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Q9UBG0 (MRC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-type mannose receptor 2
Alternative name(s):
C-type lectin domain family 13 member E
Endocytic receptor 180
Macrophage mannose receptor 2
Urokinase-type plasminogen activator receptor-associated protein
Short name=UPAR-associated protein
Short name=Urokinase receptor-associated protein
CD_antigen=CD280
Gene names
Name:MRC2
Synonyms:CLEC13E, ENDO180, KIAA0709, UPARAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1479 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). Ref.2 Ref.10

Subunit structure

Interacts with C-terminal region of type I collagen/COL1A1 By similarity. Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to form a tri-molecular complex. Interacts with collagen V. Ref.1

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Ubiquitous with low expression in brain, placenta, lung, kidney, pancreas, spleen, thymus and colon. Expressed in endothelial cells, fibroblasts and macrophages. Highly expressed in fetal lung and kidney. Ref.2 Ref.7

Domain

C-type lectin domains 3 to 8 are not required for calcium-dependent binding of mannose, fucose and N-acetylglucosamine. C-type lectin domain 2 is responsible for sugar-binding in a calcium-dependent manner. Ref.9 Ref.10

Fibronectin type-II domain mediates collagen-binding. Ref.9 Ref.10

Ricin B-type lectin domain contacts with the second C-type lectin domain By similarity. Ref.9 Ref.10

Post-translational modification

N-glycosylated. Ref.2 Ref.12

Sequence similarities

Contains 8 C-type lectin domains.

Contains 1 fibronectin type-II domain.

Contains 1 ricin B-type lectin domain.

Sequence caution

The sequence BAA31684.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 14791449C-type mannose receptor 2
PRO_0000046078

Regions

Topological domain31 – 14141384Extracellular Potential
Transmembrane1415 – 143521Helical; Potential
Topological domain1436 – 147944Cytoplasmic Potential
Domain41 – 167127Ricin B-type lectin
Domain182 – 23049Fibronectin type-II
Domain244 – 360117C-type lectin 1
Domain389 – 505117C-type lectin 2
Domain528 – 644117C-type lectin 3
Domain678 – 809132C-type lectin 4
Domain832 – 951120C-type lectin 5
Domain979 – 1107129C-type lectin 6
Domain1132 – 1243112C-type lectin 7
Domain1273 – 1393121C-type lectin 8

Amino acid modifications

Glycosylation691N-linked (GlcNAc...) (complex) Ref.11 Ref.12
Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation3641N-linked (GlcNAc...) Potential
Glycosylation5881N-linked (GlcNAc...) Potential
Glycosylation9541N-linked (GlcNAc...) Potential
Glycosylation10291N-linked (GlcNAc...) Potential
Glycosylation13501N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 68 By similarity
Disulfide bond93 ↔ 112 By similarity
Disulfide bond187 ↔ 213 By similarity
Disulfide bond201 ↔ 228 By similarity
Disulfide bond266 ↔ 359 By similarity
Disulfide bond335 ↔ 351 By similarity
Disulfide bond410 ↔ 504 By similarity
Disulfide bond481 ↔ 496 By similarity
Disulfide bond618 ↔ 635 By similarity
Disulfide bond704 ↔ 808 By similarity
Disulfide bond785 ↔ 800 By similarity
Disulfide bond853 ↔ 950 By similarity
Disulfide bond927 ↔ 942 By similarity
Disulfide bond1078 ↔ 1098 By similarity
Disulfide bond1220 ↔ 1234 By similarity
Disulfide bond1369 ↔ 1384 By similarity
Cross-link1142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1) Ref.13

Natural variations

Natural variant431V → I. Ref.2
Corresponds to variant rs2014055 [ dbSNP | Ensembl ].
VAR_025304
Natural variant11561R → H. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs2429387 [ dbSNP | Ensembl ].
VAR_025305

Experimental info

Mutagenesis4721N → D: Reduced sugar-binding activity. Ref.9
Mutagenesis14521Y → A: No alteration of distribution and trafficking. Ref.8
Mutagenesis14641E → A: Increased cell surface distribution. Ref.8
Mutagenesis1468 – 14692LV → AA: Reduction of endocytotic activity; distribution almost restricted to the cell surface.

Sequences

Sequence LengthMass (Da)Tools
Q9UBG0 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: AAAA5286F91DF7E7

FASTA1,479166,674
        10         20         30         40         50         60 
MGPGRPAPAP WPRHLLRCVL LLGCLHLGRP GAPGDAALPE PNVFLIFSHG LQGCLEAQGG 

        70         80         90        100        110        120 
QVRVTPACNT SLPAQRWKWV SRNRLFNLGT MQCLGTGWPG TNTTASLGMY ECDREALNLR 

       130        140        150        160        170        180 
WHCRTLGDQL SLLLGARTSN ISKPGTLERG DQTRSGQWRI YGSEEDLCAL PYHEVYTIQG 

       190        200        210        220        230        240 
NSHGKPCTIP FKYDNQWFHG CTSTGREDGH LWCATTQDYG KDERWGFCPI KSNDCETFWD 

       250        260        270        280        290        300 
KDQLTDSCYQ FNFQSTLSWR EAWASCEQQG ADLLSITEIH EQTYINGLLT GYSSTLWIGL 

       310        320        330        340        350        360 
NDLDTSGGWQ WSDNSPLKYL NWESDQPDNP SEENCGVIRT ESSGGWQNRD CSIALPYVCK 

       370        380        390        400        410        420 
KKPNATAEPT PPDRWANVKV ECEPSWQPFQ GHCYRLQAEK RSWQESKKAC LRGGGDLVSI 

       430        440        450        460        470        480 
HSMAELEFIT KQIKQEVEEL WIGLNDLKLQ MNFEWSDGSL VSFTHWHPFE PNNFRDSLED 

       490        500        510        520        530        540 
CVTIWGPEGR WNDSPCNQSL PSICKKAGQL SQGAAEEDHG CRKGWTWHSP SCYWLGEDQV 

       550        560        570        580        590        600 
TYSEARRLCT DHGSQLVTIT NRFEQAFVSS LIYNWEGEYF WTALQDLNST GSFFWLSGDE 

       610        620        630        640        650        660 
VMYTHWNRDQ PGYSRGGCVA LATGSAMGLW EVKNCTSFRA RYICRQSLGT PVTPELPGPD 

       670        680        690        700        710        720 
PTPSLTGSCP QGWASDTKLR YCYKVFSSER LQDKKSWVQA QGACQELGAQ LLSLASYEEE 

       730        740        750        760        770        780 
HFVANMLNKI FGESEPEIHE QHWFWIGLNR RDPRGGQSWR WSDGVGFSYH NFDRSRHDDD 

       790        800        810        820        830        840 
DIRGCAVLDL ASLQWVAMQC DTQLDWICKI PRGTDVREPD DSPQGRREWL RFQEAEYKFF 

       850        860        870        880        890        900 
EHHSTWAQAQ RICTWFQAEL TSVHSQAELD FLSHNLQKFS RAQEQHWWIG LHTSESDGRF 

       910        920        930        940        950        960 
RWTDGSIINF ISWAPGKPRP VGKDKKCVYM TASREDWGDQ RCLTALPYIC KRSNVTKETQ 

       970        980        990       1000       1010       1020 
PPDLPTTALG GCPSDWIQFL NKCFQVQGQE PQSRVKWSEA QFSCEQQEAQ LVTITNPLEQ 

      1030       1040       1050       1060       1070       1080 
AFITASLPNV TFDLWIGLHA SQRDFQWVEQ EPLMYANWAP GEPSGPSPAP SGNKPTSCAV 

      1090       1100       1110       1120       1130       1140 
VLHSPSAHFT GRWDDRSCTE ETHGFICQKG TDPSLSPSPA ALPPAPGTEL SYLNGTFRLL 

      1150       1160       1170       1180       1190       1200 
QKPLRWHDAL LLCESRNASL AYVPDPYTQA FLTQAARGLR TPLWIGLAGE EGSRRYSWVS 

      1210       1220       1230       1240       1250       1260 
EEPLNYVGWQ DGEPQQPGGC TYVDVDGAWR TTSCDTKLQG AVCGVSSGPP PPRRISYHGS 

      1270       1280       1290       1300       1310       1320 
CPQGLADSAW IPFREHCYSF HMELLLGHKE ARQRCQRAGG AVLSILDEME NVFVWEHLQS 

      1330       1340       1350       1360       1370       1380 
YEGQSRGAWL GMNFNPKGGT LVWQDNTAVN YSNWGPPGLG PSMLSHNSCY WIQSNSGLWR 

      1390       1400       1410       1420       1430       1440 
PGACTNITMG VVCKLPRAEQ SSFSPSALPE NPAALVVVLM AVLLLLALLT AALILYRRRQ 

      1450       1460       1470 
SIERGAFEGA RYSRSSSSPT EATEKNILVS DMEMNEQQE 

« Hide

References

« Hide 'large scale' references
[1]"A urokinase receptor-associated protein with specific collagen binding properties."
Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M., Danoe K.
J. Biol. Chem. 275:1993-2002(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 350-360, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, VARIANT HIS-1156.
[2]"Endo180, an endocytic recycling glycoprotein related to the macrophage mannose receptor is expressed on fibroblasts, endothelial cells and macrophages and functions as a lectin receptor."
Sheikh H., Yarwood H., Ashworth A., Isacke C.M.
J. Cell Sci. 113:1021-1032(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, GLYCOSYLATION, TISSUE SPECIFICITY, VARIANTS ILE-43 AND HIS-1156.
[3]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-1156.
Tissue: Brain.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-1156.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-1156.
[7]"Characterization of a novel member of the macrophage mannose receptor type C lectin family."
Wu K., Yuan J., Lasky L.A.
J. Biol. Chem. 271:21323-21330(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"The C-type lectin receptor Endo180 displays internalization and recycling properties distinct from other members of the mannose receptor family."
Howard M.J., Isacke C.M.
J. Biol. Chem. 277:32320-32331(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-1452; GLU-1464 AND 1468-LEU-VAL-1469.
[9]"Characterization of sugar binding by the mannose receptor family member, Endo180."
East L., Rushton S., Taylor M.E., Isacke C.M.
J. Biol. Chem. 277:50469-50475(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, MUTAGENESIS OF ASN-472.
[10]"Identification and characterization of the endocytic transmembrane glycoprotein Endo180 as a novel collagen receptor."
Wienke D., MacFadyen J.R., Isacke C.M.
Mol. Biol. Cell 14:3592-3604(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN.
[11]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69.
Tissue: Liver.
[12]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-69.
[13]"In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-1142.
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF107292 mRNA. Translation: AAF14192.1.
AF134838 mRNA. Translation: AAD30280.1.
AB014609 mRNA. Translation: BAA31684.2. Different initiation.
AC080038 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94341.1.
CH471109 Genomic DNA. Translation: EAW94342.1.
BC146647 mRNA. Translation: AAI46648.1.
BC150212 mRNA. Translation: AAI50213.1.
BC153884 mRNA. Translation: AAI53885.1.
CCDSCCDS11634.1.
RefSeqNP_006030.2. NM_006039.4.
UniGeneHs.7835.

3D structure databases

ProteinModelPortalQ9UBG0.
SMRQ9UBG0. Positions 161-361, 381-645, 681-811, 828-952, 972-1109, 1132-1235, 1260-1396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115231. 3 interactions.
IntActQ9UBG0. 1 interaction.
STRING9606.ENSP00000307513.

Protein family/group databases

MEROPSI63.001.

PTM databases

PhosphoSiteQ9UBG0.

Polymorphism databases

DMDM317373394.

Proteomic databases

MaxQBQ9UBG0.
PaxDbQ9UBG0.
PRIDEQ9UBG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303375; ENSP00000307513; ENSG00000011028.
GeneID9902.
KEGGhsa:9902.
UCSCuc002jad.4. human.

Organism-specific databases

CTD9902.
GeneCardsGC17P060704.
H-InvDBHIX0018596.
HIX0027238.
HGNCHGNC:16875. MRC2.
HPAHPA041991.
MIM612264. gene.
neXtProtNX_Q9UBG0.
PharmGKBPA134988161.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG288621.
HOGENOMHOG000231191.
HOVERGENHBG053606.
InParanoidQ9UBG0.
KOK06560.
OMAMEMNEQQ.
OrthoDBEOG7FFMQR.
PhylomeDBQ9UBG0.
TreeFamTF316663.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9UBG0.
BgeeQ9UBG0.
CleanExHS_MRC2.
GenevestigatorQ9UBG0.

Family and domain databases

Gene3D2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
[Graphical view]
SMARTSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
SSF57440. SSF57440. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 3 hits.
PS50041. C_TYPE_LECTIN_2. 8 hits.
PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMRC2. human.
GenomeRNAi9902.
NextBio37337.
PROQ9UBG0.
SOURCESearch...

Entry information

Entry nameMRC2_HUMAN
AccessionPrimary (citable) accession number: Q9UBG0
Secondary accession number(s): A6H8K4 expand/collapse secondary AC list , D3DU08, Q7LGE7, Q9Y5P9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries