ID A0A1S3ICP2_LINUN Unreviewed; 744 AA.
AC A0A1S3ICP2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Macrophage mannose receptor 1-like {ECO:0000313|RefSeq:XP_013395626.1};
GN Name=LOC106162753 {ECO:0000313|RefSeq:XP_013395626.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013395626.1};
RN [1] {ECO:0000313|RefSeq:XP_013395626.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013395626.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013395626.1; XM_013540172.1.
DR AlphaFoldDB; A0A1S3ICP2; -.
DR EnsemblMetazoa; XM_013540172.1; XP_013395626.1; LOC106162753.
DR GeneID; 106162753; -.
DR KEGG; lak:106162753; -.
DR InParanoid; A0A1S3ICP2; -.
DR OrthoDB; 3020546at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR CDD; cd00037; CLECT; 3.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 3.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
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; PF00059; Lectin_C; 3.
DR SMART; SM00034; CLECT; 3.
DR SUPFAM; SSF56436; C-type lectin-like; 3.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 3.
PE 4: Predicted;
KW Receptor {ECO:0000313|RefSeq:XP_013395626.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 80..195
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 339..452
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 536..649
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 744 AA; 82803 MW; 5F4DE2FB4C905D69 CRC64;
METPSASTPA VPPTRHAKTT GHHPTPSALL DKTTKATTKT STAIRTSPSS SSTPVAPSTP
DASRYTCPQN LEPNYQTFTY RDHCYQFVTK EDWRSTAREY CRKYQGHLIE IPDQSTMDFV
IDVLNKKLKW GVNGVWNGAT DQREEGVWEW DGSDNPVIYS NWAQGQPGGL ARWTEDCACM
RRTDNWQWHD YGCSQPGYSY RYICQYDLVE NITTNSLLLS TQTVTPRLES TSKTKQQSLP
PTALISKAPL SANRTTPKKP LSTRTTIRTI TAKQSPSISR KPSSSSYHQT SVTTPSSTPT
SVKSSTSRTN PQIDVSPFPV QGRTCPQTLG TEHKTVVYNG SYCYQFVDKS VTWNDALDYC
QRRGGALVEI YGQETMDFIA EVLRRNFSWN AVWIGASDEE KEGEFKWRGS GREVTYSNWA
PGQPSGIWTL GLEDCVALEK ADGYKWHDYH CSIGTQKLKL ICQYDLVEKN TPSVEQTSIA
SATKHTPTSA TSGYISTTTT TSETPTDTPI TGSLTTAAMS DTTCPPEVRT NERHVYGGQC
YQFVDRAVTW VGALNDCEVK GGRLLEIYDE DTMRFIARTL TNYYRWDTVW TGANDRGKEG
QFIWRGTGWE VTYTNWAPAQ PSGIWAFGLE DCVALVKNDG YKWHDFHCNI GTQQFRFICQ
YGPLPTTSPS VPLTSSLPSQ SSRKGEVTST TSSPRTMLSQ SSRKGEVTST STLPQTTAVD
TAKGPLSLKN QDEHGVSSSN NKGY
//
