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C-type mannose receptor 2 (Endocytic receptor 180) (Macrophage mannose receptor 2) (CD antigen CD280)

 MRC2_RAT                Reviewed;        1480 AA.
Q4TU93;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 1.
20-JUN-2018, entry version 94.
RecName: Full=C-type mannose receptor 2;
AltName: Full=Endocytic receptor 180;
AltName: Full=Macrophage mannose receptor 2;
AltName: CD_antigen=CD280;
Flags: Precursor;
Name=Mrc2; Synonyms=Endo180;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
GLYCOSYLATION, AND INTERACTION WITH COL1A1.
STRAIN=Sprague-Dawley;
PubMed=15817460; DOI=10.1074/jbc.M501155200;
Thomas E.K., Nakamura M., Wienke D., Isacke C.M., Pozzi A., Liang P.;
"Endo180 binds to the C-terminal region of type I collagen.";
J. Biol. Chem. 280:22596-22605(2005).
[2]
FUNCTION.
PubMed=15506989; DOI=10.1042/BJ20040966;
Mousavi S.A., Sato M., Sporstol M., Smedsrod B., Berg T., Kojima N.,
Senoo H.;
"Uptake of denatured collagen into hepatic stellate cells: evidence
for the involvement of urokinase plasminogen activator receptor-
associated protein/Endo180.";
Biochem. J. 387:39-46(2005).
-!- 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 (By
similarity). May participate in remodeling of extracellular matrix
cooperating with the matrix metalloproteinases (MMPs) secreted by
hepatic stellate cells. May mediate endocytosis of partially
degraded collagens and glycoproteins produced in the extracellular
matrix by MMPs. {ECO:0000250, ECO:0000269|PubMed:15506989}.
-!- SUBUNIT: Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to
form a tri-molecular complex. Interacts with collagen V (By
similarity). Interacts with C-terminal region of type I
collagen/COL1A1. {ECO:0000250, ECO:0000269|PubMed:15817460}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000305}.
-!- 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 (By similarity). {ECO:0000250}.
-!- DOMAIN: Fibronectin type-II domain mediates collagen-binding.
{ECO:0000250}.
-!- DOMAIN: Ricin B-type lectin domain contacts with the second C-type
lectin domain.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:15817460}.
-!- PTM: Phosphorylated. {ECO:0000250}.
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EMBL; DQ058624; AAY53886.1; -; mRNA.
RefSeq; NP_001019858.1; NM_001024687.1.
UniGene; Rn.213511; -.
ProteinModelPortal; Q4TU93; -.
SMR; Q4TU93; -.
STRING; 10116.ENSRNOP00000052010; -.
iPTMnet; Q4TU93; -.
PhosphoSitePlus; Q4TU93; -.
PaxDb; Q4TU93; -.
PRIDE; Q4TU93; -.
GeneID; 498011; -.
KEGG; rno:498011; -.
UCSC; RGD:1559436; rat.
CTD; 9902; -.
RGD; 1559436; Mrc2.
eggNOG; ENOG410IS43; Eukaryota.
eggNOG; ENOG410XQ89; LUCA.
HOGENOM; HOG000231191; -.
HOVERGEN; HBG053606; -.
InParanoid; Q4TU93; -.
KO; K06560; -.
PhylomeDB; Q4TU93; -.
PRO; PR:Q4TU93; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0005518; F:collagen binding; IPI:RGD.
GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
CDD; cd03590; CLECT_DC-SIGN_like; 1.
CDD; cd00062; FN2; 1.
CDD; cd00161; RICIN; 1.
Gene3D; 2.10.10.10; -; 1.
Gene3D; 3.10.100.10; -; 8.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR033989; CD209-like_CTLD.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR013806; Kringle-like.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00040; fn2; 1.
Pfam; PF00059; Lectin_C; 8.
SMART; SM00034; CLECT; 8.
SMART; SM00059; FN2; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF56436; SSF56436; 8.
SUPFAM; SSF57440; SSF57440; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 3.
PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
PROSITE; PS00023; FN2_1; 1.
PROSITE; PS51092; FN2_2; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
1: Evidence at protein level;
Calcium; Cell membrane; Complete proteome; Disulfide bond;
Endocytosis; Glycoprotein; Isopeptide bond; Lectin; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 1480 C-type mannose receptor 2.
/FTId=PRO_0000046080.
TOPO_DOM 31 1413 Extracellular. {ECO:0000255}.
TRANSMEM 1414 1434 Helical. {ECO:0000255}.
TOPO_DOM 1435 1480 Cytoplasmic. {ECO:0000255}.
DOMAIN 40 166 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
DOMAIN 181 229 Fibronectin type-II.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 243 359 C-type lectin 1. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 388 504 C-type lectin 2. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 527 643 C-type lectin 3. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 677 808 C-type lectin 4. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 831 950 C-type lectin 5. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 978 1106 C-type lectin 6. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 1131 1242 C-type lectin 7. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 1271 1391 C-type lectin 8. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1028 1028 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1348 1348 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 53 67 {ECO:0000250}.
DISULFID 92 111 {ECO:0000250}.
DISULFID 186 212 {ECO:0000250}.
DISULFID 200 227 {ECO:0000250}.
DISULFID 265 358 {ECO:0000250}.
DISULFID 334 350 {ECO:0000250}.
DISULFID 409 503 {ECO:0000250}.
DISULFID 480 495 {ECO:0000250}.
DISULFID 617 634 {ECO:0000250}.
DISULFID 703 807 {ECO:0000250}.
DISULFID 784 799 {ECO:0000250}.
DISULFID 852 949 {ECO:0000250}.
DISULFID 926 941 {ECO:0000250}.
DISULFID 1077 1097 {ECO:0000250}.
DISULFID 1219 1233 {ECO:0000250}.
DISULFID 1367 1382 {ECO:0000250}.
CROSSLNK 1141 1141 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q9UBG0}.
SEQUENCE 1480 AA; 167022 MW; 7E0E5C9542C95072 CRC64;
MGPIRPALAP WPRHLLRCVL LLGGLRLGHP ADSAAALLEP DVFLIFSQGM QGCLEAQGVQ
VRVIPVCNAS LPAQRWKWVS RNRLFNLGAM QCLGTGWPAT NTTVSLGMYE CDREALSLRW
QCRTLGDQLS LLLGARANNA SKPGTLERGD QTRSGHWNIY GSEEDLCARP YYEVYTIQGN
SHGKPCTIPF KYDNQWFHGC TSTGREDGHL WCATTQDYGK DERWGFCPIK SNDCETFWDK
DQLTDSCYQF NFQSTLSWRE AWASCEQQGA DLLSITEIHE QTYINGLLTG YSSTLWIGLN
DLDTSGGWQW SDNSPLKYLN WESDQPDNPG EENCGVIRTE SSGGWQNHDC SIALPYVCKK
KPNATAEPIQ PDRWANVKVE CDPSWQPFQG HCYRLQAEKR SWQESKRACL RGGGDLLSIH
SMTELEFITK QIKQEVEELW IGLNDLKLQM NFEWSDGSLV SFTHWHPFEP NNFRDSLEDC
VTIWGPEGRW NDSPCNQSLP SICKKAGRLS QGTAEEDHGC RKGWTWHSPS CYWLGEDQVI
YSDARRLCTD HGSQLVTITN RFEQAFVSSL IYNWEGEYFW TALQDLNSTG SFRWLSGDEV
MYTHWNRDQP GYRRGGCVAL ATGSAMGLWE VKNCTSFRAR YICRQSLGTP VTPELPGPDP
TPSLTGSCPQ GWVSDPKLRH CYKVFSSERL QEKKSWIEAL GVCRELGAQL LSLASYEEEH
FVANMLNKIF GESEPENHEQ HWFWIGLNRR DPREGHSWRW SDGLGFSYHN FARSQHDDDN
IRGCAVLDLA SLQWVAMQCQ TQLDWICKIP RGVDVREPDI GRQGRLEWVR FQEAEYKFFE
HHSSWAQAQR ICTWFQAELT SVHSQAELDF LGQNMQKLSS DQEQHWWIGL HTSESDGRFR
WSDGSVINFV SWAPGKPRPI GKDKKCVYMT ARQEDWGDQR CHTALPYICK RSNSSGETRP
HDLPPSTLGG CPSGWNQFLN KCFRIQGQDP QDRVKWSEAQ FSCEQQEAQL VTIANPLEQA
YITASLPNVT FDLWIGLHGS QRDFQWIEQE PLLYTNWAPG EPSGPSPAPS GTKPTSCAVI
LHSPSAHFTG RWDDRSCTEE THGFICQKGT DPSLSPSPAA ALPAPGTELS YLNRTFRLLQ
KPLRWKDALL LCESRNASLA HVPDPYTQAF LTQAARGLQA PLWIGLASEE GSRRYSWLSE
EPLNYASWQD GEPQHTGGCA YVDVDGTWRT TSCDTKLQGA VCGVSRGPPP PRISYRGSCP
QGLADSSWIP FREHCYSFHT ELLLGHKEAL QRCQRAGGTV LSILDEMENV FVWEHLQTAE
TQSRGAWLGM NFNPKGGMLV WQDNTAVNYS NWGPPGLGPS MLSHNSCYWI QSSSGLWRPG
ACTNVTMGVV CKLPRVEENG FLPSAALPEN PVALVVVLTA AVLLLLALLT GALILYRRRQ
SAERGSFEGA RYSRSSRSGP AEATEKNILV SDMEMNEQQE


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