ID A0A091KNU5_9GRUI Unreviewed; 1332 AA.
AC A0A091KNU5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Macrophage mannose receptor 1 {ECO:0000313|EMBL:KFP40960.1};
DE Flags: Fragment;
GN ORFNames=N324_09051 {ECO:0000313|EMBL:KFP40960.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP40960.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP40960.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP40960.1};
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; KK748289; KFP40960.1; -; Genomic_DNA.
DR Proteomes; UP000053330; 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 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; 2.
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:KFP40960.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053330};
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 342..459
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 483..598
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 627..746
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 774..890
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 918..1053
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1075..1186
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1215..1332
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:KFP40960.1"
FT NON_TER 1332
FT /evidence="ECO:0000313|EMBL:KFP40960.1"
SQ SEQUENCE 1332 AA; 150932 MW; 534EC601570A0C4D CRC64;
FLIYNEDTKL CLIAQSPHVV KTAACNKNSE LQKFRWVSDH QVMSMAFAQC LGVPYKQNQA
KISLYPCNKK SKFQKWECRN ATLAIPGEDL FLSAGKRKED SIVLNTGSET MNKWKIYGTM
DDLCSKGHED VFTLLGNANG APCAFPFQLS GKWHAGCTAA GRSDGLLWCA TTPNFDADHL
YGFCPTGNND RFWSADPLTG TYYQINHQSA LTWHQARKSC QQQNAELLSI TEIHEQIYLR
DLIDSKRSSL WIGLNSLNLN RGWQWSGGIP FRYFNWAQGS PEPEPEKLCA VLNPRRDAKW
ENQPCEMKVG YICKKENSTL DPFILPSGGA EPAKCPEGWL PYGDHCFMVH RDPRVWREAL
ISCNDSNGNL ASIHNPEEHG FILSQLGYKA MDALWIGLND LSTQMYFQWS DGTPVTYTRW
LPGEPTHAIN GQEDCVIMAG EDGYWADSTC DRKLDNICRR DPLQGGSGTV KTDPVCLKGW
KRHGFYCYLV GHTSVTFSEA KKTCERSNGY LTSVGDRYEQ AYLTSLVGLS SEKYFWIGLS
DTEEQGMFKW ATGEGVLYTN WNAAMPGNEA GCVALRTGNA AGLWDVQNCE VKAKFLCKKL
AEKITPPLTP ETASDSKCPL GWDTSNSTNS CFRGFVREEN QKKTWFEARD FCREIGGDLV
AIRSKEEQIV IENLILKKSP SSQPFWIGLQ CLDPDGGLSW SDGSPVNYKK NYFYNTAFEY
CGAIGEEHST SWIKVHCEYS HNWICEIKKG IPLKPEPLGP STTYEVTEDG WIIKGDKQYF
FSTEKTSMEK ARMFCKSNHG DLATIGNNSE RKFLWKCILK NGKLESYLIG LIRNADQQFS
WMDGSPVHYA AWARDEPNFA DAQENCVVLN KNDGLWNDVS CGFSNGYICE RHRSFINATL
PSEEPPPLGG CPEDWLLFKN QCYKFFGSSY EYWYTARRTC MNLGGNLASI HNEQVQAFLT
YHLKDVSNDP WIGLNDILIE LNFVWADGSA VSYTNWAPDS PKLVEPVLYP SLHPEDGQNL
QQFDCVSLKR GHADDTGKWN NEECYKSRGY ICQKNSDPEL FKPSATALDF AFDRSGGISY
FVSRSKMNWE EAQKNCNNNA SELASILDPY SQALLFLLAQ EYSEPLWIGL NSNMTNGKYQ
WIDRWRLSYS KWSSGEPKQT LACVYLDTDG TWKTASCKEK LFYACKKSDV MAPTEPPQLP
GKCPESRGHK SWIPFHGHCY YFEASRKRSW SQAHQECARL AANLVSVGDY TEANFLSDTI
KILHGKSPNF WIGLKENDRG QWVWTDKSAM DFVNWQMGEP SNKRHKECGE VCALSGYWNT
NICSFKKGYI CK
//
