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Database: UniProt
Entry: A0A2K5Y622_MANLE
LinkDB: A0A2K5Y622_MANLE
Original site: A0A2K5Y622_MANLE 
ID   A0A2K5Y622_MANLE        Unreviewed;      1456 AA.
AC   A0A2K5Y622;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Mannose receptor C-type 1 {ECO:0000313|Ensembl:ENSMLEP00000011012.1};
GN   Name=MRC1 {ECO:0000313|Ensembl:ENSMLEP00000011012.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000011012.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000011012.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   RefSeq; XP_011831973.1; XM_011976583.1.
DR   STRING; 9568.ENSMLEP00000011012; -.
DR   Ensembl; ENSMLET00000034433.1; ENSMLEP00000011012.1; ENSMLEG00000029655.1.
DR   GeneID; 105537100; -.
DR   KEGG; mleu:105537100; -.
DR   CTD; 4360; -.
DR   GeneTree; ENSGT01050000244842; -.
DR   OMA; WIDKWRV; -.
DR   OrthoDB; 4271106at2759; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0038024; F:cargo receptor activity; IEA:Ensembl.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
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   Calcium {ECO:0000256|ARBA:ARBA00022837};
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:UP000233140};
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..1456
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014411794"
FT   TRANSMEM        1388..1411
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          225..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          952..1080
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1102..1213
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   DOMAIN          1241..1356
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   1456 AA;  165905 MW;  57268B62FCA9339B CRC64;
     MRLPLLLVFA SVIPGAVLLL DTRQFLIYNE DHKRCVEAVS PSAVQTAACN QDAESQKFRW
     VSESQIMSVA FKLCLGVPSK TDWVAITLYA CDSKSEFQKW ECKNDTLLGI KGEDLFFNYG
     NRQEKNVMLY KGSGLWSRWK IYGTTDNLCS RGYEAMYTLL GNANGATCAF PFKFENKWYA
     DCTSAGRSDG WLWCGTTTDY DTDKLFGYCP LKFEGSESLW NKDPLTSISY QINSKSALMW
     HQARKSCQQQ NAELLSITEI HEQTYLTGLT SSLTSGLWIG LNSLSFNSGW QWSDRSPFRY
     LNWLPGSPSA EPGKSCVSLN PGKNAKWENL ECVQKLGYIC KKGNTTLNSF VIPSESDVPT
     HCPSQWWPYA GHCYKIHKDE KKIQRDALTA CRKEGGDLAS IHTIEEFDFI ISQLGYEPND
     ELWIGLNDIK IQMYFEWSDG TPVTFTKWLR GEPSHENNRQ EDCVVMKGKD GYWADRGCEW
     PLGYICKMKS RSQGPEIVEV EEGCKKGWKK HHFYCYMIGH TLSTFAEANQ TCNNENAYLT
     TIEDRYEQAF LTSFVGLRPE KYFWTGLSDI QTKGTFQWTI EEEVRFTHWN SDMPGRKPGC
     VAMRTGIAGG LWDVLKCDEK AKFVCKHWAE GVTHPPKPTT TPEPKCPEDW GASSRTSLCF
     KLYAKGKHEK KTWFESRDFC RALGGDLASI NNKEEQQTIW RLITASGSYH ELFWLGLTYG
     SPSEGFTWSD GSPVSYENWA YGEPNNYQNV EYCGELKGDP SMSWNDINCE HLNNWICQIH
     KGQTPKPEPT PAPQDNPPVT EDGWVIYKDY QYYFSKEKET MDNARAFCKR NFGDLVSIQS
     ESEKKFLWKY VNRNDAQSAY FIGLLISLDK KFAWMDGSKV DYVSWATGEP NFANEDENCV
     TMYSNSGFWN DINCGYPNAF ICQRHNSSIN ATTVMPTKPS VPSGCKEGWN FYNNKCFKIF
     GFVEEERKTW QEARKACIGF GGNLVSIQNE KEQAFLTYHM KDSTFSAWTG LNDVNSEHTF
     LWTDGRGVHY TNWGKGYPGG RRSSLSYEDA DCVVIIGGAS NEAGKWMDDT CDGKRGYICQ
     TRSDPSLTNP PATIQTDGFI KYGKSSYSLM RQKFQWHEAE IYCKLHNSLI ASILDPYSNA
     FAWLQMETSN ERVWIALNSN LTDSQYTWTD KWRVRYTNWA ADEPKLKSAC VYLDLDGYWK
     TAYCNESFYF LCKRSDEIPA TEPPQLPGRC PESDHTAWIP FHGHCYYIES SYTRNWGQAS
     LECLRMGSSL VSIESAAESS FLSYRVEPLK SKTNFWIGLF RNVEGMWLWI NNSPVSFVNW
     NTGDPSGERN DCVALHASSG FWSNIHCSSY KGYICKRPKI IDAKPTHESL TTKADTRKMD
     PSKPSSSVAG VVIIVILLIL TGAGLAAYFF YKKRRVHLPQ EGAFENTLYF NSQSSPGTSD
     MKDLVGNIEQ NEHAVI
//
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