C163A_HUMAN
ID C163A_HUMAN Reviewed; 1156 AA.
AC Q86VB7; C9JIG2; Q07898; Q07899; Q07900; Q07901; Q2VLH7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Scavenger receptor cysteine-rich type 1 protein M130;
DE AltName: Full=Hemoglobin scavenger receptor;
DE AltName: CD_antigen=CD163;
DE Contains:
DE RecName: Full=Soluble CD163;
DE Short=sCD163;
DE Flags: Precursor;
GN Name=CD163; Synonyms=M130;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND VARIANT VAL-342.
RX PubMed=8370408; DOI=10.1002/eji.1830230940;
RA Law S.K.A., Micklem K.J., Shaw J.M., Zhang X.-P., Dong Y., Willis A.C.,
RA Mason D.Y.;
RT "A new macrophage differentiation antigen which is a member of the
RT scavenger receptor superfamily.";
RL Eur. J. Immunol. 23:2320-2325(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-342.
RX PubMed=10403791; DOI=10.1006/bbrc.1999.0866;
RA Ritter M., Buechler C., Langmann T., Schmitz G.;
RT "Genomic organization and chromosomal localization of the human CD163
RT (M130) gene: a member of the scavenger receptor cysteine-rich
RT superfamily.";
RL Biochem. Biophys. Res. Commun. 260:466-474(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT VAL-342.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-342.
RC TISSUE=Spleen;
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 [6]
RP CLEAVAGE.
RX PubMed=10066432; DOI=10.1006/bbrc.1999.0294;
RA Droste A., Sorg C., Hogger P.;
RT "Shedding of CD163, a novel regulatory mechanism for a member of the
RT scavenger receptor cysteine-rich family.";
RL Biochem. Biophys. Res. Commun. 256:110-113(1999).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10577520; DOI=10.1002/jlb.66.5.858;
RA Van den Heuvel M.M., Tensen C.P., van As J.H., Van den Berg T.K.,
RA Fluitsma D.M., Dijkstra C.D., Dopp E.A., Droste A., Van Gaalen F.A.,
RA Sorg C., Hoegger P., Beelen R.H.J.;
RT "Regulation of CD 163 on human macrophages: cross-linking of CD163 induces
RT signaling and activation.";
RL J. Leukoc. Biol. 66:858-866(1999).
RN [8]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10648003; DOI=10.1002/jlb.67.1.97;
RA Buechler C., Ritter M., Orso E., Langmann T., Klucken J., Schmitz G.;
RT "Regulation of scavenger receptor CD163 expression in human monocytes and
RT macrophages by pro- and antiinflammatory stimuli.";
RL J. Leukoc. Biol. 67:97-103(2000).
RN [9]
RP FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF THR-1072 AND SER-1084, AND
RP INTERACTION WITH CSNK2B.
RX PubMed=11298324;
RX DOI=10.1002/1521-4141(200104)31:4<999::aid-immu999>3.0.co;2-r;
RA Ritter M., Buechler C., Kapinsky M., Schmitz G.;
RT "Interaction of CD163 with the regulatory subunit of casein kinase II
RT (CKII) and dependence of CD163 signaling on CKII and protein kinase C.";
RL Eur. J. Immunol. 31:999-1009(2001).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11196644; DOI=10.1038/35051594;
RA Kristiansen M., Graversen J.H., Jacobsen C., Sonne O., Hoffman H.-J.,
RA Law S.K.A., Moestrup S.K.;
RT "Identification of the haemoglobin scavenger receptor.";
RL Nature 409:198-201(2001).
RN [11]
RP CLEAVAGE, AND SUBCELLULAR LOCATION.
RX PubMed=12296867; DOI=10.1046/j.1365-2249.2002.01963.x;
RA Matsushita N., Kashiwagi M., Wait R., Nagayoshi R., Nakamura M.,
RA Matsuda T., Hogger P., Guyre P.M., Nagase H., Matsuyama T.;
RT "Elevated levels of soluble CD163 in sera and fluids from rheumatoid
RT arthritis patients and inhibition of the shedding of CD163 by TIMP-3.";
RL Clin. Exp. Immunol. 130:156-161(2002).
RN [12]
RP FUNCTION.
RX PubMed=12208511; DOI=10.1016/s0014-5793(02)03142-3;
RA Frings W., Dreier J., Sorg C.;
RT "Only the soluble form of the scavenger receptor CD163 acts inhibitory on
RT phorbol ester-activated T-lymphocytes, whereas membrane-bound protein has
RT no effect.";
RL FEBS Lett. 526:93-96(2002).
RN [13]
RP MISCELLANEOUS.
RX PubMed=12377940;
RA Hintz K.A., Rassias A.J., Wardwell K., Moss M.L., Morganelli P.M.,
RA Pioli P.A., Givan A.L., Wallace P.K., Yeager M.P., Guyre P.M.;
RT "Endotoxin induces rapid metalloproteinase-mediated shedding followed by
RT up-regulation of the monocyte hemoglobin scavenger receptor CD163.";
RL J. Leukoc. Biol. 72:711-717(2002).
RN [14]
RP RELEVANCE AS DISEASE MARKER IN INFLAMMATORY CONDITIONS.
RX PubMed=15478309; DOI=10.1080/07853890410033171;
RA Moestrup S.K., Moller H.J.;
RT "CD163: a regulated hemoglobin scavenger receptor with a role in the anti-
RT inflammatory response.";
RL Ann. Med. 36:347-354(2004).
RN [15]
RP DOMAIN, AND CLEAVAGE SITES.
RX PubMed=15448162; DOI=10.1074/jbc.m409629200;
RA Madsen M., Moller H.J., Nielsen M.J., Jacobsen C., Graversen J.H.,
RA van den Berg T., Moestrup S.K.;
RT "Molecular characterization of the haptoglobin.hemoglobin receptor CD163.
RT Ligand binding properties of the scavenger receptor cysteine-rich domain
RT region.";
RL J. Biol. Chem. 279:51561-51567(2004).
RN [16]
RP CLEAVAGE.
RX PubMed=15075364; DOI=10.1189/jlb.1003523;
RA Sulahian T.H., Pioli P.A., Wardwell K., Guyre P.M.;
RT "Cross-linking of FcgammaR triggers shedding of the hemoglobin-haptoglobin
RT scavenger receptor CD163.";
RL J. Leukoc. Biol. 76:271-277(2004).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [18]
RP FUNCTION, MUTAGENESIS OF TYR-1096, AND TISSUE SPECIFICITY.
RX PubMed=16434690; DOI=10.1189/jlb.1005602;
RA Nielsen M.J., Madsen M., Moller H.J., Moestrup S.K.;
RT "The macrophage scavenger receptor CD163: endocytic properties of
RT cytoplasmic tail variants.";
RL J. Leukoc. Biol. 79:837-845(2006).
RN [19]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105; ASN-140; ASN-767 AND
RP ASN-1027.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [20]
RP GLYCOSYLATION AT ASN-105.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Acute phase-regulated receptor involved in clearance and
CC endocytosis of hemoglobin/haptoglobin complexes by macrophages and may
CC thereby protect tissues from free hemoglobin-mediated oxidative damage.
CC May play a role 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. Exhibits a higher affinity for complexes of
CC hemoglobin and multimeric haptoglobin of HP*1F phenotype than for
CC complexes of hemoglobin and dimeric haptoglobin of HP*1S phenotype.
CC Induces a cascade of intracellular signals that involves tyrosine
CC kinase-dependent calcium mobilization, inositol triphosphate production
CC and secretion of IL6 and CSF1. Isoform 3 exhibits the higher capacity
CC for ligand endocytosis and the more pronounced surface expression when
CC expressed in cells.
CC -!- FUNCTION: After shedding, the soluble form (sCD163) may play an anti-
CC inflammatory role, and may be a valuable diagnostic parameter for
CC monitoring macrophage activation in inflammatory conditions.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 nM for hemoglobin/haptoglobin of HP*1S phenotype
CC {ECO:0000269|PubMed:11196644};
CC KM=0.2 nM for hemoglobin/haptoglobin of HP*1F phenotype
CC {ECO:0000269|PubMed:11196644};
CC -!- SUBUNIT: Interacts with CSNK2B. {ECO:0000269|PubMed:11298324}.
CC -!- INTERACTION:
CC Q86VB7; P12314: FCGR1A; NbExp=3; IntAct=EBI-2808455, EBI-2869867;
CC -!- SUBCELLULAR LOCATION: [Soluble CD163]: Secreted
CC {ECO:0000269|PubMed:12296867}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10577520,
CC ECO:0000269|PubMed:10648003}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:10577520, ECO:0000269|PubMed:10648003}.
CC Note=Isoform 1 and isoform 2 show a lower surface expression when
CC expressed in cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Long tail variant 1;
CC IsoId=Q86VB7-1; Sequence=Displayed;
CC Name=2; Synonyms=Long tail variant 2;
CC IsoId=Q86VB7-2; Sequence=VSP_019014;
CC Name=3; Synonyms=Short tail variant;
CC IsoId=Q86VB7-3; Sequence=VSP_019015;
CC Name=4;
CC IsoId=Q86VB7-4; Sequence=VSP_019013, VSP_019015;
CC -!- TISSUE SPECIFICITY: Expressed in monocytes and mature macrophages such
CC as Kupffer cells in the liver, red pulp macrophages in the spleen,
CC cortical macrophages in the thymus, resident bone marrow macrophages
CC and meningeal macrophages of the central nervous system. Expressed also
CC in blood. Isoform 1 is the lowest abundant in the blood. Isoform 2 is
CC the lowest abundant in the liver and the spleen. Isoform 3 is the
CC predominant isoform detected in the blood.
CC {ECO:0000269|PubMed:10577520, ECO:0000269|PubMed:11196644,
CC ECO:0000269|PubMed:16434690}.
CC -!- INDUCTION: Induced by anti-inflammatory mediators such as
CC glucocorticoids, interleukin-6/IL6 and interleukin-10/IL10; suppressed
CC by pro-inflammatory mediators like bacterial lipopolysaccharides (LPS),
CC IFNG/IFN-gamma and TNF. {ECO:0000269|PubMed:10577520,
CC ECO:0000269|PubMed:10648003}.
CC -!- DOMAIN: The SRCR domain 3 mediates calcium-sensitive interaction with
CC hemoglobin/haptoglobin complexes. {ECO:0000269|PubMed:15448162}.
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. {ECO:0000269|PubMed:10066432, ECO:0000269|PubMed:12296867,
CC ECO:0000269|PubMed:15075364, ECO:0000269|PubMed:15448162}.
CC -!- PTM: Phosphorylated. {ECO:0000305|PubMed:11298324}.
CC -!- MISCELLANEOUS: Intravenous lipopolysaccharide (LPS) produces a rapid
CC rise of sCD163 in plasma of patient as it induces metalloproteinase-
CC mediated shedding from monocytes surface. Long-term LPS infusion
CC finally increases expression of the membrane-bound form on circulating
CC monocytes.
CC -!- MISCELLANEOUS: The soluble form (sCD163) in plasma is a novel parameter
CC in diseases affecting macrophage function and monocyte/macrophage load
CC in the body. The concentration of sCD163 is probably reflecting the
CC number of macrophages of the 'alternative macrophage activation'
CC phenotype with a high CD163 expression playing a major role in
CC dampening the inflammatory response and scavenging components of
CC damaged cells. This has initiated a number of clinical studies for
CC evaluation of sCD163 as a disease marker in inflammatory conditions
CC e.g. infection, autoimmune disease, transplantation, atherosclerosis
CC and cancer.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA80541.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA80542.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA80543.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA80544.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB45233.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z22968; CAA80541.1; ALT_INIT; mRNA.
DR EMBL; Z22969; CAA80542.1; ALT_INIT; mRNA.
DR EMBL; Z22970; CAA80543.1; ALT_INIT; mRNA.
DR EMBL; Z22971; CAA80544.1; ALT_INIT; mRNA.
DR EMBL; Y18388; CAB45233.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y18389; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18390; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18391; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18392; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18393; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18394; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18395; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18396; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18397; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18398; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18399; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18400; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18401; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18402; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; Y18403; CAB45233.1; JOINED; Genomic_DNA.
DR EMBL; DQ058615; AAY99762.1; -; mRNA.
DR EMBL; AC131206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051281; AAH51281.1; -; mRNA.
DR CCDS; CCDS53742.1; -. [Q86VB7-3]
DR CCDS; CCDS8578.1; -. [Q86VB7-1]
DR PIR; I38004; I38004.
DR PIR; I38005; I38005.
DR PIR; I38006; I38006.
DR RefSeq; NP_004235.4; NM_004244.5. [Q86VB7-1]
DR RefSeq; NP_981961.2; NM_203416.3. [Q86VB7-3]
DR RefSeq; XP_016875720.1; XM_017020231.1.
DR AlphaFoldDB; Q86VB7; -.
DR SMR; Q86VB7; -.
DR BioGRID; 114741; 5.
DR IntAct; Q86VB7; 5.
DR MINT; Q86VB7; -.
DR STRING; 9606.ENSP00000352071; -.
DR DrugBank; DB05389; Tetrachlorodecaoxide.
DR GlyConnect; 1723; 14 N-Linked glycans (6 sites).
DR GlyGen; Q86VB7; 11 sites, 14 N-linked glycans (6 sites), 2 O-linked glycans (3 sites).
DR iPTMnet; Q86VB7; -.
DR PhosphoSitePlus; Q86VB7; -.
DR BioMuta; CD163; -.
DR DMDM; 313104083; -.
DR jPOST; Q86VB7; -.
DR MassIVE; Q86VB7; -.
DR PaxDb; Q86VB7; -.
DR PeptideAtlas; Q86VB7; -.
DR PRIDE; Q86VB7; -.
DR ProteomicsDB; 69982; -. [Q86VB7-1]
DR ProteomicsDB; 69983; -. [Q86VB7-2]
DR ProteomicsDB; 69984; -. [Q86VB7-3]
DR ProteomicsDB; 69985; -. [Q86VB7-4]
DR Antibodypedia; 3721; 1558 antibodies from 46 providers.
DR CPTC; Q86VB7; 1 antibody.
DR DNASU; 9332; -.
DR Ensembl; ENST00000359156.8; ENSP00000352071.4; ENSG00000177575.13. [Q86VB7-1]
DR Ensembl; ENST00000432237.3; ENSP00000403885.2; ENSG00000177575.13. [Q86VB7-3]
DR GeneID; 9332; -.
DR KEGG; hsa:9332; -.
DR MANE-Select; ENST00000432237.3; ENSP00000403885.2; NM_203416.4; NP_981961.2. [Q86VB7-3]
DR UCSC; uc001qsz.4; human. [Q86VB7-1]
DR CTD; 9332; -.
DR DisGeNET; 9332; -.
DR GeneCards; CD163; -.
DR HGNC; HGNC:1631; CD163.
DR HPA; ENSG00000177575; Tissue enhanced (lymphoid).
DR MIM; 605545; gene.
DR neXtProt; NX_Q86VB7; -.
DR OpenTargets; ENSG00000177575; -.
DR PharmGKB; PA26190; -.
DR VEuPathDB; HostDB:ENSG00000177575; -.
DR eggNOG; ENOG502QQ5W; Eukaryota.
DR GeneTree; ENSGT00940000155987; -.
DR HOGENOM; CLU_002555_0_1_1; -.
DR InParanoid; Q86VB7; -.
DR OMA; GCADKGN; -.
DR OrthoDB; 1095487at2759; -.
DR PhylomeDB; Q86VB7; -.
DR TreeFam; TF329295; -.
DR PathwayCommons; Q86VB7; -.
DR Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR Reactome; R-HSA-9662834; CD163 mediating an anti-inflammatory response.
DR SignaLink; Q86VB7; -.
DR SIGNOR; Q86VB7; -.
DR BioGRID-ORCS; 9332; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; CD163; human.
DR GeneWiki; CD163; -.
DR GenomeRNAi; 9332; -.
DR Pharos; Q86VB7; Tbio.
DR PRO; PR:Q86VB7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q86VB7; protein.
DR Bgee; ENSG00000177575; Expressed in right lung and 165 other tissues.
DR ExpressionAtlas; Q86VB7; baseline and differential.
DR Genevisible; Q86VB7; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:CAFA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0097110; F:scaffold protein binding; IPI:ARUK-UCL.
DR GO; GO:0005044; F:scavenger receptor activity; TAS:ProtInc.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR Gene3D; 3.10.250.10; -; 9.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR Pfam; PF00530; SRCR; 9.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 9.
DR SUPFAM; SSF56487; SSF56487; 9.
DR PROSITE; PS00420; SRCR_1; 4.
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; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..1156
FT /note="Scavenger receptor cysteine-rich type 1 protein
FT M130"
FT /id="PRO_0000238938"
FT CHAIN 42..?
FT /note="Soluble CD163"
FT /id="PRO_0000238939"
FT TOPO_DOM 42..1050
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1051..1071
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1072..1156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 51..152
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 159..259
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 266..366
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 373..473
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 478..578
FT /note="SRCR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 583..683
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..926
FT /note="SRCR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 929..1029
FT /note="SRCR 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT MOTIF 1096..1099
FT /note="Internalization signal"
FT SITE 269..270
FT /note="Cleavage; in calcium-free condition"
FT SITE 281..282
FT /note="Cleavage; in calcium-free condition"
FT SITE 333..334
FT /note="Cleavage; in calcium-free condition"
FT SITE 360..361
FT /note="Cleavage; in calcium-free condition"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1027
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 76..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 89..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 120..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 184..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 197..258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 228..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 291..355
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 304..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 335..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 398..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 411..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 442..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 503..567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 516..577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 547..557
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 608..672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 621..682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 652..662
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..925
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 895..905
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 954..1018
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 967..1028
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 998..1008
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT VAR_SEQ 579
FT /note="R -> SKTQKTSLIGSYTVKGTGLGSHSCLFLKPCLLPG (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:8370408"
FT /id="VSP_019013"
FT VAR_SEQ 1115..1156
FT /note="ENSHESADFSAAELISVSKFLPISGMEKEAILSHTEKENGNL -> GLWVLG
FT GSIAQGFRSVAAVEAQTFYFDKQLKKSKNVIGSLDAYNGQE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8370408"
FT /id="VSP_019014"
FT VAR_SEQ 1115..1156
FT /note="ENSHESADFSAAELISVSKFLPISGMEKEAILSHTEKENGNL -> GGHSEP
FT H (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8370408, ECO:0000303|Ref.3"
FT /id="VSP_019015"
FT VARIANT 342
FT /note="I -> V (in dbSNP:rs4883263)"
FT /evidence="ECO:0000269|PubMed:10403791,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8370408,
FT ECO:0000269|Ref.3"
FT /id="VAR_026574"
FT MUTAGEN 1072
FT /note="T->A: Impaired phosphorylation by PRKCA."
FT /evidence="ECO:0000269|PubMed:11298324"
FT MUTAGEN 1084
FT /note="S->A: Impaired phosphorylation by PRKCA."
FT /evidence="ECO:0000269|PubMed:11298324"
FT MUTAGEN 1096
FT /note="Y->A: Massive decrease of endocytotic activity."
FT /evidence="ECO:0000269|PubMed:16434690"
SQ SEQUENCE 1156 AA; 125451 MW; 57B49F76DA6C96EB CRC64;
MSKLRMVLLE DSGSADFRRH FVNLSPFTIT VVLLLSACFV TSSLGGTDKE LRLVDGENKC
SGRVEVKVQE EWGTVCNNGW SMEAVSVICN QLGCPTAIKA PGWANSSAGS GRIWMDHVSC
RGNESALWDC KHDGWGKHSN CTHQQDAGVT CSDGSNLEMR LTRGGNMCSG RIEIKFQGRW
GTVCDDNFNI DHASVICRQL ECGSAVSFSG SSNFGEGSGP IWFDDLICNG NESALWNCKH
QGWGKHNCDH AEDAGVICSK GADLSLRLVD GVTECSGRLE VRFQGEWGTI CDDGWDSYDA
AVACKQLGCP TAVTAIGRVN ASKGFGHIWL DSVSCQGHEP AIWQCKHHEW GKHYCNHNED
AGVTCSDGSD LELRLRGGGS RCAGTVEVEI QRLLGKVCDR GWGLKEADVV CRQLGCGSAL
KTSYQVYSKI QATNTWLFLS SCNGNETSLW DCKNWQWGGL TCDHYEEAKI TCSAHREPRL
VGGDIPCSGR VEVKHGDTWG SICDSDFSLE AASVLCRELQ CGTVVSILGG AHFGEGNGQI
WAEEFQCEGH ESHLSLCPVA PRPEGTCSHS RDVGVVCSRY TEIRLVNGKT PCEGRVELKT
LGAWGSLCNS HWDIEDAHVL CQQLKCGVAL STPGGARFGK GNGQIWRHMF HCTGTEQHMG
DCPVTALGAS LCPSEQVASV ICSGNQSQTL SSCNSSSLGP TRPTIPEESA VACIESGQLR
LVNGGGRCAG RVEIYHEGSW GTICDDSWDL SDAHVVCRQL GCGEAINATG SAHFGEGTGP
IWLDEMKCNG KESRIWQCHS HGWGQQNCRH KEDAGVICSE FMSLRLTSEA SREACAGRLE
VFYNGAWGTV GKSSMSETTV GVVCRQLGCA DKGKINPASL DKAMSIPMWV DNVQCPKGPD
TLWQCPSSPW EKRLASPSEE TWITCDNKIR LQEGPTSCSG RVEIWHGGSW GTVCDDSWDL
DDAQVVCQQL GCGPALKAFK EAEFGQGTGP IWLNEVKCKG NESSLWDCPA RRWGHSECGH
KEDAAVNCTD ISVQKTPQKA TTGRSSRQSS FIAVGILGVV LLAIFVALFF LTKKRRQRQR
LAVSSRGENL VHQIQYREMN SCLNADDLDL MNSSENSHES ADFSAAELIS VSKFLPISGM
EKEAILSHTE KENGNL
