ID A0A091GL50_9AVES Unreviewed; 720 AA.
AC A0A091GL50;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Macrophage mannose receptor 1 {ECO:0000313|EMBL:KFO74797.1};
DE Flags: Fragment;
GN ORFNames=N303_04169 {ECO:0000313|EMBL:KFO74797.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO74797.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO74797.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO74797.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL447554; KFO74797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GL50; -.
DR STRING; 55661.A0A091GL50; -.
DR Proteomes; UP000053760; 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; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 4.
DR PROSITE; PS00023; FN2_1; 1.
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:KFO74797.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
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 148..196
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 215..326
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 354..471
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 496..611
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 640..720
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 153..179
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 167..194
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO74797.1"
FT NON_TER 720
FT /evidence="ECO:0000313|EMBL:KFO74797.1"
SQ SEQUENCE 720 AA; 82554 MW; 1824422B10F99524 CRC64;
IFCLTDTSIF LIYNEDHKRC VLAQSSNSVT TAPCVQENES QKFRWVSDHQ LMSIAFKLCL
GVPSKKDWVP ITLYPCDKAS ELQRWECRNE TLFAIQGEDL FFNYGNRQER NIMLYKGSGL
WSRWKVYGTT DDLCSRGYED TYTVKGNANG APCVFPFKFG DKWYADCIDA GRSDGWFWCG
TTSDFNVDKM YGFCPQKSNS INLLWNIDPL TNVQYQINSD ASLKWHQARK SCQQQKADLL
SITELHEQTY LTGLTGRLSS ALWIGLNSLN FNSGWQWVGG APFRYLNWVP GHPSPEPGKI
CAALNPGKGA KWENRECDQK LGYICKRGNA TLSSFIIPTD TNVPIRCPDQ WMSYAGHCYI
IHRDPKIWKD ALTSCRKEDG DLASIHNVEE YSFVISQLGY QPADELWIGL NDLKVQMYFE
WSDGTPVTYT KWLRGEPTHA NNRQEDCVVM KGKDGFWADH SCEKKIAYIC KRKPVSEVPT
EEETIDMSCQ RGWKRHGFYC YFIGNTFVSF SEANQTCVRH QAFLATIEDR YEQAYLTSLI
GLRTERYFWI GLSDVEEKGT FKWANGESVL FTHWNSEMPG RKRGCVAMRT GIAGGLWDVI
KCEEKAKFLC KMWAEGVTVP PVPTTTPVPR CPEGWDSNNR ISFCFKPFAR GEQKKTWLES
QEFCRAIGGD LASINGKEEQ YVIWRSIANN GYYHQHFWMG LYYLNPDDGF VWSDGSPVSV
//
