ID A0A6P3H2N4_BISBB Unreviewed; 1044 AA.
AC A0A6P3H2N4;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Multiple epidermal growth factor-like domains protein 11 {ECO:0000256|ARBA:ARBA00073805};
GN Name=MEGF11 {ECO:0000313|RefSeq:XP_010832845.1};
OS Bison bison bison (North American plains bison).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bison.
OX NCBI_TaxID=43346 {ECO:0000313|Proteomes:UP000515208, ECO:0000313|RefSeq:XP_010832845.1};
RN [1] {ECO:0000313|RefSeq:XP_010832845.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_010832845.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: May regulate the mosaic spacing of specific neuron subtypes
CC in the retina through homotypic retinal neuron repulsion. Mosaics
CC provide a mechanism to distribute each cell type evenly across the
CC retina, ensuring that all parts of the visual field have access to a
CC full set of processing elements. {ECO:0000256|ARBA:ARBA00057060}.
CC -!- SUBUNIT: Homomer. Does not interact with MEGF10.
CC {ECO:0000256|ARBA:ARBA00065503}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000256|ARBA:ARBA00023768}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00023768}.
CC -!- SIMILARITY: Belongs to the MEGF family.
CC {ECO:0000256|ARBA:ARBA00038377}.
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_010832845.1; XM_010834543.1.
DR AlphaFoldDB; A0A6P3H2N4; -.
DR GeneID; 104984683; -.
DR KEGG; bbis:104984683; -.
DR CTD; 84465; -.
DR OrthoDB; 409374at2759; -.
DR Proteomes; UP000515208; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR FunFam; 2.170.300.10:FF:000007; multiple epidermal growth factor-like domains protein 10; 1.
DR FunFam; 2.10.25.10:FF:000114; Multiple epidermal growth factor-like domains protein 11; 1.
DR FunFam; 2.170.300.10:FF:000005; multiple epidermal growth factor-like domains protein 11; 1.
DR FunFam; 2.170.300.10:FF:000006; Multiple epidermal growth factor-like domains protein 11; 1.
DR FunFam; 2.170.300.10:FF:000015; multiple epidermal growth factor-like domains protein 11 isoform X3; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 6.
DR InterPro; IPR000742; EGF.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR057138; EGF_PEAR1L-like.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR042635; MEGF10/SREC1/2-like.
DR PANTHER; PTHR24043:SF9; MULTIPLE EGF LIKE DOMAINS 11; 1.
DR PANTHER; PTHR24043; SCAVENGER RECEPTOR CLASS F; 1.
DR Pfam; PF00053; EGF_laminin; 6.
DR Pfam; PF23301; EGF_PEAR1L; 1.
DR Pfam; PF23106; EGF_Teneurin; 1.
DR Pfam; PF12661; hEGF; 4.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 15.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 11.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS51041; EMI; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000515208};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1044
FT /note="Multiple epidermal growth factor-like domains
FT protein 11"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027595240"
FT TRANSMEM 849..871
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..101
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 143..173
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 181..216
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 224..259
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 267..302
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 310..345
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 399..434
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 442..477
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 490..520
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 571..606
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 659..694
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 750..780
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 753..794
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1009..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1044
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 163..172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 206..215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 249..258
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 292..301
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 335..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 424..433
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 467..476
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 510..519
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 596..605
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 684..693
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 770..779
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1044 AA; 110637 MW; 6CF760207D2C6DC9 CRC64;
MVLSAAGLIV GSLLQIVLSL NPEDPNVCSH WESYAVTVQE SYAHPFDQIY YTRCTDILNW
FKCTRHRISY KTAYRRGLRT MYRRRSQCCP GYYENGDFCI PLCTEECVHG RCVSPDTCHC
EPGWGGPDCS SGCDSDHWGP HCSNRCQCQN GALCNPITGA CVCAAGFRGW RCEELCAPGT
HGKGCQLLCQ CRHGASCDPQ TGECLCAPGY TGVYCEELCP PGSHGAHCEL RCPCQNGGTC
HHITGECACP PGWTGAVCAQ PCPPGTFGQN CSQDCPCHHG GQCDHVTGQC HCTAGYMGDR
CQEECPLGTF GFQCSQRCDC HNGGQCSPTS GACECEPGYK GPRCQERLCP EGLHGPGCSL
PCPCDADNTI SCHPVTGACT CQPGWSGYHC NESCPVGYYG DGCQLPCTCQ NGADCHSITG
SCTCAPGFMG EVCAAPCAAG TYGSNCSSVC SCNNGGTCSP VDGSCTCKEG WQGLDCTLPC
PSGTWGLNCN ESCACANGAA CSPTDGSCSC TPGWLGDTCE LPCPDGTFGL NCSERCDCSH
ADGCDPVTGH CCCLAGWTGI HCDSTCPPGR WGPNCSVSCS CENGGSCSPE DGSCECAPGF
RGPLCQRVCA PGFYGHGCTQ PCPLCVHSSG PCHHVSGICE CLPGFSGALC NQVCAGGHFG
QDCAQLCSCA NNGTCSPIDG SCQCFPGWIG KDCSQACPPG FWGPACFHTC SCHNGASCSA
EDGACHCTPG WTGLFCTQRC PAAFYGKDCG RVCQCQNGAS CDHISGKCTC RTGFTGEHCE
QRCAPGTFGY GCQQLCECMN NATCDHVTGT CYCSSGFKGI RCDQAALMME ELNPYTKISP
ALGAERHSVG AVTGIVLLLF LIVVLLGLFA WRRRRQKEKG RDLAPRVSYT PAMRMTSTDY
SLSGACGMDR RQNTYVMDKG FKDYMKESVC SSSTCSLNSS ENPYATIKDP PILTCKLPES
SYEEMKSPVH RGSPYTDVPS LSTSNKNIYE VEPTVSVVQE GRGCNSSYIQ NPYDLPRNSH
IPGHYDLLPV RQSPASGPSQ DKQS
//
