ID A0A091EE23_CORBR Unreviewed; 726 AA.
AC A0A091EE23;
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:KFO56208.1};
DE Flags: Fragment;
GN ORFNames=N302_03024 {ECO:0000313|EMBL:KFO56208.1};
OS Corvus brachyrhynchos (American crow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC Corvus.
OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO56208.1, ECO:0000313|Proteomes:UP000052976};
RN [1] {ECO:0000313|EMBL:KFO56208.1, ECO:0000313|Proteomes:UP000052976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO56208.1};
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; KK718434; KFO56208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091EE23; -.
DR STRING; 85066.A0A091EE23; -.
DR Proteomes; UP000052976; 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; 3.
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:KFO56208.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052976};
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 157..205
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 222..333
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 357..474
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 499..612
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 641..726
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 162..188
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 176..203
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO56208.1"
FT NON_TER 726
FT /evidence="ECO:0000313|EMBL:KFO56208.1"
SQ SEQUENCE 726 AA; 82535 MW; 5ED219F8025435CE CRC64;
YCILTISYVL FCFTDIETFL LYNKFNKLCL EASIAQSVRT ATCNQDNESQ KFRWITDHQL
MSVKLKLCLG VSLKKDQAMV TLYPCNQKSE LQWWECRNES LLAIQGEDLF FSPGNEEHEN
VLLKKELSAK NKWNIYGAMD VLCSQGYEET FTLLGNAFGA PCVFPFMYKE QWWAECTAAG
RTDGWLWCAT TADYDTDQRY GLCPSRDTDS TWTTDLSTNV HYQINFDSAL TWHQARRSCQ
QQNAELLSIT DIHEQTYLKE LTEGTDSALW IGLNRLDLTS GWEWTGGSPF QYLNWAPGSP
SPESGKLCAV LNPETKAKWQ NWECDQKLGY ICKKRNFTLV PSGDTGPVTC PDGWVPYVDH
CYKIFRDSKG WEGALTSCQK EGSHLASIQS LEEHSFVVSE LGYKPTDKLW IGLNDRKVQM
YFEWSDGTPV TYTKWHLGEP STTNNRPEDC VLIKGQNGYW ADHICEKKIG YICKRKATSQ
IAGEKEITEA GCKKGWRRYG NYCYFIGHVP AIFSEANTTC EGEEGYLATV ESRYEQAYLT
SLVGLRPEKY FWLGLSDMQD QGTFSWANGE AVSFTHWDAG MNKPGCVAMR TGTAAGLWDV
LDCEIKQKYI CKQWAKGATV PPIPTTALVP ACPEGWVSNH HRSSCFKCFC RSKIRKKSWF
EALDFCRQIG GDLVAINTKE EIPLVNQAMS DTHCMFETFW LGIFSLNPDE GFAWSDGSPV
SILIFH
//