MEG10_XENTR
ID MEG10_XENTR Reviewed; 1114 AA.
AC A0JM12;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Multiple epidermal growth factor-like domains protein 10;
DE Short=Multiple EGF-like domains protein 10;
DE Flags: Precursor;
GN Name=megf10;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Membrane receptor involved in phagocytosis. May also regulate
CC homotypic retinal neuron repulsion. May play role in cell adhesion and
CC motility. May also be an essential factor in the regulation of
CC myogenesis, controlling the balance between skeletal muscle satellite
CC cells proliferation and differentiation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
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DR EMBL; BC125696; AAI25697.1; -; mRNA.
DR RefSeq; NP_001072726.1; NM_001079258.1.
DR AlphaFoldDB; A0JM12; -.
DR SMR; A0JM12; -.
DR STRING; 8364.ENSXETP00000046417; -.
DR PaxDb; A0JM12; -.
DR PRIDE; A0JM12; -.
DR Ensembl; ENSXETT00000034579; ENSXETP00000034579; ENSXETG00000034085.
DR GeneID; 780183; -.
DR KEGG; xtr:780183; -.
DR CTD; 84466; -.
DR Xenbase; XB-GENE-491974; megf10.
DR eggNOG; KOG1218; Eukaryota.
DR HOGENOM; CLU_008281_1_0_1; -.
DR InParanoid; A0JM12; -.
DR OMA; SSHCGCK; -.
DR OrthoDB; 561378at2759; -.
DR PhylomeDB; A0JM12; -.
DR TreeFam; TF332598; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000034085; Expressed in early embryo and 11 other tissues.
DR ExpressionAtlas; A0JM12; differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0043277; P:apoptotic cell clearance; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0014719; P:skeletal muscle satellite cell activation; ISS:UniProtKB.
DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; ISS:UniProtKB.
DR GO; GO:0014841; P:skeletal muscle satellite cell proliferation; ISS:UniProtKB.
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; 4.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 14.
DR PROSITE; PS00022; EGF_1; 17.
DR PROSITE; PS01186; EGF_2; 16.
DR PROSITE; PS50026; EGF_3; 14.
DR PROSITE; PS51041; EMI; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain; Membrane;
KW Myogenesis; Phagocytosis; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1114
FT /note="Multiple epidermal growth factor-like domains
FT protein 10"
FT /id="PRO_0000309734"
FT TOPO_DOM 25..856
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 857..877
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 878..1114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..106
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 105..135
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 143..178
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 186..221
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 229..264
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 277..307
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 315..350
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 404..439
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 447..482
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 490..525
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 576..611
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 664..699
FT /note="EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 712..742
FT /note="EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 750..785
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 798..828
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 33..94
FT /evidence="ECO:0000255"
FT DISULFID 59..68
FT /evidence="ECO:0000255"
FT DISULFID 93..104
FT /evidence="ECO:0000255"
FT DISULFID 108..117
FT /evidence="ECO:0000250"
FT DISULFID 112..123
FT /evidence="ECO:0000250"
FT DISULFID 125..134
FT /evidence="ECO:0000250"
FT DISULFID 147..159
FT /evidence="ECO:0000250"
FT DISULFID 153..166
FT /evidence="ECO:0000250"
FT DISULFID 168..177
FT /evidence="ECO:0000250"
FT DISULFID 190..202
FT /evidence="ECO:0000250"
FT DISULFID 196..209
FT /evidence="ECO:0000250"
FT DISULFID 211..220
FT /evidence="ECO:0000250"
FT DISULFID 233..245
FT /evidence="ECO:0000250"
FT DISULFID 239..252
FT /evidence="ECO:0000250"
FT DISULFID 254..263
FT /evidence="ECO:0000250"
FT DISULFID 280..288
FT /evidence="ECO:0000250"
FT DISULFID 282..295
FT /evidence="ECO:0000250"
FT DISULFID 297..306
FT /evidence="ECO:0000250"
FT DISULFID 319..331
FT /evidence="ECO:0000250"
FT DISULFID 325..338
FT /evidence="ECO:0000250"
FT DISULFID 340..349
FT /evidence="ECO:0000250"
FT DISULFID 408..420
FT /evidence="ECO:0000250"
FT DISULFID 414..427
FT /evidence="ECO:0000250"
FT DISULFID 429..438
FT /evidence="ECO:0000250"
FT DISULFID 451..463
FT /evidence="ECO:0000250"
FT DISULFID 457..470
FT /evidence="ECO:0000250"
FT DISULFID 472..481
FT /evidence="ECO:0000250"
FT DISULFID 494..506
FT /evidence="ECO:0000250"
FT DISULFID 500..513
FT /evidence="ECO:0000250"
FT DISULFID 515..524
FT /evidence="ECO:0000250"
FT DISULFID 580..592
FT /evidence="ECO:0000250"
FT DISULFID 586..599
FT /evidence="ECO:0000250"
FT DISULFID 601..610
FT /evidence="ECO:0000250"
FT DISULFID 668..680
FT /evidence="ECO:0000250"
FT DISULFID 674..687
FT /evidence="ECO:0000250"
FT DISULFID 689..698
FT /evidence="ECO:0000250"
FT DISULFID 715..723
FT /evidence="ECO:0000250"
FT DISULFID 717..730
FT /evidence="ECO:0000250"
FT DISULFID 732..741
FT /evidence="ECO:0000250"
FT DISULFID 754..766
FT /evidence="ECO:0000250"
FT DISULFID 760..773
FT /evidence="ECO:0000250"
FT DISULFID 775..784
FT /evidence="ECO:0000250"
FT DISULFID 801..809
FT /evidence="ECO:0000250"
FT DISULFID 803..816
FT /evidence="ECO:0000250"
FT DISULFID 818..827
FT /evidence="ECO:0000250"
SQ SEQUENCE 1114 AA; 120016 MW; 7CD27F900D017D3B CRC64;
MVHSLKWLGI FPLILFQWLG TTSSLNLEDP NVCSHWESYS VTVQESYSHP YDQVYYTSCT
DILNWFKCTR HRISYRTAYR RGEKTMYRRK SQCCPGFYES REMCVPHCAD KCVHGRCIAP
NTCQCEPGWG GPNCSSACDV DHWGPHCSSR CQCKNGALCN PITGACHCSS GYKGWRCEER
CDQGTYGNDC QQKCQCQNGA SCDHVTGECR CPPGYTGAFC EDLCPPGKHG SQCEERCPCQ
NGGVCHHVTG ECSCPAGWMG TVCGQPCPEG RYGRNCSQEC QCHNGGTCDS ATGQCYCSPG
YNGERCQEEC PVGLYGVKCA QTCQCLNGGK CYHISGACLC EPGYTGERCE TPLCSEGTYG
MKCDKKCPCH LQYTQSCHPM SGECACKPGR SGLYCNETCS LGFYGEFCQQ ICSCQNGADC
DSVTGKCICA PGFTGVDCST ACPPGTYGVN CSSLCNCKNN AVCSPVDGSC TCKAGWHGVD
CSINCPRGSW GLGCNLTCQC LNGGACNPLD GTCTCAPGWR GLKCELPCQD GTYGMNCIER
CDCSHADGCH PATGYCRCLA GWAGMHCDSV CPGGHWGPNC SLSCDCKNGA SCSPDDGICE
CAPGYRGTTC QRICSPGFYG HRCSQACPQC VHSNGPCHHV TGQCDCLAGF MGSLCNEVCP
SGRYGKNCAG VCACTNNGTC NPIDGTCQCY PGWIGNDCSQ ACPPGHWGPN CIHTCNCHNG
AYCSAYDGEC KCSPGWTGLY CTQRCPLGYY GKECTLVCQC QNGADCDHIT GQCTCRTGFM
GKFCEQKCPS ASYGYGCRQV CDCLNNSTCD HITGTCYCSP GWKGARCDQA VMIVVGNLNS
LSRTSAAIPA DSYQIGAIAG IIILVLVVLF LLALFIIYRQ KQKGKDTAMP AVAYTPAVRV
LSTDYTIADT LPHNNVVNAN SQYFSNPSYH TLSQCTTGPQ VNSMDRMMVS RSKSSQLFVN
LKNLDPGKRS HTIDYTGTLP ADWKQGGFLN ENGLLKNSAY SISTCSLSST ENPYATIKDP
PVLLPKNIEC GYVEMKSPAR RDSAYAEISN SSLANKNVYE VEPTVSVVQG AFCNNGKISQ
DLYDLPKNSH IPCHYDLLPV RESSSSNKDE STSE
