ID A0A2K6NQM6_RHIRO Unreviewed; 969 AA.
AC A0A2K6NQM6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Multiple EGF like domains 11 {ECO:0000313|Ensembl:ENSRROP00000006572.1};
GN Name=MEGF11 {ECO:0000313|Ensembl:ENSRROP00000006572.1};
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:ENSRROP00000006572.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000006572.1}
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 RefSeq; XP_010361899.1; XM_010363597.1.
DR AlphaFoldDB; A0A2K6NQM6; -.
DR Ensembl; ENSRROT00000028765.1; ENSRROP00000006572.1; ENSRROG00000025747.1.
DR GeneID; 104662569; -.
DR CTD; 84465; -.
DR GeneTree; ENSGT00940000155333; -.
DR OMA; PACNINC; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
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; IPR002049; LE_dom.
DR InterPro; IPR042635; MEGF10/SREC1/2-like.
DR PANTHER; PTHR24043:SF7; MULTIPLE EGF LIKE DOMAINS 11; 1.
DR PANTHER; PTHR24043; SCAVENGER RECEPTOR CLASS F; 1.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF00053; Laminin_EGF; 7.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 17.
DR SMART; SM00180; EGF_Lam; 16.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 11.
DR PROSITE; PS50027; EGF_LAM_2; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
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 774..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..98
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 106..141
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 149..184
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 192..227
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 235..270
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 287..330
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 324..359
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 367..402
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 415..445
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 496..531
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 584..619
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 675..705
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 678..719
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 88..97
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 131..140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 174..183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 217..226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 260..269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 306..315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 349..358
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 392..401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 435..444
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 521..530
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 609..618
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 695..704
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 969 AA; 101467 MW; 5E9B46A88E0E7ABF CRC64;
MHTPSIRSIT HDAQTSSTGS SAPGTALCTE ECVHGRCVSP DTCHCEPGWG GPDCSSGCDS
DHWGPHCSNR CQCQNGALCN PITGACVCAA GFRGWRCEEL CAPGTHGKGC QLPCQCRHGA
SCDPRTGECL CAPGYTGVYC EELCPPGSHG AHCELRCPCQ NGGTCHHITG ECACPPGWTG
AVCAQPCPPG TFGQNCSQDC PCHHGGQCDH VTGQCHCTAG YMGDRCQEEC PFGTFGFQCS
QRCDCHNGGQ CSPTTGACEC QPGYKGPRCQ ERLCPEGLHG PGCTLPCPCD ADNTISCHPV
TGACACQPGW SGHHCNESCP AGYYGDGCQL PCTCQNGADC HSITGGCTCA PGFMGEVCAV
SCAAGTYGPN CSSICSCNNG GTCSPVDGSC TCKEGWQGLD CTLPCPSGTW GLNCNESCTC
ANGAACSPTD GSCSCTPGWL GDTCELPCPD GTFGLNCSEH CDCSHADGCD PITGHCCCLA
GWTGIHCDST CPPGRWGPNC SVSCSCENGG SCSPEDGSCE CAPGFQGPLC QRICAPGFYG
HSCAQPCPLC VHSSGPCHHV SGVCECLPGF SGALCNQVCA GGHFGQDCAQ LCSCANNGTC
SPIDGSCQCF PGWIGKDCSQ ACPPGFWGPA CFHTCSCHNG ASCSAEDGAC HCTPGWTGLF
CTQRCPAAFF GKDCGRVCQC QNGASCDHIS GKCTCRTGFT GQHCEQRCAP GTFGYGCQQL
CECMNNSTCD HVTGTCYCSP GFKGIRCDQA ALMMEELNPY TKISPALGAE RHSVGAVTGI
MLLLFLIVVL LGLFAWHRRR QKEKGRDLAP RVSYTPAMRM TSTDYSLSGA CGMDRRQNTY
IMDKGFKDYM KESVCSSSTC SLNSSENPYA TIKDPPILTC KLPESSYVEM KSPVHMGSPY
TDVPSLSTSN KNIYEVEPTV SVVQEGRGHN SSYIQNPYDL PRNSHIPGHY DLLPVRQSPA
NGPSQDKQS
//
