ID A0A674MDR7_TAKRU Unreviewed; 1126 AA.
AC A0A674MDR7;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE SubName: Full=Multiple EGF like domains 11 {ECO:0000313|Ensembl:ENSTRUP00000059557.1};
GN Name=megf11 {ECO:0000313|Ensembl:ENSTRUP00000059557.1};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000059557.1, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000059557.1, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000059557.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSTRUP00000059557.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
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_029698208.1; XM_029842348.1.
DR RefSeq; XP_029698209.1; XM_029842349.1.
DR AlphaFoldDB; A0A674MDR7; -.
DR Ensembl; ENSTRUT00000087418.1; ENSTRUP00000059557.1; ENSTRUG00000014394.3.
DR GeneID; 101072623; -.
DR GeneTree; ENSGT00940000155333; -.
DR InParanoid; A0A674MDR7; -.
DR OrthoDB; 409374at2759; -.
DR Proteomes; UP000005226; Chromosome 9.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:TreeGrafter.
DR FunFam; 2.170.300.10:FF:000002; Multiple epidermal growth factor-like domains 10; 1.
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 Gene3D; 2.10.25.140; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 5.
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; 3.
DR Pfam; PF23301; EGF_PEAR1L; 1.
DR Pfam; PF23106; EGF_Teneurin; 1.
DR Pfam; PF12661; hEGF; 5.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 15.
DR PROSITE; PS00022; EGF_1; 16.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 12.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1126
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025462713"
FT TRANSMEM 858..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..103
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 152..182
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 190..225
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 233..268
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 281..311
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 319..354
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 413..443
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 456..486
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 494..529
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 580..615
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 668..703
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 716..746
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 797..832
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1099..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 172..181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 215..224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 258..267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 301..310
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 344..353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 433..442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 476..485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 519..528
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 605..614
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 693..702
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 736..745
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 822..831
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1126 AA; 120245 MW; 5C60F5D1CC269706 CRC64;
MGFPVAIVAL LLVLLATGGW TLNPDDPNVC SHWESYAVTV QESYAHPFDQ IYYTRCTDIL
NWFKCTRHRI SYKTAYRRGV RTMYRRRSQC CPGYFESGDL CVPLCTEECV HGRCVSPDTC
QCEPGWGGLD CSSANTANGT GCESDFWGPH CSNRCQCQNG AKCNPITGAC VCTDGYQGWR
CEEPCEHGYY GKACQLSCQC LNGGTCIHVT GECICPPGYS GAFCGERCPS GSHGFHCEES
CPCQNGGTCH HITGDCSCPA GWTGSVCTQP CPLGKYGINC SKDCSCRNGG VCDHITGNCQ
CAAGFSGRRC QNDCPMGSFG LQCNQKCECQ NGAKCHHING ACLCETGFKG PNCQERFCPS
GLYGLICDKY CPCNSTNTVS CHPLSGECSC TGGWTGLYCN ETCPPGYYGE ACMVPCSCSN
GADCHPVTGA CVCAPGFMGE DCTTLCPPGL YGPGCMSTCS CHNHASCSPL NGSCLCREGW
QGVDCSIPCS SGTWGLGCNQ TCLCANGAAC DPIDGICTCS PGWRGQHCDE SCPDGTYGLE
CRERCDCSHA DGCDPTSGYC RCYPGWTGIH CDSVCPQGFW GPNCSFSCSC QNGGSCSPED
GTCVCAAGYR GTSCKRICSP GFYGHRCSQS CPQCVHSTGP CHHITGQCEC LPGFSGSLCN
QVCPSGRYGR ACTEVCLCSN NGTCNPIDGS CQCVPGWIGE DCSHACPSGH WGPDCLNSCN
CHNGAQCSAY DGECRCSPGW TGLYCTQRCP SGFYGRDCSE VCRCQNGADC DHSTGQCACR
TGFIGTSCDQ KCPAGTFGYG CQQLCECLNN ATCDYVTGTC YCSPGYKGIR CDQAALMMEE
LNPYTKISPA RGSERQSAGA VMGIIFLLLI IMAMLSLFVW YRQRQRDKGH ESQPTVSYSQ
AMHLTNTDYS LSECGSTVAM RTSVAEVNQS QGSCSSSAQC YQTVAQCNVS TISSKLDGNQ
TLKSGTLKSR NGSEWRAYCN LNDIDVQQGD TQTQRGTRKD YIKSSICSNS SCSLNSENPY
ATIRDPPALA CKHTENSYVE MKSPSHREVP FGGTATLLGG TGRNVYDVEP TVSVLQGPNG
MATGFSQSPY DIPRGTHIPG HYDILPMRHS PPHTPPPPPE SPSSLL
//
