ID A0A4W6EXH2_LATCA Unreviewed; 1472 AA.
AC A0A4W6EXH2;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Mannose receptor, C type 1b {ECO:0000313|Ensembl:ENSLCAP00010043111.1};
GN Name=LOC108883267 {ECO:0000313|Ensembl:ENSLCAP00010043111.1};
OS Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010043111.1, ECO:0000313|Proteomes:UP000314980};
RN [1] {ECO:0000313|Proteomes:UP000314980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sai Rama Sridatta P.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLCAP00010043111.1}
RP IDENTIFICATION.
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 Ensembl; ENSLCAT00010044171.1; ENSLCAP00010043111.1; ENSLCAG00010020084.1.
DR GeneTree; ENSGT01050000244842; -.
DR InParanoid; A0A4W6EXH2; -.
DR Proteomes; UP000314980; 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; 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; 4.
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, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000314980};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1472
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5021255371"
FT TRANSMEM 1398..1420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 162..209
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 220..335
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 358..474
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 499..614
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 643..762
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 790..907
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 935..1086
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1117..1219
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1260..1373
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 167..193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1472 AA; 167152 MW; DFD73FD689E8342C CRC64;
MSAAVRLIRR MLTPRITLVS FVLFVLASEC STANDAPFSL TNRATGFCLL KKFTRCLDMR
WTTGNRLFVV TTKKCLGAQG KSLGSEVSLY DCDINSDLQK WECKNGTLLA LKGQELYIEV
KADETIALSR TVGPNNDFTI TGTVSGACTR TFRELYTIEG NAFGKICMFP FLYKDRWFGD
CTTYDSSQKR AWCAVETKYE HEQWGYCPST STDHWVKNLV TGAYYQLNTQ AALTWPQADA
SCKQQGASLV SVTDPHQQAF MSALLGTAKH KLWIGVVLDP EHGWQWSNGK PFRYLRWSTG
HPLPNPGHNC AFLDSAGDHS WQSSSCVKKL GYICYKAGAP PVTPQIEQGF CSSPWIPYNG
HCFHLQRTPQ TWINAQKECR KEHGDLVSIR NVEDQSFVIS QLGYASIDEL WIGLNDRKTE
GLFDWIDHST VSFTSWDFGK PAVGTDLKDC VLMSGQNGNW ADRACEERHG FICMKMSAST
PTGDEVEQDV GCKTGWRRHG SYCYFLGMEA KTFDDAKEDC KSSNSYLADV SSGVDNAFLV
SLVGMRPEKN FWIGLSNQRN IDQFVWTNTD MVRFTHWNAE MPGHRQGCVA MKTGIFAGLW
DVLPCTNTEK YICKLLAEGA VLTPAPPTIH PPKCADGWNQ LGSRKDCYKL YKETYSNKRT
WYEARDYCKA IGGDLLSIHN RAELEMLPDR YESVWIGLSA PDPVTGYVWS DGSPVQFQHW
EEDEPNNKNN VESCAELKLS KVRRSGSWND VHCETYHGWL CQIRAGVTPN PPPDPVTPDY
NTTSDGWTEW NGDQYYFNRM SMAMEDARAY CKQNHGDLVT INSEAESVFL WKHVSKNRGS
SGSYWIGLIV DLDGTYAWMD GSPVVFQRWD EKQPDFLNND ENCAVMTTSM GFWHDYNCGL
EHQSICKRSG SPPVNATVAP TVPPKGGCPQ NWKKINSKCY SITTSPEATW EGARTQCKTM
GGNLASILSR HVQVFLSIEM AKAPTTNLWI GLHNKRGYTF RWTDGRPMRY TNWGNDNHRA
VIYDGPWRHH HMHRMSFYHD DLDYYHPMMH SISEVKECAV MISDPRIGIG KWISKSCNDT
NGYICLRNLD TSLPDSPEPT GTSGYVQIFN DSIKAVTQQM TWDAALKHCQ SDGANLASVR
NEWSQIYIEL MAMHLNSSVW IGLNKERTNG YFRYVDGWRM TLSNWGRREP NTYQDCVYVD
MDGKWRTAGC SQNMSTICMK STEVPPTDST DFPGFCPDDP HKHTHMPSRY FTQRNTWLPF
RAYCYLFLTE KIEWPDASAS CVRHGGNLVS IEDPSEQEFI LSNLKIYQDS HTSFWIGLYK
THQGLWRWLD KTVMDYSNWD RSVPDEDNYG TIKVSDGRWR GGRQWHDRGY ICKTPKVTPP
VPPTTASRKE DPQTRGHIIL AVVLVITAIA MGIFVIGFLF KKSGHRLTIP EKLTTFDNPL
FFNNERSQPD LVDTNKLVAN AEEEHPEPIV TV
//
