ID A0A093GQS6_DRYPU Unreviewed; 715 AA.
AC A0A093GQS6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Macrophage mannose receptor 1 {ECO:0000313|EMBL:KFV69342.1};
DE Flags: Fragment;
GN ORFNames=N307_00616 {ECO:0000313|EMBL:KFV69342.1};
OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV69342.1, ECO:0000313|Proteomes:UP000053875};
RN [1] {ECO:0000313|EMBL:KFV69342.1, ECO:0000313|Proteomes:UP000053875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV69342.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL216401; KFV69342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093GQS6; -.
DR STRING; 118200.A0A093GQS6; -.
DR Proteomes; UP000053875; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 4.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 4.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR22803:SF104; MACROPHAGE MANNOSE RECEPTOR 1; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 4.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00013; FNTYPEII.
DR PRINTS; PR01504; PNCREATITSAP.
DR SMART; SM00034; CLECT; 4.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 4.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 4.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KFV69342.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053875};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 146..194
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 213..324
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 352..468
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 493..608
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 637..715
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 151..177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 165..192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV69342.1"
FT NON_TER 715
FT /evidence="ECO:0000313|EMBL:KFV69342.1"
SQ SEQUENCE 715 AA; 80026 MW; FBEE872D64789A5F CRC64;
FYFTDSGIFS LYNEDSKLCA EAQNSSSVIT TTCDEHNAFQ KFRWVSAVQL LSVALKLCLG
VFTKEEEAAI TLESCNRTNE LQWWECRNEM LTTHGKDLFF NYGKGKGKKI RLSKGSGRGS
RWKIRGTGES VCSQRYEDIF TLGGNAFGAP CVFPFKFNGR WHAECLPRAG DAGSLWCATT
SDFDKDQVFG SCPLKDIIHN KLWKTNPVTQ NHYQINAGAL LTWHQARKSC QQQNAELLSV
TDPREEMYLL GLTSDLGVNA NLWIGLFNAL DSGWRWTGGS PFRYLNWAPG SPSVESVKVC
GTFQGRNGKW ENLACNRKLG YICQKRNSSW DSSTIASGDL KPVKCPRGWV AYAGHCYRLY
RTPKIWKEAQ TSCRKEDGEL ASIHNVEEQS FTVSQLGYKP DDKLWIGLSD FRVPMYFEWS
DGTPVTYTKW HHREPAHTGD KADCILMKGQ DGSWADSPCE MKLGYLCKRK PLAGESGAGE
VTYPGCQKGW VKHGFYCYSL GQLPATFSEA KKICEENKGY LATVRDRYEQ AFLTSVIGFN
PAKYFWIGLS DTEEQGTFSW ANGDVVIFTH WNLGMPGGEP GCVAMVTGSS AGLWDVMNCE
ETNMFVCKQL VEGVTPPPPP TLPSLPPCPE GWKSVHSSSF CFKIFRGVRE KMQTWFGARD
FCRAIGGDLA CIHSEEEQKL IADLDRDYLH TSFWMGLSAL DSSGGFVWSD GSPVS
//
