MRC2_HUMAN
ID MRC2_HUMAN Reviewed; 1479 AA.
AC Q9UBG0; A6H8K4; D3DU08; Q7LGE7; Q9Y5P9;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=C-type mannose receptor 2;
DE AltName: Full=C-type lectin domain family 13 member E;
DE AltName: Full=Endocytic receptor 180;
DE AltName: Full=Macrophage mannose receptor 2;
DE AltName: Full=Urokinase-type plasminogen activator receptor-associated protein;
DE Short=UPAR-associated protein;
DE Short=Urokinase receptor-associated protein;
DE AltName: CD_antigen=CD280;
DE Flags: Precursor;
GN Name=MRC2; Synonyms=CLEC13E, ENDO180, KIAA0709, UPARAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 350-360, IDENTIFICATION BY
RP MASS SPECTROMETRY, SUBUNIT, AND VARIANT HIS-1156.
RX PubMed=10636902; DOI=10.1074/jbc.275.3.1993;
RA Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M., Danoe K.;
RT "A urokinase receptor-associated protein with specific collagen binding
RT properties.";
RL J. Biol. Chem. 275:1993-2002(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, GLYCOSYLATION,
RP TISSUE SPECIFICITY, AND VARIANTS ILE-43 AND HIS-1156.
RX PubMed=10683150; DOI=10.1242/jcs.113.6.1021;
RA Sheikh H., Yarwood H., Ashworth A., Isacke C.M.;
RT "Endo180, an endocytic recycling glycoprotein related to the macrophage
RT mannose receptor is expressed on fibroblasts, endothelial cells and
RT macrophages and functions as a lectin receptor.";
RL J. Cell Sci. 113:1021-1032(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-1156.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-1156.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-1156.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=8702911; DOI=10.1074/jbc.271.35.21323;
RA Wu K., Yuan J., Lasky L.A.;
RT "Characterization of a novel member of the macrophage mannose receptor type
RT C lectin family.";
RL J. Biol. Chem. 271:21323-21330(1996).
RN [8]
RP MUTAGENESIS OF TYR-1452; GLU-1464 AND 1468-LEU-VAL-1469.
RX PubMed=12068012; DOI=10.1074/jbc.m203631200;
RA Howard M.J., Isacke C.M.;
RT "The C-type lectin receptor Endo180 displays internalization and recycling
RT properties distinct from other members of the mannose receptor family.";
RL J. Biol. Chem. 277:32320-32331(2002).
RN [9]
RP DOMAIN, AND MUTAGENESIS OF ASN-472.
RX PubMed=12399458; DOI=10.1074/jbc.m208985200;
RA East L., Rushton S., Taylor M.E., Isacke C.M.;
RT "Characterization of sugar binding by the mannose receptor family member,
RT Endo180.";
RL J. Biol. Chem. 277:50469-50475(2002).
RN [10]
RP FUNCTION, AND DOMAIN.
RX PubMed=12972549; DOI=10.1091/mbc.e02-12-0814;
RA Wienke D., MacFadyen J.R., Isacke C.M.;
RT "Identification and characterization of the endocytic transmembrane
RT glycoprotein Endo180 as a novel collagen receptor.";
RL Mol. Biol. Cell 14:3592-3604(2003).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP GLYCOSYLATION AT ASN-69.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [13]
RP SUMOYLATION AT LYS-1142.
RC TISSUE=Cervix carcinoma;
RX PubMed=20388717; DOI=10.1074/jbc.m110.106955;
RA Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A.,
RA Eriksson J.E., Sistonen L.;
RT "In vivo identification of sumoylation sites by a signature tag and
RT cysteine-targeted affinity purification.";
RL J. Biol. Chem. 285:19324-19329(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May play a role as endocytotic lectin receptor displaying
CC calcium-dependent lectin activity. Internalizes glycosylated ligands
CC from the extracellular space for release in an endosomal compartment
CC via clathrin-mediated endocytosis. May be involved in plasminogen
CC activation system controlling the extracellular level of PLAUR/PLAU,
CC and thus may regulate protease activity at the cell surface. May
CC contribute to cellular uptake, remodeling and degradation of
CC extracellular collagen matrices. May play a role during cancer
CC progression as well as in other chronic tissue destructive diseases
CC acting on collagen turnover. May participate in remodeling of
CC extracellular matrix cooperating with the matrix metalloproteinases
CC (MMPs). {ECO:0000269|PubMed:10683150, ECO:0000269|PubMed:12972549}.
CC -!- SUBUNIT: Interacts with C-terminal region of type I collagen/COL1A1 (By
CC similarity). Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to
CC form a tri-molecular complex. Interacts with collagen V. {ECO:0000250,
CC ECO:0000269|PubMed:10636902}.
CC -!- INTERACTION:
CC Q9UBG0; P02454: Col1a1; Xeno; NbExp=2; IntAct=EBI-1104992, EBI-915744;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitous with low expression in brain, placenta,
CC lung, kidney, pancreas, spleen, thymus and colon. Expressed in
CC endothelial cells, fibroblasts and macrophages. Highly expressed in
CC fetal lung and kidney. {ECO:0000269|PubMed:10683150,
CC ECO:0000269|PubMed:8702911}.
CC -!- DOMAIN: C-type lectin domains 3 to 8 are not required for calcium-
CC dependent binding of mannose, fucose and N-acetylglucosamine. C-type
CC lectin domain 2 is responsible for sugar-binding in a calcium-dependent
CC manner.
CC -!- DOMAIN: Fibronectin type-II domain mediates collagen-binding.
CC -!- DOMAIN: Ricin B-type lectin domain contacts with the second C-type
CC lectin domain. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10683150,
CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31684.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Endo180;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_251";
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DR EMBL; AF107292; AAF14192.1; -; mRNA.
DR EMBL; AF134838; AAD30280.1; -; mRNA.
DR EMBL; AB014609; BAA31684.2; ALT_INIT; mRNA.
DR EMBL; AC080038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94341.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94342.1; -; Genomic_DNA.
DR EMBL; BC146647; AAI46648.1; -; mRNA.
DR EMBL; BC150212; AAI50213.1; -; mRNA.
DR EMBL; BC153884; AAI53885.1; -; mRNA.
DR CCDS; CCDS11634.1; -.
DR RefSeq; NP_006030.2; NM_006039.4.
DR PDB; 5AO5; X-ray; 2.48 A; A/B=35-511.
DR PDB; 5AO6; X-ray; 3.36 A; A/B=35-511.
DR PDB; 5E4K; X-ray; 2.58 A; A=31-510.
DR PDB; 5E4L; X-ray; 2.44 A; A/B=31-510.
DR PDB; 5EW6; X-ray; 2.29 A; A=31-510.
DR PDBsum; 5AO5; -.
DR PDBsum; 5AO6; -.
DR PDBsum; 5E4K; -.
DR PDBsum; 5E4L; -.
DR PDBsum; 5EW6; -.
DR AlphaFoldDB; Q9UBG0; -.
DR SMR; Q9UBG0; -.
DR BioGRID; 115231; 68.
DR DIP; DIP-37631N; -.
DR IntAct; Q9UBG0; 35.
DR MINT; Q9UBG0; -.
DR STRING; 9606.ENSP00000307513; -.
DR GlyConnect; 764; 17 N-Linked glycans (5 sites).
DR GlyGen; Q9UBG0; 10 sites, 16 N-linked glycans (5 sites).
DR iPTMnet; Q9UBG0; -.
DR PhosphoSitePlus; Q9UBG0; -.
DR SwissPalm; Q9UBG0; -.
DR BioMuta; MRC2; -.
DR DMDM; 317373394; -.
DR EPD; Q9UBG0; -.
DR jPOST; Q9UBG0; -.
DR MassIVE; Q9UBG0; -.
DR MaxQB; Q9UBG0; -.
DR PaxDb; Q9UBG0; -.
DR PeptideAtlas; Q9UBG0; -.
DR PRIDE; Q9UBG0; -.
DR ProteomicsDB; 83964; -.
DR Antibodypedia; 31250; 261 antibodies from 30 providers.
DR DNASU; 9902; -.
DR Ensembl; ENST00000303375.10; ENSP00000307513.5; ENSG00000011028.14.
DR GeneID; 9902; -.
DR KEGG; hsa:9902; -.
DR MANE-Select; ENST00000303375.10; ENSP00000307513.5; NM_006039.5; NP_006030.2.
DR UCSC; uc002jad.5; human.
DR CTD; 9902; -.
DR DisGeNET; 9902; -.
DR GeneCards; MRC2; -.
DR HGNC; HGNC:16875; MRC2.
DR HPA; ENSG00000011028; Low tissue specificity.
DR MIM; 612264; gene.
DR neXtProt; NX_Q9UBG0; -.
DR OpenTargets; ENSG00000011028; -.
DR PharmGKB; PA134988161; -.
DR VEuPathDB; HostDB:ENSG00000011028; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT01050000244842; -.
DR HOGENOM; CLU_002069_2_0_1; -.
DR InParanoid; Q9UBG0; -.
DR OMA; GFIWEHI; -.
DR OrthoDB; 29241at2759; -.
DR PhylomeDB; Q9UBG0; -.
DR TreeFam; TF316663; -.
DR PathwayCommons; Q9UBG0; -.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR SignaLink; Q9UBG0; -.
DR BioGRID-ORCS; 9902; 15 hits in 1076 CRISPR screens.
DR ChiTaRS; MRC2; human.
DR GenomeRNAi; 9902; -.
DR Pharos; Q9UBG0; Tbio.
DR PRO; PR:Q9UBG0; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UBG0; protein.
DR Bgee; ENSG00000011028; Expressed in tendon of biceps brachii and 207 other tissues.
DR ExpressionAtlas; Q9UBG0; baseline and differential.
DR Genevisible; Q9UBG0; HS.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0030574; P:collagen catabolic process; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.10.10.10; -; 1.
DR Gene3D; 3.10.100.10; -; 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 InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF56436; SSF56436; 8.
DR SUPFAM; SSF57440; SSF57440; 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 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Endocytosis; Glycoprotein; Isopeptide bond; Lectin; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1479
FT /note="C-type mannose receptor 2"
FT /id="PRO_0000046078"
FT TOPO_DOM 31..1414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1415..1435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1436..1479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..167
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 182..230
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 244..360
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 389..505
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 528..644
FT /note="C-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 678..809
FT /note="C-type lectin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 832..951
FT /note="C-type lectin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 979..1107
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1132..1243
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1273..1393
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1450..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1029
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..68
FT /evidence="ECO:0000250"
FT DISULFID 93..112
FT /evidence="ECO:0000250"
FT DISULFID 187..213
FT /evidence="ECO:0000250"
FT DISULFID 201..228
FT /evidence="ECO:0000250"
FT DISULFID 266..359
FT /evidence="ECO:0000250"
FT DISULFID 335..351
FT /evidence="ECO:0000250"
FT DISULFID 410..504
FT /evidence="ECO:0000250"
FT DISULFID 481..496
FT /evidence="ECO:0000250"
FT DISULFID 618..635
FT /evidence="ECO:0000250"
FT DISULFID 704..808
FT /evidence="ECO:0000250"
FT DISULFID 785..800
FT /evidence="ECO:0000250"
FT DISULFID 853..950
FT /evidence="ECO:0000250"
FT DISULFID 927..942
FT /evidence="ECO:0000250"
FT DISULFID 1078..1098
FT /evidence="ECO:0000250"
FT DISULFID 1220..1234
FT /evidence="ECO:0000250"
FT DISULFID 1369..1384
FT /evidence="ECO:0000250"
FT CROSSLNK 1142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT VARIANT 43
FT /note="V -> I (in dbSNP:rs2014055)"
FT /evidence="ECO:0000269|PubMed:10683150"
FT /id="VAR_025304"
FT VARIANT 1156
FT /note="R -> H (in dbSNP:rs2429387)"
FT /evidence="ECO:0000269|PubMed:10636902,
FT ECO:0000269|PubMed:10683150, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9734811, ECO:0000269|Ref.5"
FT /id="VAR_025305"
FT MUTAGEN 472
FT /note="N->D: Reduced sugar-binding activity."
FT /evidence="ECO:0000269|PubMed:12399458"
FT MUTAGEN 1452
FT /note="Y->A: No alteration of distribution and
FT trafficking."
FT /evidence="ECO:0000269|PubMed:12068012"
FT MUTAGEN 1464
FT /note="E->A: Increased cell surface distribution."
FT /evidence="ECO:0000269|PubMed:12068012"
FT MUTAGEN 1468..1469
FT /note="LV->AA: Reduction of endocytotic activity;
FT distribution almost restricted to the cell surface."
FT /evidence="ECO:0000269|PubMed:12068012"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5EW6"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:5EW6"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5EW6"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:5EW6"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5AO5"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:5EW6"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:5EW6"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:5E4L"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5EW6"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5EW6"
FT TURN 180..184
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:5EW6"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:5EW6"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:5AO5"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:5EW6"
FT HELIX 259..267
FT /evidence="ECO:0007829|PDB:5EW6"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:5EW6"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:5EW6"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:5AO5"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:5EW6"
FT TURN 340..343
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 392..401
FT /evidence="ECO:0007829|PDB:5EW6"
FT HELIX 403..412
FT /evidence="ECO:0007829|PDB:5EW6"
FT HELIX 423..432
FT /evidence="ECO:0007829|PDB:5EW6"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 439..445
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:5E4L"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 478..485
FT /evidence="ECO:0007829|PDB:5EW6"
FT TURN 486..489
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 490..495
FT /evidence="ECO:0007829|PDB:5EW6"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:5EW6"
SQ SEQUENCE 1479 AA; 166674 MW; AAAA5286F91DF7E7 CRC64;
MGPGRPAPAP WPRHLLRCVL LLGCLHLGRP GAPGDAALPE PNVFLIFSHG LQGCLEAQGG
QVRVTPACNT SLPAQRWKWV SRNRLFNLGT MQCLGTGWPG TNTTASLGMY ECDREALNLR
WHCRTLGDQL SLLLGARTSN ISKPGTLERG DQTRSGQWRI YGSEEDLCAL PYHEVYTIQG
NSHGKPCTIP FKYDNQWFHG CTSTGREDGH LWCATTQDYG KDERWGFCPI KSNDCETFWD
KDQLTDSCYQ FNFQSTLSWR EAWASCEQQG ADLLSITEIH EQTYINGLLT GYSSTLWIGL
NDLDTSGGWQ WSDNSPLKYL NWESDQPDNP SEENCGVIRT ESSGGWQNRD CSIALPYVCK
KKPNATAEPT PPDRWANVKV ECEPSWQPFQ GHCYRLQAEK RSWQESKKAC LRGGGDLVSI
HSMAELEFIT KQIKQEVEEL WIGLNDLKLQ MNFEWSDGSL VSFTHWHPFE PNNFRDSLED
CVTIWGPEGR WNDSPCNQSL PSICKKAGQL SQGAAEEDHG CRKGWTWHSP SCYWLGEDQV
TYSEARRLCT DHGSQLVTIT NRFEQAFVSS LIYNWEGEYF WTALQDLNST GSFFWLSGDE
VMYTHWNRDQ PGYSRGGCVA LATGSAMGLW EVKNCTSFRA RYICRQSLGT PVTPELPGPD
PTPSLTGSCP QGWASDTKLR YCYKVFSSER LQDKKSWVQA QGACQELGAQ LLSLASYEEE
HFVANMLNKI FGESEPEIHE QHWFWIGLNR RDPRGGQSWR WSDGVGFSYH NFDRSRHDDD
DIRGCAVLDL ASLQWVAMQC DTQLDWICKI PRGTDVREPD DSPQGRREWL RFQEAEYKFF
EHHSTWAQAQ RICTWFQAEL TSVHSQAELD FLSHNLQKFS RAQEQHWWIG LHTSESDGRF
RWTDGSIINF ISWAPGKPRP VGKDKKCVYM TASREDWGDQ RCLTALPYIC KRSNVTKETQ
PPDLPTTALG GCPSDWIQFL NKCFQVQGQE PQSRVKWSEA QFSCEQQEAQ LVTITNPLEQ
AFITASLPNV TFDLWIGLHA SQRDFQWVEQ EPLMYANWAP GEPSGPSPAP SGNKPTSCAV
VLHSPSAHFT GRWDDRSCTE ETHGFICQKG TDPSLSPSPA ALPPAPGTEL SYLNGTFRLL
QKPLRWHDAL LLCESRNASL AYVPDPYTQA FLTQAARGLR TPLWIGLAGE EGSRRYSWVS
EEPLNYVGWQ DGEPQQPGGC TYVDVDGAWR TTSCDTKLQG AVCGVSSGPP PPRRISYHGS
CPQGLADSAW IPFREHCYSF HMELLLGHKE ARQRCQRAGG AVLSILDEME NVFVWEHLQS
YEGQSRGAWL GMNFNPKGGT LVWQDNTAVN YSNWGPPGLG PSMLSHNSCY WIQSNSGLWR
PGACTNITMG VVCKLPRAEQ SSFSPSALPE NPAALVVVLM AVLLLLALLT AALILYRRRQ
SIERGAFEGA RYSRSSSSPT EATEKNILVS DMEMNEQQE
