ID A0A671WE13_SPAAU Unreviewed; 1421 AA.
AC A0A671WE13;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Mannose receptor C type 2 {ECO:0000313|Ensembl:ENSSAUP00010036829.1};
GN Name=MRC2 {ECO:0000313|Ensembl:ENSSAUP00010036829.1};
OS Sparus aurata (Gilthead sea bream).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Sparus.
OX NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010036829.1, ECO:0000313|Proteomes:UP000472265};
RN [1] {ECO:0000313|Ensembl:ENSSAUP00010036829.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSSAUT00010038774.1; ENSSAUP00010036829.1; ENSSAUG00010014174.1.
DR GeneTree; ENSGT01050000244842; -.
DR Proteomes; UP000472265; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 6.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR CDD; cd00062; FN2; 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; IPR033989; CD209-like_CTLD.
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 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 PRINTS; PR00013; FNTYPEII.
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; 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|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000472265};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1354..1378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..188
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 202..318
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 348..459
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 481..588
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 631..759
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 777..896
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 924..1043
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1078..1183
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1216..1328
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 602..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 145..171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 159..186
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1421 AA; 160482 MW; 8F4C81DE945A0072 CRC64;
MPLFPSLCTV PLDSDEFAFF HEGAQGCLGV RDHSLVLSTS CEEPNQRWKW VTRARLFNLG
SSLCLGLTTG NVSSRGDRSP LGVYTCDREP PRVRWTWNCA QVLDNLNTYL PSPSFWNSTS
SSDFEVCLYS TEIYTIQGNS HGRPCYLPFL YDGQWFHSCT SIGREDGHLW CSTTYDYGKD
ERWGFCPVKS GGCETFWDTD PLTDSCYQFN FQATLSWSEA RISCQQQGAD LLSITKLHEQ
TYINGLLTGY SAALWIGLND LDIHGGWQWA DSSPLKYLNW ETDQPNHVEE ENCAVIRTES
SGRWQNRDCS VALPYVCKKR PNATLDPFTT DSWADDAKYE CDVGWQAFQA GCYKLTSEKL
DWDTSQKTCQ KMEANLVSVH TLPELEFILH IDQLWIGLHD TDMQMDFQWT DHTPVIFTYW
HPFEPNNFRN TQEDCVSIWG AEGRWDDSPC NLTLPSICKK PGTKTDGKPQ HQDCKQGWKW
HSPACYWVGE DLLTFDEARK SCENNGAALV TITNRFEQAF ANSLVFGRSG DSFWIGLHDQ
SSPGSFHWLS GDEVSFTNWN RDQPGTVRGG CVSMATGFAT GLWEVRECAS SKAKFICRQN
QDTSLSPEPP VPQPTPSLSG SCPSGWKSNS NLRYCYKVFH SSQLEQKLSW LQAHLYCHRH
GANLLSIGSP EEEQFVLQVL HEAFGWVESE DHEQHWFWIG LNRRNPMDNG SWKWSDGLAF
TYQNFGRYYY NIRQCAAADL GTMTWLAMHC DSELDWICKI PRGTTALDLL SPEWIGFQEA
EYKFFDHRTT WDQAQRICSW FDSSLASVHS AEEEAFLANT LAKMSKVEGD NWWLGLHTYE
YDGRFRWSDH SVLNYVSWAL GRPHPLSRDR RCVYMSATKA DWADQKCHSD LPYICKRVNV
TGTIPPTPST PHPPAGCPDG WSSYQHKCFR VFDQAPRVTW SAAKLKCEAQ RGVLAVVTNH
LEQAFVTTLL NNASVDLWVG LTSDSKGHFQ WPKAGLLSYT NWGPGEPLDN SGPHHNRTPG
NCVVMIHGNP LKNSGMWASR ACEMESNGFI CQRPQGMILS LPPAPALIPV SLSKPVELGG
VTYRVVEKRL DWTGALHICE SLNGTLATVK DPYQQGYLTL LINSLRRPAW IGLYGYGGRS
YTWLGEEEAL YSNWKDGEPN QIGGCGHMST TGQWITTPCD AKLEAAICQI SGPVSHQWVY
PGQCPHSLGA WAWVPFRNHC YAFNLQSLKL QQDARMSCKK VGAELLSILD ETENGFISEH
IQSYAEQAHG AWLGISVKGR GLVWSEDTEM SYTNWEARDV AFSVLSPNSC FWIQSNSGLW
KPGSCRNRTH GVICKTPRTN QSSVKPEKAD GDHLPTLIVV MVTGLVLVAL IVGVIYLYRR
RVVGSRGSYE GARYSRTNSS LAEQTEKNIL VSDMELNEQP E
//
