GenomeNet

Database: UniProt
Entry: G3TNX9_LOXAF
LinkDB: G3TNX9_LOXAF
Original site: G3TNX9_LOXAF 
ID   G3TNX9_LOXAF            Unreviewed;      1455 AA.
AC   G3TNX9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Mannose receptor C-type 1 {ECO:0000313|Ensembl:ENSLAFP00000017020.2};
GN   Name=MRC1 {ECO:0000313|Ensembl:ENSLAFP00000017020.2};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000017020.2, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000017020.2, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017020.2,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000017020.2}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017020.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   Ensembl; ENSLAFT00000021691.2; ENSLAFP00000017020.2; ENSLAFG00000022148.2.
DR   GeneTree; ENSGT01050000244842; -.
DR   HOGENOM; CLU_002069_0_0_1; -.
DR   InParanoid; G3TNX9; -.
DR   Proteomes; UP000007646; 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   Pfam; PF00652; Ricin_B_lectin; 1.
DR   PRINTS; PR00013; FNTYPEII.
DR   SMART; SM00034; CLECT; 8.
DR   SMART; SM00059; FN2; 1.
DR   SMART; SM00458; RICIN; 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; 6.
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}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1455
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003455269"
FT   TRANSMEM        1387..1410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          163..211
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000259|PROSITE:PS51092"
FT   DOMAIN          230..341
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          369..487
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          511..626
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          655..778
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          807..923
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          951..1079
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1101..1212
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1240..1355
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DISULFID        168..194
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        182..209
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ   SEQUENCE   1455 AA;  165716 MW;  648476629C08A4ED CRC64;
     LRLPVLLVFL SLVQVAVQLL DTRQFLIYNE DHKRCVEALS PSAVQTAACN PDNESQKFRW
     VSDSQVMSVA FKLCLGVPSK TDWVAITLYA CDSKNEFQKW ECKNDTLFGI KGEDLFFNYG
     NRQEKNIMLY KGSGLWSRWK IYGTTDDLCS RSYEAMFTLL GNANGATCAF PFKFENKWYA
     DCTSVGRSDG WLWCGTTTDY DTDKLFGFCP LKFEGSESLW NKDPLTSIYY QINSKSALTW
     HQARKSCQQQ SAELLSITEI HEQTYLTGLT SSLTSGLWIG LNSLSFNSGW QWSEGSPFRY
     LNWLPGSPST EPGKSCVSLN PGKNAKWENL ECVQKLGYIC KKGNTTLNPF VIPSERDVPT
     SCPSQWWPYA GHCYKIYRGE KKIQRNALTA CRKEGGDLAS IHSIEEFDFI FSQLGYESND
     ELWIGLNDIK IQMYFEWSDG TPVTFTKWLH GEPSHENNRQ EDCVVMKGKD GHWADRACEQ
     PLDYICKMKA QTQVPAIVEV ETGCRKGWKR HGFFCYLIGH TLSTFTEANQ TCGNEKAYLT
     TVEDRYEQAF LTSFVGLRPE RYFWTGLSDI QSKGTFQWTI EEGVQFTHWN ADMPGRKAGC
     VAMRTGIAGG LWDVLKCDEK AKFVCKHWAE GATRPPEPTT TPEPKCPEDW GTTSKSSLCF
     KLFTKGKHDK KTWFESRDFC RALGGDLASI NNKEEQQAIW RLITSSSSYH ELFWLGLTYG
     SPSEGFTWSD GSPVSYEHWA YGEPNNYQNV EFCGELKGDP GMFWNDINCE HLNNWICQIK
     KGQTPKPEPT PAPQDNPPVT EDGWVIYKEY QYYFSKEKET MDNAREFCKR NFGDLVSIQS
     ESEKKFLWKY VNRNDAQSAY FIGLLISLDK KFIWVDGSKV DYVAWATGEP NFANDDENCV
     AMYSNSGFWN DINCGYPHAF ICQRHNSSIN ATVLPTTPPV KGGCEQGWKS YNNKCFKIFG
     FVEEERKNWQ EARKACIGFG GNLVSIRNEK EQAFLTYQMT GSSFNAWIGL NDVNSEHTFL
     WTDQRGVYYT NWGKGYPGGR RSSLSYEDAD CVVIIGGKSQ DAGKWMDDTC DSKRGYICHT
     LPNPSLPVSP TTVPSDGFIN FGESSYSLID LKLSWYEAEK YCTLHNSHIG SILDPYSNAF
     VWIQMEKLNS PVWIALNSNL TNNEYVWTDK WRVRYTNWAA DEPKLKSACV YLDTDGYWKT
     AYCNESFYSL CKRSNDTPAT EPPQLPGRCP ESDHTAWIPF HGHCYYIESS YTKNWGHASL
     ECLRMGSSLV SIESAAESSF LSYRVEPLKS KTNFWIGLFR NVEGMWLWIN KNPVSFVNWN
     AGDPSGERND CVTLLASSGF WNNVHCSSYK GYICKRPKIV DAEPTRTLMT TKADSRKMDP
     SKPSSSVAGI VVIVILLILT GTGLAAYFFY KKRRVQLPQE STFENTLYFN SRSSPGTNDT
     KDLMDNIEQN ERAAI
//
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