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Protein

C-type mannose receptor 2

Gene

Mrc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs).3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
C-type mannose receptor 2
Alternative name(s):
Lectin lambda
Macrophage mannose receptor 2
CD_antigen: CD280
Gene namesi
Name:Mrc2
Synonyms:Kiaa0709
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:107818. Mrc2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 14131383ExtracellularSequence analysisAdd
BLAST
Transmembranei1414 – 143421HelicalSequence analysisAdd
BLAST
Topological domaini1435 – 147945CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Mice show impaired mammary tumor growth. Tumors from mice lacking Mrc2 display an abrogation of cellular collagen uptake, a fibrotic state characterized by the accumulation of both basement membrane and interstitial collagens, and an overall tumor size reduction, despite the collagen accumulation. Fibroblasts from mice lacking Mrc2 display a severe impairment of internalization of collagen IV and V and thus, exhibit a general deficiency in uptake and delivery of collagens to vesicular compartments. Fibroblasts also have diminished initial adhesion to collagen as well as impaired migration on fibrillar collagen. Mice with a targeted deletion of Mrc2 exon 2-6 are phenotypically normal, healthy and fertile. This deletion resulted in expression of a protein that lacks the ricin B-type lectin domain, the fibronectin type-II domain and the first C-type lectin domain. Fibroblasts from these mice display C-type lectin activity, but have a defect in collagen-binding and internalization, and an impaired migratory phenotype.4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Chaini31 – 14791449C-type mannose receptor 2PRO_0000046079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi92 ↔ 111By similarity
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence analysis
Glycosylationi139 – 1391N-linked (GlcNAc...)1 Publication
Disulfide bondi186 ↔ 212By similarity
Disulfide bondi200 ↔ 227By similarity
Disulfide bondi265 ↔ 358By similarity
Disulfide bondi334 ↔ 350By similarity
Glycosylationi363 – 3631N-linked (GlcNAc...)1 Publication
Disulfide bondi409 ↔ 503By similarity
Disulfide bondi480 ↔ 495By similarity
Disulfide bondi617 ↔ 634By similarity
Disulfide bondi703 ↔ 807By similarity
Disulfide bondi784 ↔ 799By similarity
Disulfide bondi852 ↔ 949By similarity
Disulfide bondi926 ↔ 941By similarity
Glycosylationi1028 – 10281N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1077 ↔ 1097By similarity
Cross-linki1141 – 1141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Disulfide bondi1219 ↔ 1233By similarity
Glycosylationi1348 – 13481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1367 ↔ 1382By similarity

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ64449.
PaxDbiQ64449.
PeptideAtlasiQ64449.
PRIDEiQ64449.

PTM databases

iPTMnetiQ64449.
PhosphoSiteiQ64449.

Expressioni

Tissue specificityi

Highly expressed in heart, lung and kidney, but little or no expression in brain, thymus or adult liver. Expressed at highly endothelialized sites such as those in choroid plexus and kidney glomerulai as well as in chondrocytes in cartilaginous regions of the embryo.1 Publication

Developmental stagei

Highly expressed at day 7 of embryonic development and detected throughout the later stages of embryonic development.1 Publication

Gene expression databases

BgeeiENSMUSG00000020695.
CleanExiMM_MRC2.
ExpressionAtlasiQ64449. baseline and differential.
GenevisibleiQ64449. MM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

MINTiMINT-4997385.

Structurei

3D structure databases

ProteinModelPortaliQ64449.
SMRiQ64449. Positions 43-171, 176-360, 380-506, 519-644, 681-810, 827-951, 971-1108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 190154Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST
Domaini181 – 22949Fibronectin type-IIPROSITE-ProRule annotationAdd
BLAST
Domaini243 – 359117C-type lectin 1PROSITE-ProRule annotationAdd
BLAST
Domaini388 – 504117C-type lectin 2PROSITE-ProRule annotationAdd
BLAST
Domaini527 – 643117C-type lectin 3PROSITE-ProRule annotationAdd
BLAST
Domaini677 – 808132C-type lectin 4PROSITE-ProRule annotationAdd
BLAST
Domaini831 – 950120C-type lectin 5PROSITE-ProRule annotationAdd
BLAST
Domaini978 – 1106129C-type lectin 6PROSITE-ProRule annotationAdd
BLAST
Domaini1131 – 1242112C-type lectin 7PROSITE-ProRule annotationAdd
BLAST
Domaini1271 – 1391121C-type lectin 8PROSITE-ProRule annotationAdd
BLAST

Domaini

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 (By similarity).By similarity
Fibronectin type-II domain mediates collagen-binding.By similarity
Ricin B-type lectin domain contacts with the second C-type lectin domain.

Sequence similaritiesi

Contains 8 C-type lectin domains.PROSITE-ProRule annotation
Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KDF3. Eukaryota.
ENOG410XQ89. LUCA.
GeneTreeiENSGT00720000108514.
HOGENOMiHOG000231191.
HOVERGENiHBG053606.
InParanoidiQ64449.
KOiK06560.
OMAiIGLHASQ.
OrthoDBiEOG091G0EGC.
TreeFamiTF316663.

Family and domain databases

CDDicd00062. FN2. 1 hit.
Gene3Di2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProiIPR001304. 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]
PfamiPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
[Graphical view]
SMARTiSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00615. 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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q64449-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVPIRPALAP WPRHLLRCVL LLGGLRLGHP ADSAAALLEP DVFLIFSQGM
60 70 80 90 100
QGCLEAQGVQ VRVTPVCNAS LPAQRWKWVS RNRLFNLGAT QCLGTGWPVT
110 120 130 140 150
NTTVSLGMYE CDREALSLRW QCRTLGDQLS LLLGARASNA SKPGTLERGD
160 170 180 190 200
QTRSGHWNIY GSEEDLCARP YYEVYTIQGN SHGKPCTIPF KYDNQWFHGC
210 220 230 240 250
TSTGREDGHL WCATTQDYGK DERWGFCPIK SNDCETFWDK DQLTDSCYQF
260 270 280 290 300
NFQSTLSWRE AWASCEQQGA DLLSITEIHE QTYINGLLTG YSSTLWIGLN
310 320 330 340 350
DLDTSGGWQW SDNSPLKYLN WESDQPDNPG EENCGVIRTE SSGGWQNHDC
360 370 380 390 400
SIALPYVCKK KPNATVEPIQ PDRWTNVKVE CDPSWQPFQG HCYRLQAEKR
410 420 430 440 450
SWQESKRACL RGGGDLLSIH SMAELEFITK QIKQEVEELW IGLNDLKLQM
460 470 480 490 500
NFEWSDGSLV SFTHWHPFEP NNFRDSLEDC VTIWGPEGRW NDSPCNQSLP
510 520 530 540 550
SICKKAGRLS QGAAEEDHGC RKGWTWHSPS CYWLGEDQVI YSDARRLCTD
560 570 580 590 600
HGSQLVTITN RFEQAFVSSL IYNWEGEYFW TALQDLNSTG SFRWLSGDEV
610 620 630 640 650
IYTHWNRDQP GYRRGGCVAL ATGSAMGLWE VKNCTSFRAR YICRQSLGTP
660 670 680 690 700
VTPELPGPDP TPSLTGSCPQ GWVSDPKLRH CYKVFSSERL QEKKSWIQAL
710 720 730 740 750
GVCRELGAQL LSLASYEEEH FVAHMLNKIF GESEPESHEQ HWFWIGLNRR
760 770 780 790 800
DPREGHSWRW SDGLGFSYHN FARSRHDDDD IRGCAVLDLA SLQWVPMQCQ
810 820 830 840 850
TQLDWICKIP RGVDVREPDI GRQGRLEWVR FQEAEYKFFE HHSSWAQAQR
860 870 880 890 900
ICTWFQADLT SVHSQAELDF LGQNLQKLSS DQEQHWWIGL HTLESDGRFR
910 920 930 940 950
WTDGSIINFI SWAPGKPRPI GKDKKCVYMT ARQEDWGDQR CHTALPYICK
960 970 980 990 1000
RSNSSGETQP QDLPPSALGG CPSGWNQFLN KCFRIQGQDP QDRVKWSEAQ
1010 1020 1030 1040 1050
FSCEQQEAQL VTIANPLEQA FITASLPNVT FDLWIGLHAS QRDFQWIEQE
1060 1070 1080 1090 1100
PLLYTNWAPG EPSGPSPAPS GTKPTSCAVI LHSPSAHFTG RWDDRSCTEE
1110 1120 1130 1140 1150
THGFICQKGT DPSLSPSPAA TPPAPGAELS YLNHTFRLLQ KPLRWKDALL
1160 1170 1180 1190 1200
LCESRNASLA HVPDPYTQAF LTQAARGLQT PLWIGLASEE GSRRYSWLSE
1210 1220 1230 1240 1250
EPLNYVSWQD EEPQHSGGCA YVDVDGTWRT TSCDTKLQGA VCGVSRGPPP
1260 1270 1280 1290 1300
RRINYRGSCP QGLADSSWIP FREHCYSFHM EVLLGHKEAL QRCQKAGGTV
1310 1320 1330 1340 1350
LSILDEMENV FVWEHLQTAE AQSRGAWLGM NFNPKGGTLV WQDNTAVNYS
1360 1370 1380 1390 1400
NWGPPGLGPS MLSHNSCYWI QSSSGLWRPG ACTNITMGVV CKLPRVEENS
1410 1420 1430 1440 1450
FLPSAALPES PVALVVVLTA VLLLLALMTA ALILYRRRQS AERGSFEGAR
1460 1470
YSRSSHSGPA EATEKNILVS DMEMNEQQE
Length:1,479
Mass (Da):167,074
Last modified:July 27, 2011 - v3
Checksum:iAFC78624FE331E32
GO
Isoform 2 (identifier: Q64449-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     173-180: EVYTIQGN → GEGSIAKS
     181-1479: Missing.

Note: No experimental confirmation available.
Show »
Length:180
Mass (Da):19,706
Checksum:iB83C2ABEC02029D4
GO

Sequence cautioni

The sequence AAC52729 differs from that shown. Reason: Frameshift at positions 120 and 145. Curated
The sequence BAC35672 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661V → F in AAC52729 (PubMed:8702911).Curated
Sequence conflicti519 – 5191G → D in AAC52729 (PubMed:8702911).Curated
Sequence conflicti869 – 8691D → G in AAC52729 (PubMed:8702911).Curated
Sequence conflicti984 – 9841R → Q in BAC98005 (PubMed:14621295).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei173 – 1808EVYTIQGN → GEGSIAKS in isoform 2. 1 PublicationVSP_017223
Alternative sequencei181 – 14791299Missing in isoform 2. 1 PublicationVSP_017224Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56734 mRNA. Translation: AAC52729.1. Frameshift.
AK054150 mRNA. Translation: BAC35672.1. Different initiation.
AL645684, AL645471, AL645572 Genomic DNA. Translation: CAM22193.1.
AL645572, AL645471, AL645684 Genomic DNA. Translation: CAM22804.1.
AL645471, AL645572, AL645684 Genomic DNA. Translation: CAM24832.1.
AK129195 mRNA. Translation: BAC98005.1.
CCDSiCCDS25539.1. [Q64449-1]
PIRiT42710.
RefSeqiNP_032652.3. NM_008626.3. [Q64449-1]
UniGeneiMm.235616.

Genome annotation databases

EnsembliENSMUST00000100335; ENSMUSP00000097909; ENSMUSG00000020695. [Q64449-1]
GeneIDi17534.
KEGGimmu:17534.
UCSCiuc007lxi.1. mouse. [Q64449-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Endo180

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U56734 mRNA. Translation: AAC52729.1. Frameshift.
AK054150 mRNA. Translation: BAC35672.1. Different initiation.
AL645684, AL645471, AL645572 Genomic DNA. Translation: CAM22193.1.
AL645572, AL645471, AL645684 Genomic DNA. Translation: CAM22804.1.
AL645471, AL645572, AL645684 Genomic DNA. Translation: CAM24832.1.
AK129195 mRNA. Translation: BAC98005.1.
CCDSiCCDS25539.1. [Q64449-1]
PIRiT42710.
RefSeqiNP_032652.3. NM_008626.3. [Q64449-1]
UniGeneiMm.235616.

3D structure databases

ProteinModelPortaliQ64449.
SMRiQ64449. Positions 43-171, 176-360, 380-506, 519-644, 681-810, 827-951, 971-1108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4997385.

PTM databases

iPTMnetiQ64449.
PhosphoSiteiQ64449.

Proteomic databases

MaxQBiQ64449.
PaxDbiQ64449.
PeptideAtlasiQ64449.
PRIDEiQ64449.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000100335; ENSMUSP00000097909; ENSMUSG00000020695. [Q64449-1]
GeneIDi17534.
KEGGimmu:17534.
UCSCiuc007lxi.1. mouse. [Q64449-1]

Organism-specific databases

CTDi9902.
MGIiMGI:107818. Mrc2.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410KDF3. Eukaryota.
ENOG410XQ89. LUCA.
GeneTreeiENSGT00720000108514.
HOGENOMiHOG000231191.
HOVERGENiHBG053606.
InParanoidiQ64449.
KOiK06560.
OMAiIGLHASQ.
OrthoDBiEOG091G0EGC.
TreeFamiTF316663.

Miscellaneous databases

PROiQ64449.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020695.
CleanExiMM_MRC2.
ExpressionAtlasiQ64449. baseline and differential.
GenevisibleiQ64449. MM.

Family and domain databases

CDDicd00062. FN2. 1 hit.
Gene3Di2.10.10.10. 1 hit.
3.10.100.10. 8 hits.
InterProiIPR001304. 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]
PfamiPF00040. fn2. 1 hit.
PF00059. Lectin_C. 8 hits.
[Graphical view]
SMARTiSM00034. CLECT. 8 hits.
SM00059. FN2. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF56436. SSF56436. 8 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00615. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiMRC2_MOUSE
AccessioniPrimary (citable) accession number: Q64449
Secondary accession number(s): A2AAB0, Q6ZQ64, Q8C6P0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.