ID C163A_MOUSE Reviewed; 1121 AA.
AC Q2VLH6; A6H691; Q2VLH5; Q99MX8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Scavenger receptor cysteine-rich type 1 protein M130;
DE AltName: CD_antigen=CD163;
DE Contains:
DE RecName: Full=Soluble CD163;
DE Short=sCD163;
DE Flags: Precursor;
GN Name=Cd163; Synonyms=M130;
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] (ISOFORM 1), INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11345593; DOI=10.1007/s002510100304;
RA Schaer D.J., Boretti F.S., Hongegger A., Poehler D., Linnscheid P.,
RA Staege H., Mueller C., Schoedon G., Schaffner A.;
RT "Molecular cloning and characterization of the mouse CD163 homologue, a
RT highly glucocorticoid-inducible member of the scavenger receptor cysteine-
RT rich family.";
RL Immunogenetics 53:170-177(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=BALB/cJ;
RA Welch S.-K.W., Calvert J.G., Slade D.E., Shields S.L.;
RT "Scavenger receptor cd163 is a cell permissive factor for infection with
RT porcine reproductive and respiratory syndrome viruses.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, and Spleen;
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).
CC -!- FUNCTION: Involved in clearance and endocytosis of
CC hemoglobin/haptoglobin complexes by macrophages and may thereby protect
CC tissues from free hemoglobin-mediated oxidative damage. May play a role
CC in the uptake and recycling of iron, via endocytosis of
CC hemoglobin/haptoglobin and subsequent breakdown of heme. Binds
CC hemoglobin/haptoglobin complexes in a calcium-dependent and pH-
CC dependent manner. Induces a cascade of intracellular signals that
CC involves tyrosine kinase-dependent calcium mobilization, inositol
CC triphosphate production and secretion of IL6 and CSF1 (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: After shedding, the soluble form (sCD163) may play an anti-
CC inflammatory role. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CSNK2B. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Soluble CD163]: Secreted
CC {ECO:0000250|UniProtKB:Q86VB7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86VB7};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q86VB7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CD163v2;
CC IsoId=Q2VLH6-1; Sequence=Displayed;
CC Name=2; Synonyms=CD163v3;
CC IsoId=Q2VLH6-2; Sequence=VSP_019016;
CC -!- TISSUE SPECIFICITY: Expressed in monocytes and mature macrophages such
CC as Kupffer cells in the liver, red pulp macrophages in the spleen and
CC mesenteric lymph nodes. {ECO:0000269|PubMed:11345593}.
CC -!- INDUCTION: Induced by anti-inflammatory mediators such as
CC glucocorticoids and IL10; suppressed by IL4.
CC {ECO:0000269|PubMed:11345593}.
CC -!- DOMAIN: The SRCR domain 3 mediates calcium-sensitive interaction with
CC hemoglobin/haptoglobin complexes. {ECO:0000250}.
CC -!- PTM: A soluble form (sCD163) is produced by proteolytic shedding which
CC can be induced by lipopolysaccharide, phorbol ester and Fc region of
CC immunoglobulin gamma. This cleavage is dependent on protein kinase C
CC and tyrosine kinases and can be blocked by protease inhibitors. The
CC shedding is inhibited by the tissue inhibitor of metalloproteinase
CC TIMP3, and thus probably induced by membrane-bound metalloproteinases
CC ADAMs (By similarity). {ECO:0000250}.
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DR EMBL; AF274883; AAK16065.1; -; mRNA.
DR EMBL; DQ058616; AAY99763.1; -; mRNA.
DR EMBL; DQ058617; AAY99764.1; -; mRNA.
DR EMBL; CH466523; EDK99729.1; -; Genomic_DNA.
DR EMBL; BC145793; AAI45794.1; -; mRNA.
DR CCDS; CCDS20516.1; -. [Q2VLH6-1]
DR CCDS; CCDS51905.1; -. [Q2VLH6-2]
DR RefSeq; NP_444324.2; NM_053094.2. [Q2VLH6-1]
DR AlphaFoldDB; Q2VLH6; -.
DR SMR; Q2VLH6; -.
DR STRING; 10090.ENSMUSP00000108160; -.
DR GlyConnect; 2428; 2 N-Linked glycans (1 site). [Q2VLH6-2]
DR GlyCosmos; Q2VLH6; 3 sites, 2 glycans.
DR GlyGen; Q2VLH6; 3 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q2VLH6; -.
DR PhosphoSitePlus; Q2VLH6; -.
DR SwissPalm; Q2VLH6; -.
DR MaxQB; Q2VLH6; -.
DR PaxDb; 10090-ENSMUSP00000108160; -.
DR ProteomicsDB; 265458; -. [Q2VLH6-1]
DR ProteomicsDB; 265459; -. [Q2VLH6-2]
DR Antibodypedia; 3721; 1785 antibodies from 46 providers.
DR DNASU; 93671; -.
DR Ensembl; ENSMUST00000032234.5; ENSMUSP00000032234.3; ENSMUSG00000008845.10. [Q2VLH6-1]
DR Ensembl; ENSMUST00000112541.8; ENSMUSP00000108160.3; ENSMUSG00000008845.10. [Q2VLH6-2]
DR GeneID; 93671; -.
DR KEGG; mmu:93671; -.
DR UCSC; uc009dqn.2; mouse. [Q2VLH6-1]
DR AGR; MGI:2135946; -.
DR CTD; 9332; -.
DR MGI; MGI:2135946; Cd163.
DR VEuPathDB; HostDB:ENSMUSG00000008845; -.
DR eggNOG; ENOG502QQ5W; Eukaryota.
DR GeneTree; ENSGT00940000155987; -.
DR HOGENOM; CLU_002555_0_1_1; -.
DR InParanoid; Q2VLH6; -.
DR OMA; AGENKCS; -.
DR OrthoDB; 5403281at2759; -.
DR TreeFam; TF329295; -.
DR Reactome; R-MMU-2168880; Scavenging of heme from plasma.
DR BioGRID-ORCS; 93671; 1 hit in 77 CRISPR screens.
DR PRO; PR:Q2VLH6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q2VLH6; Protein.
DR Bgee; ENSMUSG00000008845; Expressed in stroma of bone marrow and 101 other cell types or tissues.
DR ExpressionAtlas; Q2VLH6; baseline and differential.
DR Genevisible; Q2VLH6; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; ISO:MGI.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR Gene3D; 3.10.250.10; SRCR-like domain; 9.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48071:SF15; SRCR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00530; SRCR; 9.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 9.
DR SUPFAM; SSF56487; SRCR-like; 9.
DR PROSITE; PS00420; SRCR_1; 3.
DR PROSITE; PS50287; SRCR_2; 9.
PE 1: Evidence at protein level;
KW Acute phase; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Inflammatory response; Membrane; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..1121
FT /note="Scavenger receptor cysteine-rich type 1 protein
FT M130"
FT /id="PRO_0000238940"
FT CHAIN 39..?
FT /note="Soluble CD163"
FT /id="PRO_0000238941"
FT TOPO_DOM 39..1045
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1046..1066
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1067..1121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 50..150
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 157..258
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 265..365
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 372..472
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 477..577
FT /note="SRCR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 582..682
FT /note="SRCR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 719..819
FT /note="SRCR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 824..927
FT /note="SRCR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 930..1030
FT /note="SRCR 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT MOTIF 1091..1094
FT /note="Internalization signal"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 88..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 119..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 183..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 196..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 227..237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 290..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 303..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 334..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 397..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 410..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 441..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 502..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 515..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 546..556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 607..671
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 620..681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 651..661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 744..808
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 757..818
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 788..798
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 864..926
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 895..905
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 955..1019
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 968..1029
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 999..1009
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT VAR_SEQ 1108..1121
FT /note="GVIQRHTEKENDNL -> ENSNNSYDFNDDGLTSLSKYLPISGIKKGSFRGT
FT LRRKMIIYNPLRLEFKKP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_019016"
FT CONFLICT 492
FT /note="V -> M (in Ref. 2; AAY99764)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="Y -> C (in Ref. 1; AAK16065)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="N -> S (in Ref. 2; AAY99763)"
FT /evidence="ECO:0000305"
FT CONFLICT 950
FT /note="S -> F (in Ref. 2; AAY99763)"
FT /evidence="ECO:0000305"
FT CONFLICT 1072
FT /note="Q -> R (in Ref. 1; AAK16065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1121 AA; 120921 MW; 553B1EF5ED5064BD CRC64;
MGGHRMVLLG GAGSPGCKRF VHLGFFVVAV SSLLSASAVT NAPGEMKKEL RLAGGENNCS
GRVELKIHDK WGTVCSNGWS MNEVSVVCQQ LGCPTSIKAL GWANSSAGSG YIWMDKVSCT
GNESALWDCK HDGWGKHNCT HEKDAGVTCS DGSNLEMRLV NSAGHRCLGR VEIKFQGKWG
TVCDDNFSKD HASVICKQLG CGSAISFSGS AKLGAGSGPI WLDDLACNGN ESALWDCKHR
GWGKHNCDHA EDVGVICLEG ADLSLRLVDG VSRCSGRLEV RFQGEWGTVC DDNWDLRDAS
VVCKQLGCPT AISAIGRVNA SEGSGQIWLD NISCEGHEAT LWECKHQEWG KHYCHHREDA
GVTCSDGADL ELRLVGGGSR CAGIVEVEIQ KLTGKMCSRG WTLADADVVC RQLGCGSALQ
TQAKIYSKTG ATNTWLFPGS CNGNETTFWQ CKNWQWGGLS CDNFEEAKVT CSGHREPRLV
GGEIPCSGRV EVKHGDVWGS VCDFDLSLEA ASVVCRELQC GTVVSILGGA HFGEGSGQIW
GEEFQCSGDE SHLSLCSVAP PLDRTCTHSR DVSVVCSRYI DIRLAGGESS CEGRVELKTL
GAWGPLCSSH WDMEDAHVLC QQLKCGVAQS IPEGAHFGKG AGQVWSHMFH CTGTEEHIGD
CLMTALGAPT CSEGQVASVI CSGNQSQTLL PCSSLSPVQT TSSTIPKESE VPCIASGQLR
LVGGGGRCAG RVEVYHEGSW GTVCDDNWDM TDANVVCKQL DCGVAINATG SAYFGEGAGA
IWLDEVICTG KESHIWQCHS HGWGRHNCRH KEDAGVICSE FMSLRLTNEA HKENCTGRLE
VFYNGTWGSI GSSNMSPTTV GVVCRQLGCA DNGTVKPIPS DKTPSRPMWV DRVQCPKGVD
TLWQCPSSPW KQRQASPSSQ ESWIICDNKI RLQEGHTDCS GRVEIWHKGS WGTVCDDSWD
LNDAKVVCKQ LGCGQAVKAL KEAAFGPGTG PIWLNEIKCR GNESSLWDCP AKPWSHSDCG
HKEDASIQCL PKMTSESHHG TGHPTLTALL VCGAILLVLL IVFLLWTLKR RQIQRLTVSS
RGEVLIHQVQ YQEMDSKADD LDLLKSSGVI QRHTEKENDN L
//
