ID A0A553R664_9TELE Unreviewed; 1239 AA.
AC A0A553R664;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Macrophage mannose receptor 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=DNTS_035477 {ECO:0000313|EMBL:TRY97664.1};
OS Danionella translucida.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danionella.
OX NCBI_TaxID=623744 {ECO:0000313|EMBL:TRY97664.1, ECO:0000313|Proteomes:UP000316079};
RN [1] {ECO:0000313|Proteomes:UP000316079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bolton {ECO:0000313|Proteomes:UP000316079};
RA Kadobianskyi M., Schulze L., Schuelke M., Judkewitz B.;
RT "Hybrid genome assembly and annotation of Danionella translucida.";
RL bioRxiv 0:0-0(2019).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TRY97664.1}.
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DR EMBL; SRMA01025215; TRY97664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553R664; -.
DR STRING; 623744.A0A553R664; -.
DR Proteomes; UP000316079; 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; 7.
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; 7.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
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; 7.
DR SMART; SM00034; CLECT; 7.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 7.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 7.
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|PROSITE-ProRule:PRU00479};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000316079};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1239
FT /note="Macrophage mannose receptor 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021982291"
FT TRANSMEM 1179..1199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 158..206
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 222..304
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 311..428
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 454..569
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 598..717
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 744..859
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 887..1002
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1033..1146
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 163..189
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 177..204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1239 AA; 142381 MW; 8ECD68EFC10BD38A CRC64;
MKITLVALLL VLDLSTCFAQ SGESFLIYNV ELNRCLAWDY MERLTHCDPF SHRQLFRWIS
KNRILNTNTK TCLGAGSKSV GRKMQLLRCD DSDLQKWECH GDGLLGLKNE TLYLSTDDSD
YLQLSKDTGK RSKWTIHGTQ NSICSRPYKE MYTIDGNAFG QPCNFPFLYK NTWYADCTTA
DKPNKRLWCA TETDYSLKER WGYCPTRQNT YWVKHPLTNI YYQLNGRSTL TWYQARMSCQ
QQGAELLSVV EPHEHTFVAG LVQRSQGSLW IGLNMLDTSS GWQWTNGQPL RYLKWLSVID
TGYCQSPWIP YSGSCYLLHR VKKSWRDARE TCLREGGDLI SILNVEEQSF AITQLGYMKI
DVLWIGFNDR KTQMFFEWSD QSSVQFVAWD VGEPTHSALH PEDCVLMRGE EGKWADEICE
KKFGFICEKK TSSKASNNDT IVTNPGCQTG WSRYGYYCYT AGSETKTFDE AKQACKKAES
HLVDISSRVE NAFLVSLVGA RPETHFWIGL SSQKDRHSFE WTNSKHVPFT HFNTGMPGRT
QGCVAMITGI VAGVWDVLSC SNKEKYICKQ KADGVVTTPA PPTTPSLTCP EEWSLIGTRD
YCVKHFNVPM LQMKTWDEAL NFCQELGGDL LSIQYESDIP WKQGGGYPSW IGYRMYDPLV
GFVWSDGSPS SYQSWATDEP NNLNNMENCV EMRVSLWDDD GLWNDVNCND KKDWYCQIRK
GKTPKEVNIS ETVYNKTEDG WTEFKGSQYF VVKFSAMSMH EARAFCKRKH GDLVTINDEE
ERIFIWHKCK ESYSSLIIGL LVDFDGTYQW MDGSPVVFEA WEANQPAFTN SDERCAKMTS
SQGLWETINC GDEYNFVCKR SESPSVNSTV APTPNPKGGC APGWIHFKRK CYNVREETKT
WMEARKHCRD LAFLTTQIRD TSVDLWIGFN NLANQRFKWT DGSGVSFTEW ANGEPHSTPN
WRSQFWTIYH YLDRKECVLL SNSNFGKWVA TDCNSTNGFI CNRDIGIPPT PPIQHPGHCP
EQVEDSPMRW IPFKDSCYAF VTNMKSWSRA ARICMTWGAT LVSIRDEPEQ TFIESNLLLL
ESYKEFWIGL LNNHKGNWFW LDRSVVDYTN WASESDYEDD YEGHSWNPDC ALISATHKKW
KKRNCEYTIL PFICKTAKEV ITTTETPHKG LEAHSTNTGL AVFLTIAILG IFGALAYVYH
RKARHWLMPA FENPMYNNTD SDHADKDNKT LLGQIEIVE
//
