ID A0A091UA06_PHALP Unreviewed; 700 AA.
AC A0A091UA06;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Macrophage mannose receptor 1 {ECO:0000313|EMBL:KFQ70858.1};
DE Flags: Fragment;
GN ORFNames=N335_05717 {ECO:0000313|EMBL:KFQ70858.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ70858.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ70858.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ70858.1};
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; KK443236; KFQ70858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091UA06; -.
DR PhylomeDB; A0A091UA06; -.
DR Proteomes; UP000053638; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR013806; Kringle-like.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR22803:SF124; C-TYPE LECTIN DOMAIN FAMILY 19 MEMBER A-RELATED; 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; SSF57440; Kringle-like; 1.
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:KFQ70858.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053638};
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 146..194
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 213..324
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 352..468
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 485..596
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 625..700
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 151..177
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 165..192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ70858.1"
FT NON_TER 700
FT /evidence="ECO:0000313|EMBL:KFQ70858.1"
SQ SEQUENCE 700 AA; 78705 MW; 4C083D36A06F7250 CRC64;
FYFIDSGIFS IYNEDSKLCA QAQNSSSVVT TACDEHNEFQ KFRWVSATQL LSVALKLCLG
VLTKDDEAAI TLESCNRTNE LQWWECRNEM VATHGKDLFF NYGKGKGKKI RLSKGSGKGS
RWKIHGTADS VCSLRYEDIY TLGGNAFGAP CVFPFKFDGK WYAECIRRSD NSGSLWCATS
SDFDKDQLFG NCPLKDTIHN DLWKTNPVTE THYQINSESL LTWHQARKSC QQQGAELLSV
TDLREEMYLL GLTSDMGVNA KLWTGLFSAL DSGWRWIGGS PFRYLNWAPG NPSVESGKIC
GTFQGRNGKW ENQLCDRKLG YICQKRNSSL DSSTIASGDL KPFKCPREWV AYAGHCYRIF
RTPKIWKAAQ SSCRKEDGDL ASIHNIEEYS FTVSQLGYKP DDELWIGLND FRVQMYFEWS
DGTPVTYTKW HHGEPTHTRN KADCIVMKGE DGSWADSACE TKLGYVCKRK PLAEGSGEDE
GWTKHGFYCY SVGQLPATFS EAKQICEENK GYLATVTDRY EQAFLTSVIG FNPAKYFWIG
LSDAEEQGTF SHLSIRFKNF IFHEGRESGC VAMITGTSAG LWDILNCEET NMFLCKQLVE
GVTPPPPPTT TPLLACPEGW QSVPQSSSCF KVGREKMQTW FGARDFCRAI GGDLACIHSE
EEQNLIAGLK RDYLHLSYWM GLSALDSDSG FVWSDGSPVS
//
