ID A0A093PRB3_PHACA Unreviewed; 1046 AA.
AC A0A093PRB3;
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:KFW79378.1};
DE Flags: Fragment;
GN ORFNames=N336_11173 {ECO:0000313|EMBL:KFW79378.1};
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW79378.1, ECO:0000313|Proteomes:UP000053238};
RN [1] {ECO:0000313|EMBL:KFW79378.1, ECO:0000313|Proteomes:UP000053238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW79378.1};
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; KL415269; KFW79378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093PRB3; -.
DR Proteomes; UP000053238; 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; 6.
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; 6.
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; 6.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00034; CLECT; 6.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 6.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 3.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 6.
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:KFW79378.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053238};
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 137..185
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 197..313
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 341..458
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 482..597
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 626..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..1043
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 142..168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 156..183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW79378.1"
FT NON_TER 1046
FT /evidence="ECO:0000313|EMBL:KFW79378.1"
SQ SEQUENCE 1046 AA; 118259 MW; 750CDB154C4DE7D7 CRC64;
FLMYNEDTKL CLIAQSSHAV TTAVCNKNTE LQKFRWVPDH QVMSMAFAQC LGVPYKQNQA
KISLYPCNKK SEFQKWECRN ATLAIQGEDL FLSAGKNKEN IVLDIGSVMV NKWKVYGTMD
DLCSKGHEDL FTLLGNANGA PCVFPFQLSG KWHAGCTAAG RSDGLLWCAT TPNFDADHLY
GFCPAGNNDR FWSTDPLTGI SYQINYQSAL TWHQARKSCQ QQNAELLSIT EIHEQLYLRD
WIDSKRSSLW IGLNSLNLNS GWQWSGGVPF RYFNWALGSP EPEPEKHCAV LNPRRDAKWE
KQSCELKVGY ICKKENSTLD PFIIPSGDAE PVKCPEGWLP YGDHCFMVYR DPRVWREALI
SCNESNGNLA SIHNPEEHGF ILSQLGYESA DELWIGLNDL NTQMYFEWSD GTPVTYTKWL
PGEPTHAING QEDCVIMAGE DGYWADSACD RKLGYICRRD PVQGVSGTVK TDPACLKGWE
RHGFYCYLVG HISVTFSEAK KTCERSSGYL TSVGDRYEQA YLTSLVGLSS EKYFWIGLSD
TEEQGMFKWV TGEGVLYTNW NAAMPGNEAG CVALRTGNAA GLWDVQNCEV KAKFLCKKLA
EKITLPLTPE TVSDSKCPLG WDTSNSTNSC FRVFVREENQ KKTWFEARDF CREIGGDLAA
IRSEEEETVI ENLIIKKSPS SQPFWIGLQC LDPDHGLSWS DGSPVNYKKN HYFYNTAFEY
CGAISEEPPM SWIEVHCEYS HNWICEIKKG TPLKPEPLGP SAAYEVTEDG WILKGDKQYF
FSTEKTSMEK ARTFCRSSHG DLATIENSSE RKFLWKCILK KGKLESYLIG LIQNADRQFS
WMDGSPVHYA AWAQGEPNFA DAQENCVVLN KKDGLWNDVS CGFSNGYICE RHRSFIKAAL
PSEVPSPPGG CPQDWLLFKN QCYKFFGSSY EDWHTARRTC INLGGNLASI HNEQVQAFLT
YQLKDVSNDL WIGLNDILSE LNFVWTDGSA VSYTNWAPDS PKLVEPVLFH KQFDCVSLKR
GHADDTGKWK NEECYKSTGY ICQKNS
//
