C163A_PIG
ID C163A_PIG Reviewed; 1115 AA.
AC Q2VL90; Q2VL89; Q8HY22;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 80.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-1115 (ISOFORM 1).
RC TISSUE=Lung;
RA Gomez N., Ortuno E., Alonso F., Dominguez J., Ezquerra A.;
RT "Cloning and characterization of the cDNA coding for the porcine homologous
RT to human CD163 antigen.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=14648288; DOI=10.1007/s00705-003-0188-4;
RA Sanchez-Torres C., Gomez-Puertas P., Gomez-del-Moral M., Alonso F.,
RA Escribano J.M., Ezquerra A., Dominguez J.;
RT "Expression of porcine CD163 on monocytes/macrophages correlates with
RT permissiveness to African swine fever infection.";
RL Arch. Virol. 148:2307-2323(2003).
RN [4]
RP INDUCTION.
RX PubMed=15481141; DOI=10.1016/j.imbio.2004.02.002;
RA Chamorro S., Revilla C., Gomez N., Alvarez B., Alonso F., Ezquerra A.,
RA Dominguez J.;
RT "In vitro differentiation of porcine blood CD163- and CD163+ monocytes into
RT functional dendritic cells.";
RL Immunobiology 209:57-65(2004).
RN [5]
RP INTERACTION WITH PORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME VIRUS
RP GLYCOPROTEIN 4 AND GLYCOPROTEIN 2A.
RX PubMed=19939927; DOI=10.1128/jvi.01774-09;
RA Das P.B., Dinh P.X., Ansari I.H., de Lima M., Osorio F.A., Pattnaik A.K.;
RT "The minor envelope glycoproteins GP2a and GP4 of porcine reproductive and
RT respiratory syndrome virus interact with the receptor CD163.";
RL J. Virol. 84:1731-1740(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 May play a role in the process of infection of porcine
CC monocytes/macrophages by African swine fever virus (ASFV). In case of
CC porcine reproductive and respiratory syndrome virus (PRRSV), serves
CC mediates virion attachment and plays a role in viral entry.
CC {ECO:0000250, ECO:0000269|PubMed:14648288}.
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;
CC IsoId=Q2VL90-1; Sequence=Displayed;
CC Name=2; Synonyms=CD163v3;
CC IsoId=Q2VL90-2; Sequence=VSP_019017;
CC -!- TISSUE SPECIFICITY: Expressed in monocytes and macrophages. Detected
CC only in one population of monocytes (CD163+) which is in advanced
CC maturation stage. {ECO:0000269|PubMed:14648288}.
CC -!- INDUCTION: Suppressed when monocytes are differentiated towards
CC dendritic cells by CSF1 and IL4. {ECO:0000269|PubMed:15481141}.
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}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC {ECO:0000305}.
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DR EMBL; DQ067278; AAZ50616.1; -; mRNA.
DR EMBL; DQ067279; AAZ50617.1; -; mRNA.
DR EMBL; AJ311716; CAC84397.1; -; mRNA.
DR RefSeq; NP_999141.1; NM_213976.1.
DR PDB; 5HRJ; X-ray; 1.80 A; A=477-577.
DR PDB; 5JFB; X-ray; 2.00 A; A=477-577.
DR PDBsum; 5HRJ; -.
DR PDBsum; 5JFB; -.
DR AlphaFoldDB; Q2VL90; -.
DR SMR; Q2VL90; -.
DR PeptideAtlas; Q2VL90; -.
DR PRIDE; Q2VL90; -.
DR GeneID; 397031; -.
DR KEGG; ssc:397031; -.
DR CTD; 9332; -.
DR InParanoid; Q2VL90; -.
DR OrthoDB; 1095487at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
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; 3.
DR PROSITE; PS50287; SRCR_2; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Acute phase; Alternative splicing; Cell membrane;
KW Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW Host-virus interaction; Inflammatory response; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..46
FT /evidence="ECO:0000255"
FT CHAIN 47..1115
FT /note="Scavenger receptor cysteine-rich type 1 protein
FT M130"
FT /id="PRO_0000238942"
FT CHAIN 47..?
FT /note="Soluble CD163"
FT /id="PRO_0000238943"
FT TOPO_DOM 47..1044
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 51..151
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 158..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 718..818
FT /note="SRCR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 823..925
FT /note="SRCR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 928..1028
FT /note="SRCR 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT MOTIF 1090..1093
FT /note="Internalization signal"
FT CARBOHYD 105
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 936
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 76..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 89..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 120..130
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 743..807
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 756..817
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 787..797
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 863..924
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 894..904
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 953..1017
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 966..1027
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 997..1007
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT VAR_SEQ 15..260
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019017"
FT CONFLICT 9..11
FT /note="HEN -> LED (in Ref. 2; CAC84397)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="G -> R (in Ref. 2; CAC84397)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="G -> E (in Ref. 2; CAC84397)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="V -> L (in Ref. 2; CAC84397)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="D -> N (in Ref. 1; AAZ50617 and 2; CAC84397)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="N -> S (in Ref. 2; CAC84397)"
FT /evidence="ECO:0000305"
FT CONFLICT 735..737
FT /note="HEG -> PGA (in Ref. 2; CAC84397)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="R -> K (in Ref. 1; AAZ50617)"
FT /evidence="ECO:0000305"
FT CONFLICT 981
FT /note="A -> P (in Ref. 2; CAC84397)"
FT /evidence="ECO:0000305"
FT CONFLICT 1002
FT /note="T -> P (in Ref. 2; CAC84397)"
FT /evidence="ECO:0000305"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:5HRJ"
FT STRAND 487..494
FT /evidence="ECO:0007829|PDB:5HRJ"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:5HRJ"
FT HELIX 508..517
FT /evidence="ECO:0007829|PDB:5HRJ"
FT STRAND 522..527
FT /evidence="ECO:0007829|PDB:5HRJ"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:5HRJ"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:5HRJ"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:5HRJ"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:5HRJ"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:5HRJ"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:5HRJ"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:5HRJ"
SQ SEQUENCE 1115 AA; 120456 MW; 68877E34BA5955C1 CRC64;
MDKLRMVLHE NSGSADFRRC SAHLSSFTFA VVAVLSACLV TSSLGGKDKE LRLTGGENKC
SGRVEVKVQE EWGTVCNNGW DMDVVSVVCR QLGCPTAIKA TGWANFSAGS GRIWMDHVSC
RGNESALWDC KHDGWGKHNC THQQDAGVTC SDGSDLEMGL VNGGNRCLGR IEVKFQGRWG
TVCDDNFNIN HASVVCKQLE CGSAVSFSGS ANFGEGSGPI WFDDLVCNGN ESALWNCKHE
GWGKHNCDHA EDAGVICLNG ADLKLRVVDG VTECSGRLEV KFQGEWGTIC DDGWDSDDAA
VACKQLGCPT AVTAIGRVNA SEGTGHIWLD SVSCHGHESA LWQCRHHEWG KHYCNHDEDA
GVTCSDGSDL ELRLKGGGSH CAGTVEVEIQ KLVGKVCDRS WGLKEADVVC RQLGCGSALK
TSYQVYSKTK ATNTWLFVSS CNGNETSLWD CKNWQWGGLS CDHYDEAKIT CSAHRKPRLV
GGDIPCSGRV EVQHGDTWGT VCDSDFSLEA ASVLCRELQC GTVVSLLGGA HFGEGSGQIW
AEEFQCEGHE SHLSLCPVAP RPDGTCSHSR DVGVVCSRYT QIRLVNGKTP CEGRVELNIL
GSWGSLCNSH WDMEDAHVLC QQLKCGVALS IPGGAPFGKG SEQVWRHMFH CTGTEKHMGD
CSVTALGASL CSSGQVASVI CSGNQSQTLS PCNSSSSDPS SSIISEENGV ACIGSGQLRL
VDGGGRCAGR VEVYHEGSWG TICDDSWDLN DAHVVCKQLS CGWAINATGS AHFGEGTGPI
WLDEINCNGK ESHIWQCHSH GWGRHNCRHK EDAGVICSEF MSLRLISENS RETCAGRLEV
FYNGAWGSVG RNSMSPATVG VVCRQLGCAD RGDISPASSD KTVSRHMWVD NVQCPKGPDT
LWQCPSSPWK KRLASPSEET WITCANKIRL QEGNTNCSGR VEIWYGGSWG TVCDDSWDLE
DAQVVCRQLG CGSALEAGKE AAFGQGTGPI WLNEVKCKGN ETSLWDCPAR SWGHSDCGHK
EDAAVTCSEI AKSRESLHAT GRSSFVALAI FGVILLACLI AFLIWTQKRR QRQRLSVFSG
GENSVHQIQY REMNSCLKAD ETDMLNPSGD HSEVQ
