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Scavenger receptor cysteine-rich type 1 protein M130 (Hemoglobin scavenger receptor) (CD antigen CD163) [Cleaved into: Soluble CD163 (sCD163)]

 C163A_HUMAN             Reviewed;        1156 AA.
Q86VB7; C9JIG2; Q07898; Q07899; Q07900; Q07901; Q2VLH7;
30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 2.
27-SEP-2017, entry version 125.
RecName: Full=Scavenger receptor cysteine-rich type 1 protein M130;
AltName: Full=Hemoglobin scavenger receptor;
AltName: CD_antigen=CD163;
Contains:
RecName: Full=Soluble CD163;
Short=sCD163;
Flags: Precursor;
Name=CD163; Synonyms=M130;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND VARIANT
VAL-342.
PubMed=8370408; DOI=10.1002/eji.1830230940;
Law S.K.A., Micklem K.J., Shaw J.M., Zhang X.-P., Dong Y.,
Willis A.C., Mason D.Y.;
"A new macrophage differentiation antigen which is a member of the
scavenger receptor superfamily.";
Eur. J. Immunol. 23:2320-2325(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-342.
PubMed=10403791; DOI=10.1006/bbrc.1999.0866;
Ritter M., Buechler C., Langmann T., Schmitz G.;
"Genomic organization and chromosomal localization of the human CD163
(M130) gene: a member of the scavenger receptor cysteine-rich
superfamily.";
Biochem. Biophys. Res. Commun. 260:466-474(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT VAL-342.
Welch S.-K.W., Calvert J.G., Slade D.E., Shields S.L.;
"Scavenger receptor cd163 is a cell permissive factor for infection
with porcine reproductive and respiratory syndrome viruses.";
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-342.
TISSUE=Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
CLEAVAGE.
PubMed=10066432; DOI=10.1006/bbrc.1999.0294;
Droste A., Sorg C., Hogger P.;
"Shedding of CD163, a novel regulatory mechanism for a member of the
scavenger receptor cysteine-rich family.";
Biochem. Biophys. Res. Commun. 256:110-113(1999).
[7]
FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=10577520;
Van den Heuvel M.M., Tensen C.P., van As J.H., Van den Berg T.K.,
Fluitsma D.M., Dijkstra C.D., Dopp E.A., Droste A., Van Gaalen F.A.,
Sorg C., Hoegger P., Beelen R.H.J.;
"Regulation of CD 163 on human macrophages: cross-linking of CD163
induces signaling and activation.";
J. Leukoc. Biol. 66:858-866(1999).
[8]
INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=10648003;
Buechler C., Ritter M., Orso E., Langmann T., Klucken J., Schmitz G.;
"Regulation of scavenger receptor CD163 expression in human monocytes
and macrophages by pro- and antiinflammatory stimuli.";
J. Leukoc. Biol. 67:97-103(2000).
[9]
FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF THR-1072 AND SER-1084, AND
INTERACTION WITH CSNK2B.
PubMed=11298324;
DOI=10.1002/1521-4141(200104)31:4<999::AID-IMMU999>3.0.CO;2-R;
Ritter M., Buechler C., Kapinsky M., Schmitz G.;
"Interaction of CD163 with the regulatory subunit of casein kinase II
(CKII) and dependence of CD163 signaling on CKII and protein kinase
C.";
Eur. J. Immunol. 31:999-1009(2001).
[10]
FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11196644; DOI=10.1038/35051594;
Kristiansen M., Graversen J.H., Jacobsen C., Sonne O., Hoffman H.-J.,
Law S.K.A., Moestrup S.K.;
"Identification of the haemoglobin scavenger receptor.";
Nature 409:198-201(2001).
[11]
CLEAVAGE, AND SUBCELLULAR LOCATION.
PubMed=12296867; DOI=10.1046/j.1365-2249.2002.01963.x;
Matsushita N., Kashiwagi M., Wait R., Nagayoshi R., Nakamura M.,
Matsuda T., Hogger P., Guyre P.M., Nagase H., Matsuyama T.;
"Elevated levels of soluble CD163 in sera and fluids from rheumatoid
arthritis patients and inhibition of the shedding of CD163 by TIMP-
3.";
Clin. Exp. Immunol. 130:156-161(2002).
[12]
FUNCTION.
PubMed=12208511; DOI=10.1016/S0014-5793(02)03142-3;
Frings W., Dreier J., Sorg C.;
"Only the soluble form of the scavenger receptor CD163 acts inhibitory
on phorbol ester-activated T-lymphocytes, whereas membrane-bound
protein has no effect.";
FEBS Lett. 526:93-96(2002).
[13]
MISCELLANEOUS.
PubMed=12377940;
Hintz K.A., Rassias A.J., Wardwell K., Moss M.L., Morganelli P.M.,
Pioli P.A., Givan A.L., Wallace P.K., Yeager M.P., Guyre P.M.;
"Endotoxin induces rapid metalloproteinase-mediated shedding followed
by up-regulation of the monocyte hemoglobin scavenger receptor
CD163.";
J. Leukoc. Biol. 72:711-717(2002).
[14]
RELEVANCE AS DISEASE MARKER IN INFLAMMATORY CONDITIONS.
PubMed=15478309; DOI=10.1080/07853890410033171;
Moestrup S.K., Moller H.J.;
"CD163: a regulated hemoglobin scavenger receptor with a role in the
anti-inflammatory response.";
Ann. Med. 36:347-354(2004).
[15]
DOMAIN, AND CLEAVAGE SITES.
PubMed=15448162; DOI=10.1074/jbc.M409629200;
Madsen M., Moller H.J., Nielsen M.J., Jacobsen C., Graversen J.H.,
van den Berg T., Moestrup S.K.;
"Molecular characterization of the haptoglobin.hemoglobin receptor
CD163. Ligand binding properties of the scavenger receptor cysteine-
rich domain region.";
J. Biol. Chem. 279:51561-51567(2004).
[16]
CLEAVAGE.
PubMed=15075364; DOI=10.1189/jlb.1003523;
Sulahian T.H., Pioli P.A., Wardwell K., Guyre P.M.;
"Cross-linking of FcgammaR triggers shedding of the hemoglobin-
haptoglobin scavenger receptor CD163.";
J. Leukoc. Biol. 76:271-277(2004).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[18]
FUNCTION, MUTAGENESIS OF TYR-1096, AND TISSUE SPECIFICITY.
PubMed=16434690; DOI=10.1189/jlb.1005602;
Nielsen M.J., Madsen M., Moller H.J., Moestrup S.K.;
"The macrophage scavenger receptor CD163: endocytic properties of
cytoplasmic tail variants.";
J. Leukoc. Biol. 79:837-845(2006).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105; ASN-140; ASN-767 AND
ASN-1027.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[20]
GLYCOSYLATION AT ASN-105.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Acute phase-regulated receptor involved in clearance and
endocytosis of hemoglobin/haptoglobin complexes by macrophages and
may thereby protect tissues from free hemoglobin-mediated
oxidative damage. May play a role in the uptake and recycling of
iron, via endocytosis of hemoglobin/haptoglobin and subsequent
breakdown of heme. Binds hemoglobin/haptoglobin complexes in a
calcium-dependent and pH-dependent manner. Exhibits a higher
affinity for complexes of hemoglobin and multimeric haptoglobin of
HP*1F phenotype than for complexes of hemoglobin and dimeric
haptoglobin of HP*1S phenotype. Induces a cascade of intracellular
signals that involves tyrosine kinase-dependent calcium
mobilization, inositol triphosphate production and secretion of
IL6 and CSF1. Isoform 3 exhibits the higher capacity for ligand
endocytosis and the more pronounced surface expression when
expressed in cells.
-!- FUNCTION: After shedding, the soluble form (sCD163) may play an
anti-inflammatory role, and may be a valuable diagnostic parameter
for monitoring macrophage activation in inflammatory conditions.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.0 nM for hemoglobin/haptoglobin of HP*1S phenotype
{ECO:0000269|PubMed:11196644};
KM=0.2 nM for hemoglobin/haptoglobin of HP*1F phenotype
{ECO:0000269|PubMed:11196644};
-!- SUBUNIT: Interacts with CSNK2B. {ECO:0000269|PubMed:11298324}.
-!- SUBCELLULAR LOCATION: Soluble CD163: Secreted
{ECO:0000269|PubMed:12296867}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10577520,
ECO:0000269|PubMed:10648003}; Single-pass type I membrane protein
{ECO:0000269|PubMed:10577520, ECO:0000269|PubMed:10648003}.
Note=Isoform 1 and isoform 2 show a lower surface expression when
expressed in cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Long tail variant 1;
IsoId=Q86VB7-1; Sequence=Displayed;
Name=2; Synonyms=Long tail variant 2;
IsoId=Q86VB7-2; Sequence=VSP_019014;
Name=3; Synonyms=Short tail variant;
IsoId=Q86VB7-3; Sequence=VSP_019015;
Name=4;
IsoId=Q86VB7-4; Sequence=VSP_019013, VSP_019015;
-!- TISSUE SPECIFICITY: Expressed in monocytes and mature macrophages
such as Kupffer cells in the liver, red pulp macrophages in the
spleen, cortical macrophages in the thymus, resident bone marrow
macrophages and meningeal macrophages of the central nervous
system. Expressed also in blood. Isoform 1 is the lowest abundant
in the blood. Isoform 2 is the lowest abundant in the liver and
the spleen. Isoform 3 is the predominant isoform detected in the
blood. {ECO:0000269|PubMed:10577520, ECO:0000269|PubMed:11196644,
ECO:0000269|PubMed:16434690}.
-!- INDUCTION: Induced by anti-inflammatory mediators such as
glucocorticoids, interleukin-6/IL6 and interleukin-10/IL10;
suppressed by proinflammatory mediators like bacterial
lipopolysaccharides (LPS), IFNG/IFN-gamma and TNF.
{ECO:0000269|PubMed:10577520, ECO:0000269|PubMed:10648003}.
-!- DOMAIN: The SRCR domain 3 mediates calcium-sensitive interaction
with hemoglobin/haptoglobin complexes.
{ECO:0000269|PubMed:15448162}.
-!- PTM: A soluble form (sCD163) is produced by proteolytic shedding
which can be induced by lipopolysaccharide, phorbol ester and Fc
region of immunoglobulin gamma. This cleavage is dependent on
protein kinase C and tyrosine kinases and can be blocked by
protease inhibitors. The shedding is inhibited by the tissue
inhibitor of metalloproteinase TIMP3, and thus probably induced by
membrane-bound metalloproteinases ADAMs.
{ECO:0000269|PubMed:10066432, ECO:0000269|PubMed:12296867,
ECO:0000269|PubMed:15075364, ECO:0000269|PubMed:15448162}.
-!- PTM: Phosphorylated. {ECO:0000305|PubMed:11298324}.
-!- MISCELLANEOUS: Intravenous lipopolysaccharide (LPS) produces a
rapid rise of sCD163 in plasma of patient as it induces
metalloproteinase-mediated shedding from monocytes surface. Long-
term LPS infusion finally increases expression of the membrane-
bound form on circulating monocytes.
-!- MISCELLANEOUS: The soluble form (sCD163) in plasma is a novel
parameter in diseases affecting macrophage function and
monocyte/macrophage load in the body. The concentration of sCD163
is probably reflecting the number of macrophages of the
'alternative macrophage activation' phenotype with a high CD163
expression playing a major role in dampening the inflammatory
response and scavenging components of damaged cells. This has
initiated a number of clinical studies for evaluation of sCD163 as
a disease marker in inflammatory conditions e.g. infection,
autoimmune disease, transplantation, atherosclerosis and cancer.
-!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA80541.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA80542.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA80543.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA80544.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB45233.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; Z22968; CAA80541.1; ALT_INIT; mRNA.
EMBL; Z22969; CAA80542.1; ALT_INIT; mRNA.
EMBL; Z22970; CAA80543.1; ALT_INIT; mRNA.
EMBL; Z22971; CAA80544.1; ALT_INIT; mRNA.
EMBL; Y18388; CAB45233.1; ALT_INIT; Genomic_DNA.
EMBL; Y18389; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18390; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18391; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18392; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18393; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18394; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18395; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18396; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18397; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18398; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18399; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18400; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18401; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18402; CAB45233.1; JOINED; Genomic_DNA.
EMBL; Y18403; CAB45233.1; JOINED; Genomic_DNA.
EMBL; DQ058615; AAY99762.1; -; mRNA.
EMBL; AC131206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC051281; AAH51281.1; -; mRNA.
CCDS; CCDS53742.1; -. [Q86VB7-3]
CCDS; CCDS8578.1; -. [Q86VB7-1]
PIR; I38004; I38004.
PIR; I38005; I38005.
PIR; I38006; I38006.
RefSeq; NP_004235.4; NM_004244.5. [Q86VB7-1]
RefSeq; NP_981961.2; NM_203416.3. [Q86VB7-3]
RefSeq; XP_016875720.1; XM_017020231.1. [Q86VB7-2]
UniGene; Hs.504641; -.
ProteinModelPortal; Q86VB7; -.
SMR; Q86VB7; -.
BioGrid; 114741; 2.
IntAct; Q86VB7; 1.
STRING; 9606.ENSP00000352071; -.
DrugBank; DB05389; WF10.
iPTMnet; Q86VB7; -.
PhosphoSitePlus; Q86VB7; -.
BioMuta; CD163; -.
DMDM; 313104083; -.
PaxDb; Q86VB7; -.
PeptideAtlas; Q86VB7; -.
PRIDE; Q86VB7; -.
Ensembl; ENST00000359156; ENSP00000352071; ENSG00000177575. [Q86VB7-1]
Ensembl; ENST00000432237; ENSP00000403885; ENSG00000177575. [Q86VB7-3]
GeneID; 9332; -.
KEGG; hsa:9332; -.
UCSC; uc001qsz.4; human. [Q86VB7-1]
CTD; 9332; -.
DisGeNET; 9332; -.
EuPathDB; HostDB:ENSG00000177575.12; -.
GeneCards; CD163; -.
HGNC; HGNC:1631; CD163.
HPA; CAB002432; -.
HPA; HPA046404; -.
HPA; HPA051974; -.
MIM; 605545; gene.
neXtProt; NX_Q86VB7; -.
OpenTargets; ENSG00000177575; -.
PharmGKB; PA26190; -.
eggNOG; ENOG410IHBC; Eukaryota.
eggNOG; ENOG410XQVR; LUCA.
GeneTree; ENSGT00870000136382; -.
HOVERGEN; HBG080943; -.
InParanoid; Q86VB7; -.
KO; K06545; -.
OMA; NWQWGGL; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; Q86VB7; -.
TreeFam; TF329295; -.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
SIGNOR; Q86VB7; -.
ChiTaRS; CD163; human.
GeneWiki; CD163; -.
GenomeRNAi; 9332; -.
PRO; PR:Q86VB7; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000177575; -.
CleanEx; HS_CD163; -.
ExpressionAtlas; Q86VB7; baseline and differential.
Genevisible; Q86VB7; HS.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IDA:CAFA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005044; F:scavenger receptor activity; TAS:ProtInc.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
InterPro; IPR001190; SRCR.
InterPro; IPR017448; SRCR-like_dom.
Pfam; PF00530; SRCR; 9.
PRINTS; PR00258; SPERACTRCPTR.
SMART; SM00202; SR; 9.
SUPFAM; SSF56487; SSF56487; 9.
PROSITE; PS00420; SRCR_1; 4.
PROSITE; PS50287; SRCR_2; 9.
1: Evidence at protein level;
Acute phase; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Inflammatory response; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 41 {ECO:0000255}.
CHAIN 42 1156 Scavenger receptor cysteine-rich type 1
protein M130.
/FTId=PRO_0000238938.
CHAIN 42 ? Soluble CD163.
/FTId=PRO_0000238939.
TOPO_DOM 42 1050 Extracellular. {ECO:0000255}.
TRANSMEM 1051 1071 Helical. {ECO:0000255}.
TOPO_DOM 1072 1156 Cytoplasmic. {ECO:0000255}.
DOMAIN 51 152 SRCR 1. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 159 259 SRCR 2. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 266 366 SRCR 3. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 373 473 SRCR 4. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 478 578 SRCR 5. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 583 683 SRCR 6. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 719 819 SRCR 7. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 824 926 SRCR 8. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 929 1029 SRCR 9. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
MOTIF 1096 1099 Internalization signal.
SITE 269 270 Cleavage; in calcium-free condition.
SITE 281 282 Cleavage; in calcium-free condition.
SITE 333 334 Cleavage; in calcium-free condition.
SITE 360 361 Cleavage; in calcium-free condition.
CARBOHYD 105 105 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 767 767 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 1027 1027 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 76 141 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 89 151 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 120 130 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 184 248 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 197 258 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 228 238 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 291 355 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 304 365 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 335 345 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 398 462 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 411 472 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 442 452 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 503 567 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 516 577 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 547 557 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 608 672 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 621 682 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 652 662 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 744 808 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 757 818 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 788 798 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 864 925 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 895 905 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 954 1018 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 967 1028 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 998 1008 {ECO:0000255|PROSITE-ProRule:PRU00196}.
VAR_SEQ 579 579 R -> SKTQKTSLIGSYTVKGTGLGSHSCLFLKPCLLPG
(in isoform 4).
{ECO:0000303|PubMed:8370408}.
/FTId=VSP_019013.
VAR_SEQ 1115 1156 ENSHESADFSAAELISVSKFLPISGMEKEAILSHTEKENGN
L -> GLWVLGGSIAQGFRSVAAVEAQTFYFDKQLKKSKNV
IGSLDAYNGQE (in isoform 2).
{ECO:0000303|PubMed:8370408}.
/FTId=VSP_019014.
VAR_SEQ 1115 1156 ENSHESADFSAAELISVSKFLPISGMEKEAILSHTEKENGN
L -> GGHSEPH (in isoform 3 and isoform
4). {ECO:0000303|PubMed:8370408,
ECO:0000303|Ref.3}.
/FTId=VSP_019015.
VARIANT 342 342 I -> V (in dbSNP:rs4883263).
{ECO:0000269|PubMed:10403791,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8370408,
ECO:0000269|Ref.3}.
/FTId=VAR_026574.
MUTAGEN 1072 1072 T->A: Impaired phosphorylation by PRKCA.
{ECO:0000269|PubMed:11298324}.
MUTAGEN 1084 1084 S->A: Impaired phosphorylation by PRKCA.
{ECO:0000269|PubMed:11298324}.
MUTAGEN 1096 1096 Y->A: Massive decrease of endocytotic
activity. {ECO:0000269|PubMed:16434690}.
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


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