GenomeNet

Database: UniProt
Entry: A0JM12
LinkDB: A0JM12
Original site: A0JM12 
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   16-JAN-2019, entry version 70.
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;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   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
CC       regulate homotypic retinal neuron repulsion. May play role in cell
CC       adhesion and motility. May also be an essential factor in the
CC       regulation of myogenesis, controlling the balance between skeletal
CC       muscle satellite cells proliferation and differentiation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MEGF family. {ECO:0000305}.
DR   EMBL; BC125696; AAI25697.1; -; mRNA.
DR   RefSeq; NP_001072726.1; NM_001079258.1.
DR   UniGene; Str.46279; -.
DR   ProteinModelPortal; A0JM12; -.
DR   SMR; A0JM12; -.
DR   STRING; 8364.ENSXETP00000034579; -.
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   eggNOG; ENOG410XQWV; LUCA.
DR   GeneTree; ENSGT00940000157703; -.
DR   HOVERGEN; HBG108333; -.
DR   InParanoid; A0JM12; -.
DR   OMA; HISGACL; -.
DR   OrthoDB; 561378at2759; -.
DR   TreeFam; TF332598; -.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   Bgee; ENSXETG00000034085; Expressed in 11 organ(s), highest expression level in embryo.
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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030239; P:myofibril assembly; IEA:Ensembl.
DR   GO; GO:0006909; P:phagocytosis; 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; Laminin_EGF.
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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Membrane; Myogenesis; Phagocytosis;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25   1114       Multiple epidermal growth factor-like
FT                                domains protein 10.
FT                                /FTId=PRO_0000309734.
FT   TOPO_DOM     25    856       Extracellular. {ECO:0000255}.
FT   TRANSMEM    857    877       Helical. {ECO:0000255}.
FT   TOPO_DOM    878   1114       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       29    106       EMI. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00384}.
FT   DOMAIN      105    135       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      143    178       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      186    221       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      229    264       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      277    307       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      315    350       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      404    439       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      447    482       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      490    525       EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      576    611       EGF-like 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      664    699       EGF-like 11. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      712    742       EGF-like 12. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      750    785       EGF-like 13. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      798    828       EGF-like 14. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS   1103   1106       Poly-Ser.
FT   DISULFID     33     94       {ECO:0000255}.
FT   DISULFID     59     68       {ECO:0000255}.
FT   DISULFID     93    104       {ECO:0000255}.
FT   DISULFID    108    117       {ECO:0000250}.
FT   DISULFID    112    123       {ECO:0000250}.
FT   DISULFID    125    134       {ECO:0000250}.
FT   DISULFID    147    159       {ECO:0000250}.
FT   DISULFID    153    166       {ECO:0000250}.
FT   DISULFID    168    177       {ECO:0000250}.
FT   DISULFID    190    202       {ECO:0000250}.
FT   DISULFID    196    209       {ECO:0000250}.
FT   DISULFID    211    220       {ECO:0000250}.
FT   DISULFID    233    245       {ECO:0000250}.
FT   DISULFID    239    252       {ECO:0000250}.
FT   DISULFID    254    263       {ECO:0000250}.
FT   DISULFID    280    288       {ECO:0000250}.
FT   DISULFID    282    295       {ECO:0000250}.
FT   DISULFID    297    306       {ECO:0000250}.
FT   DISULFID    319    331       {ECO:0000250}.
FT   DISULFID    325    338       {ECO:0000250}.
FT   DISULFID    340    349       {ECO:0000250}.
FT   DISULFID    408    420       {ECO:0000250}.
FT   DISULFID    414    427       {ECO:0000250}.
FT   DISULFID    429    438       {ECO:0000250}.
FT   DISULFID    451    463       {ECO:0000250}.
FT   DISULFID    457    470       {ECO:0000250}.
FT   DISULFID    472    481       {ECO:0000250}.
FT   DISULFID    494    506       {ECO:0000250}.
FT   DISULFID    500    513       {ECO:0000250}.
FT   DISULFID    515    524       {ECO:0000250}.
FT   DISULFID    580    592       {ECO:0000250}.
FT   DISULFID    586    599       {ECO:0000250}.
FT   DISULFID    601    610       {ECO:0000250}.
FT   DISULFID    668    680       {ECO:0000250}.
FT   DISULFID    674    687       {ECO:0000250}.
FT   DISULFID    689    698       {ECO:0000250}.
FT   DISULFID    715    723       {ECO:0000250}.
FT   DISULFID    717    730       {ECO:0000250}.
FT   DISULFID    732    741       {ECO:0000250}.
FT   DISULFID    754    766       {ECO:0000250}.
FT   DISULFID    760    773       {ECO:0000250}.
FT   DISULFID    775    784       {ECO:0000250}.
FT   DISULFID    801    809       {ECO:0000250}.
FT   DISULFID    803    816       {ECO:0000250}.
FT   DISULFID    818    827       {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
//
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