MRC2_RAT
ID MRC2_RAT Reviewed; 1480 AA.
AC Q4TU93;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=C-type mannose receptor 2;
DE AltName: Full=Endocytic receptor 180;
DE AltName: Full=Macrophage mannose receptor 2;
DE AltName: CD_antigen=CD280;
DE Flags: Precursor;
GN Name=Mrc2; Synonyms=Endo180;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY,
RP GLYCOSYLATION, AND INTERACTION WITH COL1A1.
RC STRAIN=Sprague-Dawley;
RX PubMed=15817460; DOI=10.1074/jbc.m501155200;
RA Thomas E.K., Nakamura M., Wienke D., Isacke C.M., Pozzi A., Liang P.;
RT "Endo180 binds to the C-terminal region of type I collagen.";
RL J. Biol. Chem. 280:22596-22605(2005).
RN [2]
RP FUNCTION.
RX PubMed=15506989; DOI=10.1042/bj20040966;
RA Mousavi S.A., Sato M., Sporstol M., Smedsrod B., Berg T., Kojima N.,
RA Senoo H.;
RT "Uptake of denatured collagen into hepatic stellate cells: evidence for the
RT involvement of urokinase plasminogen activator receptor-associated
RT protein/Endo180.";
RL Biochem. J. 387:39-46(2005).
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 (By similarity). May participate in
CC remodeling of extracellular matrix cooperating with the matrix
CC metalloproteinases (MMPs) secreted by hepatic stellate cells. May
CC mediate endocytosis of partially degraded collagens and glycoproteins
CC produced in the extracellular matrix by MMPs. {ECO:0000250,
CC ECO:0000269|PubMed:15506989}.
CC -!- SUBUNIT: Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to form a
CC tri-molecular complex. Interacts with collagen V (By similarity).
CC Interacts with C-terminal region of type I collagen/COL1A1.
CC {ECO:0000250, ECO:0000269|PubMed:15817460}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Fibronectin type-II domain mediates collagen-binding.
CC {ECO:0000250}.
CC -!- DOMAIN: Ricin B-type lectin domain contacts with the second C-type
CC lectin domain.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15817460}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; DQ058624; AAY53886.1; -; mRNA.
DR RefSeq; NP_001019858.1; NM_001024687.1.
DR AlphaFoldDB; Q4TU93; -.
DR SMR; Q4TU93; -.
DR STRING; 10116.ENSRNOP00000052010; -.
DR GlyGen; Q4TU93; 5 sites.
DR iPTMnet; Q4TU93; -.
DR PhosphoSitePlus; Q4TU93; -.
DR PaxDb; Q4TU93; -.
DR PRIDE; Q4TU93; -.
DR GeneID; 498011; -.
DR KEGG; rno:498011; -.
DR UCSC; RGD:1559436; rat.
DR CTD; 9902; -.
DR RGD; 1559436; Mrc2.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q4TU93; -.
DR PhylomeDB; Q4TU93; -.
DR Reactome; R-RNO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR PRO; PR:Q4TU93; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IPI:RGD.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0030574; P:collagen catabolic process; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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 Calcium; Cell membrane; Disulfide bond; Endocytosis; Glycoprotein;
KW Isopeptide bond; Lectin; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1480
FT /note="C-type mannose receptor 2"
FT /id="PRO_0000046080"
FT TOPO_DOM 31..1413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1414..1434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1435..1480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..166
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 181..229
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 243..359
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 388..504
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 527..643
FT /note="C-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 677..808
FT /note="C-type lectin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 831..950
FT /note="C-type lectin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 978..1106
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1131..1242
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1271..1391
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1446..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1028
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..67
FT /evidence="ECO:0000250"
FT DISULFID 92..111
FT /evidence="ECO:0000250"
FT DISULFID 186..212
FT /evidence="ECO:0000250"
FT DISULFID 200..227
FT /evidence="ECO:0000250"
FT DISULFID 265..358
FT /evidence="ECO:0000250"
FT DISULFID 334..350
FT /evidence="ECO:0000250"
FT DISULFID 409..503
FT /evidence="ECO:0000250"
FT DISULFID 480..495
FT /evidence="ECO:0000250"
FT DISULFID 617..634
FT /evidence="ECO:0000250"
FT DISULFID 703..807
FT /evidence="ECO:0000250"
FT DISULFID 784..799
FT /evidence="ECO:0000250"
FT DISULFID 852..949
FT /evidence="ECO:0000250"
FT DISULFID 926..941
FT /evidence="ECO:0000250"
FT DISULFID 1077..1097
FT /evidence="ECO:0000250"
FT DISULFID 1219..1233
FT /evidence="ECO:0000250"
FT DISULFID 1367..1382
FT /evidence="ECO:0000250"
FT CROSSLNK 1141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBG0"
SQ 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
