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Database: UniProt
Entry: A0A3P9PFL5_POERE
LinkDB: A0A3P9PFL5_POERE
Original site: A0A3P9PFL5_POERE 
ID   A0A3P9PFL5_POERE        Unreviewed;      1461 AA.
AC   A0A3P9PFL5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Macrophage mannose receptor 1-like {ECO:0000313|Ensembl:ENSPREP00000020701.1};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000020701.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000020701.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000020701.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00479}.
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DR   RefSeq; XP_008432795.1; XM_008434573.2.
DR   STRING; 8081.ENSPREP00000020701; -.
DR   Ensembl; ENSPRET00000020921.1; ENSPREP00000020701.1; ENSPREG00000014004.1.
DR   GeneID; 103479889; -.
DR   KEGG; pret:103479889; -.
DR   GeneTree; ENSGT01050000244842; -.
DR   OMA; ICYSKGV; -.
DR   OrthoDB; 4271106at2759; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000014004; Expressed in caudal fin and 1 other cell type or tissue.
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; 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; 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; 8.
DR   SMART; SM00034; CLECT; 8.
DR   SMART; SM00059; FN2; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 8.
DR   SUPFAM; SSF57440; Kringle-like; 1.
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};
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:UP000242638};
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..1461
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018166988"
FT   TRANSMEM        1385..1407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          151..197
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000259|PROSITE:PS51092"
FT   DOMAIN          208..327
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          351..467
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          492..607
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          640..758
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          786..900
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          928..1070
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1091..1202
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1249..1360
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          760..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1461 AA;  164957 MW;  2B7167779E1E1DA0 CRC64;
     MRSTCIVTVL LLKMLQCLAL DDSPFQLTNA AGFCLVKTDS VCQEIRWTTA DRLLVPGKNK
     CLGVQGTTPM SEVSLYDCDE NNELQKWNCT KDYLLTLQAS TGQKLFVELH ADNRAVLVTT
     AGPISKLVIS GTSSGACTRT YREFYTIGGN AAGRPCMFPF FYENQWYSSC TLADSRNQHW
     CSVETKYEHQ TWGYCPTNNK DSWIKHPTSG ALYQLNTESA LTWSEAETSC KQQSASLLTI
     TDPQEKAYIT ALLEPGGTHQ GYKLWTGLTL DSEHGWQWSN GDPFRYLNWD SGHPVNNPAH
     TCGVVDGNVR YAWQSSTCNK KFGYICYSKG VLAAPTAGPD MGHCSAPWVP YNGHCFRLYR
     NAQSWSXAQQ TCRKEGGDLA SIRNTEDHSF ISTELGYAST DELWIGLNDK KTEGLFDWTD
     HTTVTFTSWQ FGKPQGGNNQ NDCVLVRGEN GNWADDDCTK SHGFICMKAS ASEPTGDEVQ
     QDAGCKTGWK RYGSYCYFIG TERKTFGDAK EDCKRSNSYL ADVSNRVDNA FLVSLVGLRS
     EKHFWLGLSN QKNRDVFEWT STAPVRYTHW NREMPGHNQG CVAMTTGSTA GLWDVLPCTS
     REKYICKYQA EGTAQTPAPT TAPSALCAKG WTRVQSRYVC HKVFSESKSW FEARDYCRGI
     GGDLMSVHSA AEINFNMETP RYYYSRSSAL WIGLSANDQG TGYEWSDGSP VNFQHWQDGE
     PNNKNNVESC VEFTSRNFDD SGSWNDNQCE ARNGFVCQIR TGLTPQSPPP TPTPDYNRTD
     DGWLEWGGNK YYFENRQMAN EDARKSCREK HADLVTINSE AERIFLWKQI SRRSSSFWIG
     LTVDLDKSFQ WMDGSPVIYQ MWDEGQPNFA NNDENCVSMR SFHGFWHDYN CGFEFGSICK
     RSSSPPVNAT VAPTAPPKGN CKDGWQKINS KCYKIISDKT LTWLDARQQC IDMEGNLASI
     PSRHEQVFLV SEMSKTPNRD LWIGFQSSYG NGFYWTDGRP RSYVNLESER RIYHFPHLSH
     RYGPMYDHDD DIFVSLRNEK RCAVINANPS FGIGKWIPKS CNDTNGFICS MPLNDKLPNK
     TQTNPENYFK ILNDSIKLVT QQKNWSEAQK ACEADGAKLV SVRTEWTQAY IELLALNLNR
     SLWIGLNKKQ TNNYFRYVEG WPLIFTRWSG NEPRRDGICV YVDVDGKWKT NDCNQEFSSL
     CMKSTDIPPE VKADDYPGVC PEDPHLSMSG YRPSRFSFGQ RQWQAWKPFR GFCYLFSSDE
     KEWQDATTSC LGHGGSLASI GDPFEQEFIL NSIKSFQDSH TSYWMGLYKT NKGEWKWLDN
     MVMDFENWQN YPSGPFGMIS ASDGKWHTGQ RWMDRPYICK AAKVLLSKPS SAPSVVSGPQ
     GRGHAALTAV LVIAGIAAGA GVAFFLFKKS GRQMMTRPIP GGLTAFDNPL FSSNRTQKNL
     VDTKKLLGNA DEDNSQPVIT I
//
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