ID F7H7X5_CALJA Unreviewed; 1146 AA.
AC F7H7X5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Multiple EGF like domains 10 {ECO:0000313|Ensembl:ENSCJAP00000035633.4};
GN Name=MEGF10 {ECO:0000313|Ensembl:ENSCJAP00000035633.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000035633.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000035633.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000035633.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_008989843.1; XM_008991595.1.
DR RefSeq; XP_017825200.1; XM_017969711.1.
DR AlphaFoldDB; F7H7X5; -.
DR STRING; 9483.ENSCJAP00000035633; -.
DR Ensembl; ENSCJAT00000037632.4; ENSCJAP00000035633.4; ENSCJAG00000019171.5.
DR GeneID; 100399631; -.
DR KEGG; cjc:100399631; -.
DR CTD; 84466; -.
DR GeneTree; ENSGT00940000157703; -.
DR InParanoid; F7H7X5; -.
DR OMA; CPCHLPN; -.
DR Proteomes; UP000008225; Chromosome 2.
DR Bgee; ENSCJAG00000019171; Expressed in cerebellum and 3 other cell types or tissues.
DR GO; GO:0001891; C:phagocytic cup; IEA:Ensembl.
DR GO; GO:0001849; F:complement component C1q complex binding; IEA:Ensembl.
DR GO; GO:0005112; F:Notch binding; IEA:Ensembl.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:Ensembl.
DR GO; GO:1902742; P:apoptotic process involved in development; IEA:Ensembl.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IEA:Ensembl.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0055001; P:muscle cell development; IEA:Ensembl.
DR GO; GO:0048627; P:myoblast development; IEA:Ensembl.
DR GO; GO:0051451; P:myoblast migration; IEA:Ensembl.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IEA:Ensembl.
DR GO; GO:0043654; P:recognition of apoptotic cell; IEA:Ensembl.
DR GO; GO:0051147; P:regulation of muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0048641; P:regulation of skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0014719; P:skeletal muscle satellite cell activation; IEA:Ensembl.
DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IEA:Ensembl.
DR GO; GO:0014841; P:skeletal muscle satellite cell proliferation; IEA:Ensembl.
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; 16.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 9.
DR PROSITE; PS51041; EMI; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1146
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035228221"
FT TRANSMEM 854..879
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..107
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 144..179
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 187..222
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 230..265
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 278..308
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 316..351
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 491..526
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 577..612
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 713..743
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 751..786
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1111..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 169..178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 212..221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 255..264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 298..307
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 341..350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 516..525
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 602..611
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 733..742
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 776..785
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1146 AA; 122845 MW; 8C259B65F2B0908E CRC64;
MVISLNSFLS FICLLLCHWI GTSSPLNLED PNVCSHWESY SVTVQESYPH PFDQIYYTSC
TDILNWFKCT RHRISYRTAY RHGEKTMYRR KSQCCPGFYE SGEMCVPHCA DKCVHGRCIA
PNTCQCEPGW GGTNCSSACD GDHWGPHCTS RCQCKNGALC NPITGACHCA AGFRGWRCEN
RCKQGTYGND CHQRCQCQNG ATCDHVTGEC RCPPGYTGAF CEDLCPPGKH GPQCEQRCPC
QNGGVCHHVT GECSCPSGWM GTVCGQPCPE GRFGKNCSQE CQCHNGGTCD AATGQCHCSP
GYTGERCQDE CPVGTYGVRC AEACRCVNGG KCYHVSGACL CEAGFAGERC EARLCPEGLY
GIKCDKRCPC HLDNTHSCHP MSGECACKPG WSGLYCNETC SPGFYGEACQ QICSCQNGAD
CDSVTGKCTC APGFKGIDCS TPCPLGTYGI NCSSRCGCKN DAVCSPVDGS CTCRAGWHGV
DCSIRCPSGT WGFGCNLTCQ CLNGGACNTL DGTCTCAPGW RGKKCELHCQ DGTYGLNCAE
RCDCSHADGC HPTTGHCRCL PGWSGVHCDS VCAEGRWGPN CSLPCYCKNG ASCSPDDGIC
ECAPGFRGTT CQRICSPGFY GHRCSQTCPQ CVHSSGPCHH ISGLCDCLPG FTGALCNEVC
PSGRFGKNCA GICTCTNNGT CNPIDRSCQC YPGWIGSDCS QPCPPAHWGP NCIHTCNCHN
GAFCSAYDGE CKCTPGWTGL YCTQRCPLGF YGKDCALICQ CQNGADCDHI SGQCTCRTGF
MGRHCEQKCP AGTYGYGCRQ LCDCLNNSTC DHITGTCYCS PGWKGARCDQ AGVIIVGNLN
SLSRTSTALP ADSYQIGAIA GIIILVLVVL FLLALFIIYR HKQKGKDSSM PAVTYTPAMR
VINADYTISG TLPHSNGGNA NSHYFTNPSY HTLTQCATSP HVNNRDRMTI TKSKNNQLFV
NLKNVNPGKR GPVGDCTGTL PADWKHGGYL NELGAFGLDR SYMGKSLKDL GKNSEYNSSN
CSLSSSENPY ATIKDPPVLI PKNSECGYVE MKSPARRDSP YAEINNSTSA NKNVYEVEPT
VSVVQGAFSN NGHLTQDPYD LPKNSHIPCH YDLLPVRDSS SSPKREDSGG SSSSSSSSSS
SSSSSE
//
