ID A0A0A0AM65_CHAVO Unreviewed; 724 AA.
AC A0A0A0AM65;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Macrophage mannose receptor 1 {ECO:0000313|EMBL:KGL95007.1};
DE Flags: Fragment;
GN ORFNames=N301_01539 {ECO:0000313|EMBL:KGL95007.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL95007.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL95007.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL95007.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL872299; KGL95007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AM65; -.
DR STRING; 50402.A0A0A0AM65; -.
DR Proteomes; UP000053858; 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:KGL95007.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
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..719
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:KGL95007.1"
FT NON_TER 724
FT /evidence="ECO:0000313|EMBL:KGL95007.1"
SQ SEQUENCE 724 AA; 82989 MW; 1931B17F6E555B06 CRC64;
VFCLTDTSIF LIYNEDHKRC VLAQSSNSVT TAPCVQENES QKFRWVSDHQ LMSIAFKLCL
GVPSKKDWVP ITLYPCDKAS ELQRWECRNE TLFAIQGEDL FFNYGNRQER NIMLYKGSGL
WSRWKVYGTT DDLCSRGYED TYTVKGNANG APCVFPFKFG DKWYADCTDA GRSDGWFWCG
TTSNFDVDKM YGFCPLKFNS IDLLWNTDPL TNVQYQINSE AALKWHQARK SCQQQKAELL
SITELHEQTY LTGLTGRLSS ALWFGLNSLN FNSGWQWVGG APFRYLNWVP GHPSPEPGKI
CAALNPGKGA KWENRECDQK LGYICKRGNT TLESFIIPTE TNVPTRCPDQ WMSYAGHCYI
IHRDPKIWKD ALTSCRKEDG DLASIHNVEE YSFVISQLGY QPADELWIGL NDLKVQMYFE
WSDGTPVTYT KWLRGEPTHA NNRQEDCVVM KGKDGFWADH SCEKKIGYIC KRKPMAEAST
EEETIDVGCQ RGWKRHGFYC YFIGNTFLSF SQANQTCGKH QAFLATVEDR YEQAYLTSLV
GLRTERYFWI GLSDVEEKGT FKWANGESVL FTHWNSKMPG RKPGCVAMRT GISGGLWDVI
KCEEKAKFLC KVWAEGVTLP PVPTTTPIPR CPEGWDSNNR ISFCFKPFSR GDQKKTWLDS
QEFCRSIGGD LASINGKEEQ YVIWHSIANN GYYHQHFWMG LYYLNPDDGF VWSDGSPVSD
LIFY
//
