ID A0A093HNQ5_STRCA Unreviewed; 723 AA.
AC A0A093HNQ5;
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:KFV80642.1};
DE Flags: Fragment;
GN ORFNames=N308_12506 {ECO:0000313|EMBL:KFV80642.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV80642.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV80642.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV80642.1};
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; KL206260; KFV80642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HNQ5; -.
DR STRING; 441894.ENSSCUP00000010889; -.
DR Proteomes; UP000053584; 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:KFV80642.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
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:KFV80642.1"
FT NON_TER 723
FT /evidence="ECO:0000313|EMBL:KFV80642.1"
SQ SEQUENCE 723 AA; 82757 MW; D983E25B92B34ECF CRC64;
VFCPTDTSIF LIYNEDHKRC VLAQSSSSVT TAPCVQDNES QKFRWVSDHQ LMSIALKLCL
GVPSKKDWVP ITLYPCDKAS ELQRWECRNE TLFAIQGEDL FFNYGNRQER NIMLYKGSGL
WSRWKVYGTT DDLCSRGYED TYTVKGNANG APCVFPFKFS GKWYADCTDA GRSDGWFWCG
TTSDFDVDKM YGFCPLKFNS LDLLWNTDPL TNVQYQINSE AALKWHQARK SCQQQKAELL
SITELHEQTY LTGLTGRLSS ALWFGLNSLN FNSGWQWVGG APFRYLNWVP GNPSPEPGKI
CAALNPGKGA KWENRECDQK LGYICKRGNA TLESFIISAE TNVPVRCPDQ WMSYAGHCYI
IHRDPKIWKD ALTSCRKEDG DLASIHNVEE YSFVISQLGY QPDDELWIGL NDLKVQMYFE
WSDGTPVTYT KWLRGEPTHA NNRQEDCVIM RGKDGFWADH SCEKKIGYVC KRKPMSEAPT
EEETIDMGCQ RGWKRHGFYC YFIGNTFVSF SQANQTCERH QAFLATIEDR YEQAYLTSLV
GLRTEKFFWI GLSDVEEKGT FKWTNGESVL FTHWNSEMPG RKPGCVAMRT GIAGGLWDVI
KCEEKAKFIC KVWAEGVTPP PIPTTTPIPR CPEGWDSNSR ISFCFKPFSR GEQKKTWLES
QEFCRAIGGD LASINGKEEQ YVIWRSIANN GYYHQHFWMG LYYLNPDDGF VWSDGSPVSG
LIF
//
