ID A0A2K6PM42_RHIRO Unreviewed; 1033 AA.
AC A0A2K6PM42;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Multiple EGF like domains 10 {ECO:0000313|Ensembl:ENSRROP00000017611.1};
GN Name=MEGF10 {ECO:0000313|Ensembl:ENSRROP00000017611.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000017611.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000017611.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6PM42; -.
DR STRING; 61622.ENSRROP00000017611; -.
DR Ensembl; ENSRROT00000041765.1; ENSRROP00000017611.1; ENSRROG00000032891.1.
DR GeneTree; ENSGT00940000157703; -.
DR Proteomes; UP000233200; Unplaced.
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:0034109; P:homotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0055001; P:muscle cell development; IEA:Ensembl.
DR GO; GO:0033002; P:muscle cell proliferation; 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: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:0014816; P:skeletal muscle satellite cell differentiation; IEA:Ensembl.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 4.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
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; 6.
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.
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:UP000233200};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 747..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..72
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 80..115
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 123..158
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 171..201
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 209..244
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 384..419
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 470..505
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 606..636
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 644..679
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1004..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 62..71
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 105..114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 148..157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 191..200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 234..243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 409..418
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 495..504
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 626..635
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 669..678
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1033 AA; 109644 MW; 2FE20EC12550A0EC CRC64;
HCADKCVHGR CIAPNTCQCE PGWGGTNCSS ACDGDHWGPH CTSRCQCKNG ALCNPITGAC
HCAAGFRGWR CEDRCEQGTY GNDCHQRCQC QNGATCDHVT GECRCPPGYT GAFCEDLCPP
GKHGPQCEQR CPCQNGGVCH HVTGECSCPS GWMGTVCGQP CPEGRFGKNC SQECQCHNGG
TCDAPTGQCH CSPGYTGERC QDECPVGTYG VLCAETCQCV NGGKCYHVSG TCLCEAGFAG
ERCEARLCPE GLYGIKCDKQ CPCHLDNTHS CHPMSGECAC KPGWSGLYCN ETCSPGFYGE
ACQQICSCQN GADCDSVTGK CTCAPGFKGI DCSTPCPLGT YGINCSSRCG CKNDAVCSPV
DGSCTCKAGW HGVDCSIRCP SGTWGFGCNL TCQCLNGGAC NTLDGTCTCA PGWRGEKCEL
PCQDGTYGLN CAERCDCSHA DGCHPTTGHC RCLPGWSGVH CDSVCAEGRW GPNCSLPCYC
KNGASCSPDD GICECAPGFR GTTCQRICSP GFYGHRCSQT CPQCVHSSGP CHHITGLCDC
LPGFTGALCN EVCPSGRFGK NCAGICTCTN NGTCNPIDRS CQCYPGWIGS DCSQPCPPAH
WGPNCIHTCN CHNGAFCSAY DGECKCTPGW TGLYCTQRCP LGFYGKDCAL ICQCENGADC
DHISGQCTCR TGFMGRHCEQ KCPAGTYGYG CRQICDCLNN STCDHITGTC YCSPGWKGAR
CDQAGVIIVG NLNSLSRTST ALPADSYQIG AIAGIIILVL VVLFLLALFI IYRHKQKGKE
SSMPAVTYTP AMRVINADYT ISGTLPHSNG GNANSHYFTN PSYHTLTQCA TSPHVNNRDR
MTVTKSKNNQ LFVNLKNVNP GKRGPVGDCT GTLPADWKHG GYLNELGAFG LDRSYMGKSL
KDLGKNSEYN SSNCSLSSSE NPYATIKDPP VLIPKSSECG YVEMKSPARR DSPYAEINNS
TSANKNVYEV EPTVSVVQGV FSNNGHLTQD PYDLPKNSHI PCHYDLLPVR DSSSSPKQED
SGGSSSSSSS SSE
//
