ID A0A091NUJ3_HALAL Unreviewed; 1330 AA.
AC A0A091NUJ3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Macrophage mannose receptor 1 {ECO:0000313|EMBL:KFP96360.1};
DE Flags: Fragment;
GN ORFNames=N329_07143 {ECO:0000313|EMBL:KFP96360.1};
OS Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Haliaeetus.
OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFP96360.1, ECO:0000313|Proteomes:UP000054379};
RN [1] {ECO:0000313|EMBL:KFP96360.1, ECO:0000313|Proteomes:UP000054379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFP96360.1};
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; KK641665; KFP96360.1; -; Genomic_DNA.
DR Proteomes; UP000054379; 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; 8.
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; 8.
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: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; 8.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00013; FNTYPEII.
DR PRINTS; PR01504; PNCREATITSAP.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 8.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 3.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
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:KFP96360.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054379};
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 138..186
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 198..314
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 339..456
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 480..595
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 624..744
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 772..888
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 916..1051
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1073..1184
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1213..1330
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 143..169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 157..184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP96360.1"
FT NON_TER 1330
FT /evidence="ECO:0000313|EMBL:KFP96360.1"
SQ SEQUENCE 1330 AA; 150363 MW; 78BF00F8F275C4AA CRC64;
LLIYNEDTKL CLTAQSSHAV TTASCKKNTE LQKFRWVSAH QVMSVAFAQC LGVPYKQKQA
KISLYPCNNK SEFQKWECRN ATLAIQGEEL FLSAGKRKDD NIVLNTGSAM MNKWKIYGTM
DDLCSRGHGD LFTLLGNANG AACAFPFQLS GKWYAGCTAA GRSDGLLWCA TTPDFDADHL
YGFCPTGNND RFWSTDPLTG TYYQINYQSA LTWHQARKSC QQQNAELLSV TEIHEQMYLR
DLIDSKRSSL WIGLNSLNLK SGWQWSGGIP FRYFNWAPGS PEPEPEKLCA VLNPRRDAKW
ENQPCELKVG YICKKENSTL DPFILPSEPV KCPEGWLHYG DHCFMVHRDP RVWREALISC
NESNGNLASI HNPEEHSFIL SQLGYKAVDE LWIGLNDLNT QMYFEWSDGT PVTYTKWLPG
EPTHAINGQE DCVIMAGEDG YWADSACDRK LGYICRRDPL QGVSGTAKTD PACLKGWERH
GFYCYLVGHT SVTFSEAKKT CERSSGYLTS IRDRYEQAYL TSLVGLSSEK YFWIGLSDTE
EQGMFKWVTG EGVLYTNWNA AMPGNEAGCV ALRTGNAAGL WDVQNCEVKA KFLCKKLAEK
ITLPLAPETV SDSKCPLGWD ISNSTNSCFR AFVREENQKK TWLEARDFCR EIGGDLAAIT
SEEEQTVIEN LIIKKSPSSQ PFWIGLQCLD PDGGLSWSDG SPVNYKKNGY FYNTAFEYCG
AISEESSMSW IEVHCEYSHN WICEIKKGTP LKPEPQGPSA EYEVTEDGWI IKGDKQYFFS
TEKTSMEKAR TFCRNNHGDL ATIGSNSERK FLWKRILKNG KLKSYLIGLI QNADQQFSWM
DGSPVHYAAW AQGEPNFADA QENCVVLNKN DGLWNDVNCG FSNGYICERH RSFINATLPS
AVPSPPGGCP EDWLLFKNKC YKFFGSSYEY WHTARRNCMS LGGNLASIHN EQVQAFLTYH
LKDVSNDPWI GLNDILSELN FVWTDGSAVS YTNWAPDSPK LVEPVLYPSL HPEDGHNLQQ
FDCVSLKRGH ADDTGKWNNE ECFKSRGYIC QKTSDPELFN SSATVLDFAL YHSGGISYSV
TPSKMNWEEA QKNCNNNASE LASILDPYSQ ALLFLLAQEY GEPLWIGLNS NATNGKYQWI
DRWRLAYSKW SSGEPKQTLA CVYLDTDGTW KTASCTENLF SVCKKSDVKA PTEPPQLPGK
CPETRGHKSW IPFHRHCYYF EASRKRSWSQ AHQECARLAA NLVSVGDYTE ANFLSDTIKI
LHGKSPNFWI GLKKNDRGQW VWTDKSAMDF VNWQMGEPSN KRHKECGEVY ASSGYWNTNV
CSFKKGYICK
//
