 2 sites.
DR   iPTMnet; Q6DIB5; -.
DR   PhosphoSitePlus; Q6DIB5; -.
DR   MaxQB; Q6DIB5; -.
DR   PaxDb; 10090-ENSMUSP00000075174; -.
DR   PeptideAtlas; Q6DIB5; -.
DR   ProteomicsDB; 292292; -.
DR   Antibodypedia; 14004; 112 antibodies from 14 providers.
DR   DNASU; 70417; -.
DR   Ensembl; ENSMUST00000075770.13; ENSMUSP00000075174.7; ENSMUSG00000024593.16.
DR   GeneID; 70417; -.
DR   KEGG; mmu:70417; -.
DR   UCSC; uc008eyz.2; mouse.
DR   AGR; MGI:2685177; -.
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; CPCHLPN; -.
DR   OrthoDB; 2540323at2759; -.
DR   PhylomeDB; Q6DIB5; -.
DR   TreeFam; TF332598; -.
DR   BioGRID-ORCS; 70417; 3 hits in 76 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 143 other cell types or tissues.
DR   ExpressionAtlas; Q6DIB5; baseline and differential.
DR   GO; GO:0042995; C:cell projection; 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   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 6.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR011489; EMI_domain.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR24035; MULTIPLE EPIDERMAL GROWTH FACTOR-LIKE DOMAINS PROTEIN; 1.
DR   PANTHER; PTHR24035:SF136; MULTIPLE EPIDERMAL GROWTH FACTOR-LIKE DOMAINS PROTEIN 10; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF12661; hEGF; 6.
DR   Pfam; PF00053; Laminin_EGF; 5.
DR   PRINTS; PR00011; EGFLAMININ.
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.
DR   Genevisible; Q6DIB5; MM.
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
//