UniProt ID or protein name

MRC2_HUMAN » C-type mannose receptor 2

MRC2_HUMAN » C-type mannose receptor 2
Magnify MRC2_HUMAN » C-type mannose receptor 2Enlarged view of image
3D view in Chime, Jmol or Webmol

gray dot

Download Coordinates

gray dot

Topology in Cell membrane
Topologyout side
in side
MRC2_HUMAN » C-type mannose receptor 2 » Macrophage mannose receptor 2;Urokinase-type plasminogen activator receptor-associated protein;Urokinase receptor-associated protein; UPAR-associated protein; Endocytic receptor 180;
Hydrophobic Thickness 31.2 ± 3.2 Å
Tilt Angle 37 ± 2°
ΔGtransfer -28.5 kcal/mol
Links to MRC2_HUMAN UniProtKB, Pfam, iHOP, STRING, PharmGKB, HGNC, Wikipedia, Interpro
Topology Out
Domains

AA: 187-228, PDBID: 1.00E, Subunit A, Seq Identity:51%, Fibronectin type II domain

AA: 255-361, PDBID: 1tdq, Subunit B, Seq Identity:34%, Lectin C-type domain

AA: 399-506, PDBID: 1t8c, Subunit A, Seq Identity:40%, Lectin C-type domain

AA: 538-646, PDBID: 1lit, Subunit A, Seq Identity:29%, Lectin C-type domain

AA: 693-810, PDBID: 2e3x, Subunit B, Seq Identity:30%, Lectin C-type domain

AA: 842-952, PDBID: 1t8c, Subunit A, Seq Identity:34%, Lectin C-type domain

AA: 993-1109, PDBID: 1t8c, Subunit A, Seq Identity:31%, Lectin C-type domain

AA: 1142-1245, PDBID: 1t8c, Subunit A, Seq Identity:31%, Lectin C-type domain

AA: 1286-1395, PDBID: 2os9, Subunit A, Seq Identity:27%, Lectin C-type domain

Transmembrane segments
Segments: 1412-1439
Uniprot annotation for MRC2_HUMAN » C-type mannose receptor 2
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 co-operating with the matrix metalloproteinases (MMPs).
SUBUNIT: 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.
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.
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.
DOMAIN: Fibronectin type-II domain mediates collagen-binding.
DOMAIN: Ricin B-type lectin domain contacts with the second C-type lectin domain (By similarity).
-- Uniprot annotation--
Uniprot features for MRC2_HUMAN » C-type mannose receptor 2
SIGNAL 1 30 Potential.
CHAIN 31 1479 C-type mannose receptor 2.
DOMAIN 41 167 Ricin B-type lectin.
DOMAIN 182 230 Fibronectin type-II.
DOMAIN 244 360 C-type lectin 1.
DOMAIN 389 505 C-type lectin 2.
DOMAIN 528 644 C-type lectin 3.
DOMAIN 678 809 C-type lectin 4.
DOMAIN 832 951 C-type lectin 5.
DOMAIN 979 1107 C-type lectin 6.
DOMAIN 1132 1243 C-type lectin 7.
DOMAIN 1273 1393 C-type lectin 8.
DISULFID 54 68 By similarity.
DISULFID 93 112 By similarity.
DISULFID 187 213 By similarity.
DISULFID 201 228 By similarity.
DISULFID 266 359 By similarity.
DISULFID 335 351 By similarity.
DISULFID 410 504 By similarity.
DISULFID 481 496 By similarity.
DISULFID 618 635 By similarity.
DISULFID 704 808 By similarity.
DISULFID 785 800 By similarity.
DISULFID 853 950 By similarity.
DISULFID 927 942 By similarity.
DISULFID 1078 1098 By similarity.
DISULFID 1220 1234 By similarity.
DISULFID 1369 1384 By similarity.