ID A0A087QV86_APTFO Unreviewed; 727 AA.
AC A0A087QV86;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Macrophage mannose receptor 1 {ECO:0000313|EMBL:KFM05140.1};
DE Flags: Fragment;
GN ORFNames=AS27_03766 {ECO:0000313|EMBL:KFM05140.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM05140.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM05140.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM05140.1};
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; KL225943; KFM05140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QV86; -.
DR STRING; 9233.A0A087QV86; -.
DR Proteomes; UP000053286; 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:KFM05140.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
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 149..197
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 214..325
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 349..473
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 498..613
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 642..727
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 154..180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 168..195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM05140.1"
FT NON_TER 727
FT /evidence="ECO:0000313|EMBL:KFM05140.1"
SQ SEQUENCE 727 AA; 82609 MW; D6BFAF3A4C03E737 CRC64;
VLFCFTDIET FLIYNKVNKL CLQVSIAQSV RTATCHQDNE SQKFRWITDH QLMSVRLNLC
LGVPSKKDQA VITLYPCNRT SELQWWECRN ESLLAIQGED LFFSPGNEEH DNVLLKKGVS
AKDKWKIYGA VDVLCSRGYE ETFTLLGNAF GAPCVFPFMY NKQWYAKCTD AGRSDGWLWC
ATTADYDTDQ RYGFCPSKDK DTTWTTDLLT NVHYQINSES ALMWHQARKS CQQQNAELLS
ITDIHEQTYL KDLTEGTDSA LWIGLNRLDL RSGWEWTGGS PFRYLNWAPG SPSPESGKLC
VVLNPETKAK WQNWECDQKL GYICKKRNFT LVPSGDIGPV TCPDGWVPYI DHCYKIFRET
KAWEEALTSC QKEGSHLASI QSLEEHSFMV SRLGYILCFH VLEPTDKLWI GLNDHKVQMY
FEWSDGTPVT YTKWHLGEPS TTNNRPEDCV LIKGQNGYWA DYVCEKKAGY ICKRKPVSQI
TGEKEITDAG CKKGWRRYGT YCYFIGHVPA TFSEANTTCE GEKGYLATVE SRYEQAYLTS
LVGLRPEKYF WLGLSDVEDQ GTFRWANGEA VSFTHWGAAM PGSNPGCVAM RTGTAAGLWD
VLDCETKQKY ICKQWAKSAT APPIPTTALV PTCPEGWVSN NRSSSCFKCF CRSNIKKKSW
LEARDFCREI GGDLVTINSK EEIPLLIKAM YETHCSFQEV WLGIVSLNPD EGFAWSDGSP
VSILIFH
//
