MRC1_MOUSE
ID MRC1_MOUSE Reviewed; 1456 AA.
AC Q61830; Q8C502;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Macrophage mannose receptor 1;
DE Short=MMR;
DE AltName: CD_antigen=CD206;
DE Flags: Precursor;
GN Name=Mrc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J; TISSUE=Macrophage;
RX PubMed=1421407;
RA Harris N., Rits M., Chang G., Ezekowitz R.A.B.;
RT "Characterization of the murine macrophage mannose receptor: demonstration
RT that the downregulation of receptor expression mediated by interferon-gamma
RT occurs at the level of transcription.";
RL Blood 80:2363-2373(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1318-1456.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 20-153 IN COMPLEX WITH
RP CARBOHYDRATE LIGAND.
RX PubMed=10748229; DOI=10.1084/jem.191.7.1105;
RA Liu Y., Chirino A.J., Misulovin Z., Leteux C., Feizi T., Nussenzweig M.C.,
RA Bjorkman P.J.;
RT "Crystal structure of the cysteine-rich domain of mannose receptor
RT complexed with a sulfated carbohydrate ligand.";
RL J. Exp. Med. 191:1105-1116(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 21-154 IN COMPLEX WITH
RP CARBOHYDRATE LIGAND.
RX PubMed=11152606; DOI=10.1006/jmbi.2000.4326;
RA Liu Y., Misulovin Z., Bjorkman P.J.;
RT "The molecular mechanism of sulfated carbohydrate recognition by the
RT cysteine-rich domain of mannose receptor.";
RL J. Mol. Biol. 305:481-490(2001).
CC -!- FUNCTION: Mediates the endocytosis of glycoproteins by macrophages.
CC Binds both sulfated and non-sulfated polysaccharide chains. Acts as
CC phagocytic receptor for bacteria, fungi and other pathogens.
CC {ECO:0000269|PubMed:1421407}.
CC -!- INTERACTION:
CC Q61830; P0DTC2: S; Xeno; NbExp=2; IntAct=EBI-642509, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Single-pass type
CC I membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Single-
CC pass type I membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in macrophages.
CC {ECO:0000269|PubMed:1421407}.
CC -!- INDUCTION: Down-regulated by interferon gamma.
CC {ECO:0000269|PubMed:1421407}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Macrophage mannose receptor;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_181";
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DR EMBL; Z11974; CAA78028.1; -; mRNA.
DR EMBL; AL845290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK079897; BAC37778.1; -; mRNA.
DR CCDS; CCDS15700.1; -.
DR PIR; A48925; A48925.
DR RefSeq; NP_032651.2; NM_008625.2.
DR PDB; 1DQG; X-ray; 1.70 A; A=20-154.
DR PDB; 1DQO; X-ray; 2.20 A; A=20-154.
DR PDB; 1FWU; X-ray; 1.90 A; A=21-154.
DR PDB; 1FWV; X-ray; 2.20 A; A=21-154.
DR PDBsum; 1DQG; -.
DR PDBsum; 1DQO; -.
DR PDBsum; 1FWU; -.
DR PDBsum; 1FWV; -.
DR AlphaFoldDB; Q61830; -.
DR SMR; Q61830; -.
DR BioGRID; 201484; 1.
DR IntAct; Q61830; 2.
DR STRING; 10090.ENSMUSP00000028045; -.
DR UniLectin; Q61830; -.
DR GlyGen; Q61830; 7 sites.
DR PhosphoSitePlus; Q61830; -.
DR CPTAC; non-CPTAC-3930; -.
DR jPOST; Q61830; -.
DR MaxQB; Q61830; -.
DR PaxDb; Q61830; -.
DR PRIDE; Q61830; -.
DR ProteomicsDB; 291441; -.
DR Antibodypedia; 72990; 803 antibodies from 43 providers.
DR DNASU; 17533; -.
DR Ensembl; ENSMUST00000028045; ENSMUSP00000028045; ENSMUSG00000026712.
DR GeneID; 17533; -.
DR KEGG; mmu:17533; -.
DR UCSC; uc008ikk.2; mouse.
DR CTD; 4360; -.
DR MGI; MGI:97142; Mrc1.
DR VEuPathDB; HostDB:ENSMUSG00000026712; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT01050000244842; -.
DR HOGENOM; CLU_002069_0_0_1; -.
DR InParanoid; Q61830; -.
DR OMA; VPTDGFI; -.
DR OrthoDB; 29241at2759; -.
DR PhylomeDB; Q61830; -.
DR TreeFam; TF316663; -.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR BioGRID-ORCS; 17533; 5 hits in 72 CRISPR screens.
DR EvolutionaryTrace; Q61830; -.
DR PRO; PR:Q61830; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q61830; protein.
DR Bgee; ENSMUSG00000026712; Expressed in stroma of bone marrow and 211 other tissues.
DR ExpressionAtlas; Q61830; baseline and differential.
DR Genevisible; Q61830; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0038024; F:cargo receptor activity; ISS:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IDA:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
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; 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 Pfam; PF00652; Ricin_B_lectin; 1.
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; 6.
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 3D-structure; Calcium; Cell membrane; Disulfide bond; Endocytosis;
KW Endosome; Glycoprotein; Lectin; Membrane; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1456
FT /note="Macrophage mannose receptor 1"
FT /id="PRO_0000017549"
FT TOPO_DOM 20..1388
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1389..1409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1410..1456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..142
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 163..211
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 225..341
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 369..487
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 511..626
FT /note="C-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 655..778
FT /note="C-type lectin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 807..923
FT /note="C-type lectin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 951..1079
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1101..1212
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1240..1355
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 930
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..49
FT DISULFID 74..91
FT DISULFID 102..149
FT DISULFID 168..194
FT /evidence="ECO:0000250"
FT DISULFID 182..209
FT /evidence="ECO:0000250"
FT DISULFID 247..340
FT /evidence="ECO:0000250"
FT DISULFID 316..332
FT /evidence="ECO:0000250"
FT DISULFID 391..486
FT /evidence="ECO:0000250"
FT DISULFID 463..478
FT /evidence="ECO:0000250"
FT DISULFID 532..625
FT /evidence="ECO:0000250"
FT DISULFID 600..617
FT /evidence="ECO:0000250"
FT DISULFID 680..777
FT /evidence="ECO:0000250"
FT DISULFID 753..769
FT /evidence="ECO:0000250"
FT DISULFID 828..922
FT /evidence="ECO:0000250"
FT DISULFID 899..914
FT /evidence="ECO:0000250"
FT DISULFID 976..1078
FT /evidence="ECO:0000250"
FT DISULFID 1051..1070
FT /evidence="ECO:0000250"
FT DISULFID 1122..1211
FT /evidence="ECO:0000250"
FT DISULFID 1189..1203
FT /evidence="ECO:0000250"
FT DISULFID 1262..1354
FT /evidence="ECO:0000250"
FT DISULFID 1331..1346
FT /evidence="ECO:0000250"
FT CONFLICT 826
FT /note="A -> R (in Ref. 1; CAA78028)"
FT /evidence="ECO:0000305"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1DQG"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:1DQG"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:1DQG"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1DQG"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1DQG"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1DQG"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1DQG"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:1DQG"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:1DQG"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1DQG"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1DQG"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1FWU"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1DQG"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1DQG"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1DQG"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:1DQG"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1DQG"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1DQG"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1DQG"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:1DQG"
SQ SEQUENCE 1456 AA; 164981 MW; FD568C1B812214D2 CRC64;
MRLLLLLAFI SVIPVSVQLL DARQFLIYNE DHKRCVDALS AISVQTATCN PEAESQKFRW
VSDSQIMSVA FKLCLGVPSK TDWASVTLYA CDSKSEYQKW ECKNDTLFGI KGTELYFNYG
NRQEKNIKLY KGSGLWSRWK VYGTTDDLCS RGYEAMYSLL GNANGAVCAF PFKFENKWYA
DCTSAGRSDG WLWCGTTTDY DKDKLFGFCP LHFEGSERLW NKDPLTGILY QINSKSALTW
HQARASCKQQ NADLLSVTEI HEQMYLTGLT SSLSSGLWIG LNSLSVRSGW QWAGGSPFRY
LNWLPGSPSS EPGKSCVSLN PGKNAKWENL ECVQKLGYIC KKGNNTLNPF IIPSASDVPT
GCPNQWWPYA GHCYRIHREE KKIQKYALQA CRKEGGDLAS IHSIEEFDFI FSQLGYEPND
ELWIGLNDIK IQMYFEWSDG TPVTFTKWLP GEPSHENNRQ EDCVVMKGKD GYWADRACEQ
PLGYICKMVS QSHAVVPEGA DKGCRKGWKR HGFYCYLIGS TLSTFTDANH TCTNEKAYLT
TVEDRYEQAF LTSLVGLRPE KYFWTGLSDV QNKGTFRWTV DEQVQFTHWN ADMPGRKAGC
VAMKTGVAGG LWDVLSCEEK AKFVCKHWAE GVTRPPEPTT TPEPKCPENW GTTSKTSMCF
KLYAKGKHEK KTWFESRDFC KAIGGELASI KSKDEQQVIW RLITSSGSYH ELFWLGLTYG
SPSEGFTWSD GSPVSYENWA YGEPNNYQNV EYCGELKGDP GMSWNDINCE HLNNWICQIQ
KGKTLLPEPT PAPQDNPPVT ADGWVIYKDY QYYFSKEKET MDNARAFCKK NFGDLATIKS
ESEKKFLWKY INKNGGQSPY FIGMLISMDK KFIWMDGSKV DFVAWATGEP NFANDDENCV
TMYTNSGFWN DINCGYPNNF ICQRHNSSIN ATAMPTTPTT PGGCKEGWHL YKNKCFKIFG
FANEEKKSWQ DARQACKGLK GNLVSIENAQ EQAFVTYHMR DSTFNAWTGL NDINAEHMFL
WTAGQGVHYT NWGKGYPGGR RSSLSYEDAD CVVVIGGNSR EAGTWMDDTC DSKQGYICQT
QTDPSLPVSP TTTPKDGFVT YGKSSYSLMK LKLPWHEAET YCKDHTSLLA SILDPYSNAF
AWMKMHPFNV PIWIALNSNL TNNEYTWTDR WRVRYTNWGA DEPKLKSACV YMDVDGYWRT
SYCNESFYFL CKKSDEIPAT EPPQLPGKCP ESEQTAWIPF YGHCYYFESS FTRSWGQASL
ECLRMGASLV SIETAAESSF LSYRVEPLKS KTNFWIGMFR NVEGKWLWLN DNPVSFVNWK
TGDPSGERND CVVLASSSGL WNNIHCSSYK GFICKMPKII DPVTTHSSIT TKADQRKMDP
QPKGSSKAAG VVTVVLLIVI GAGVAAYFFY KKRHALHIPQ EATFENTLYF NSNLSPGTSD
TKDLMGNIEQ NEHAII
