C163A_CHLAE
ID C163A_CHLAE Reviewed; 1151 AA.
AC Q2VLG4; Q2VL91; Q2VLG0; Q2VLG1; Q2VLG2; Q2VLG3; Q2VLG5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 63.
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 Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
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.
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=3;
CC Name=1; Synonyms=CD163v3, CD163v7;
CC IsoId=Q2VLG4-1; Sequence=Displayed;
CC Name=2; Synonyms=CD163v2, CD163v6;
CC IsoId=Q2VLG4-2; Sequence=VSP_019012;
CC Name=3; Synonyms=CD163v4, CD163v5;
CC IsoId=Q2VLG4-3; Sequence=VSP_019011, VSP_019012;
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}.
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DR EMBL; DQ060838; AAY99767.1; -; mRNA.
DR EMBL; DQ060839; AAY99768.1; -; mRNA.
DR EMBL; DQ060840; AAY99769.1; -; mRNA.
DR EMBL; DQ060841; AAY99770.1; -; mRNA.
DR EMBL; DQ060842; AAY99771.1; -; mRNA.
DR EMBL; DQ060843; AAY99772.1; -; mRNA.
DR EMBL; DQ067277; AAZ50615.1; -; mRNA.
DR PDB; 6K0L; X-ray; 1.58 A; A/B=478-578.
DR PDBsum; 6K0L; -.
DR AlphaFoldDB; Q2VLG4; -.
DR SMR; Q2VLG4; -.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
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 3D-structure; Acute phase; Alternative splicing; Cell membrane;
KW Disulfide bond; Glycoprotein; Inflammatory response; Membrane;
KW Phosphoprotein; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..45
FT /evidence="ECO:0000255"
FT CHAIN 46..1151
FT /note="Scavenger receptor cysteine-rich type 1 protein
FT M130"
FT /id="PRO_0000238936"
FT CHAIN 46..?
FT /note="Soluble CD163"
FT /id="PRO_0000238937"
FT TOPO_DOM 46..1046
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1047..1067
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1068..1151
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 1091..1094
FT /note="Internalization signal"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 854
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 1042..1076
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019011"
FT VAR_SEQ 1110..1151
FT /note="ENSNESADFNAAELISVSKFLPISGMEKEAILRHTEKENGNL -> GGHSEA
FT H (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019012"
FT CONFLICT 190
FT /note="I -> V (in Ref. 1; AAY99770)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="D -> G (in Ref. 1; AAY99767)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="T -> A (in Ref. 1; AAY99770/AAY99771/AAY99772/
FT AAZ50615)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="C -> R (in Ref. 1; AAY99767)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="S -> P (in Ref. 1; AAZ50615)"
FT /evidence="ECO:0000305"
FT CONFLICT 999
FT /note="K -> E (in Ref. 1; AAY99767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1030
FT /note="D -> AQK (in Ref. 1; AAY99770/AAY99771/AAY99772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034
FT /note="R -> H (in Ref. 1; AAY99770/AAY99771/AAY99772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1034
FT /note="R -> N (in Ref. 1; AAZ50615)"
FT /evidence="ECO:0000305"
FT CONFLICT 1044..1046
FT /note="QSS -> RSF (in Ref. 1; AAY99771)"
FT /evidence="ECO:0000305"
FT CONFLICT 1046
FT /note="S -> F (in Ref. 1; AAY99772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1050
FT /note="V -> F (in Ref. 1; AAY99771/AAY99772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1059
FT /note="A -> V (in Ref. 1; AAZ50615)"
FT /evidence="ECO:0000305"
FT CONFLICT 1104
FT /note="D -> N (in Ref. 1; AAY99769)"
FT /evidence="ECO:0000305"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:6K0L"
FT STRAND 488..495
FT /evidence="ECO:0007829|PDB:6K0L"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:6K0L"
FT HELIX 504..506
FT /evidence="ECO:0007829|PDB:6K0L"
FT HELIX 509..518
FT /evidence="ECO:0007829|PDB:6K0L"
FT STRAND 523..528
FT /evidence="ECO:0007829|PDB:6K0L"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:6K0L"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:6K0L"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:6K0L"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:6K0L"
FT STRAND 574..578
FT /evidence="ECO:0007829|PDB:6K0L"
SQ SEQUENCE 1151 AA; 124873 MW; 82F06AD79C12CE2D CRC64;
MSKLRMVLLE DSGSADVRRH FVNLSPFTIA VVLLLRACFV TSSLGGTTKE LRLVDGENKC
SGRVEVKIQE EWGTVCNNGW SMEAVSVICN QLGCPTAIKA TGWANSSAGS GRIWMDHVSC
RGNESALWDC KHDGWGKHSN CTHQQDAGVT CSDGSDLEMR LTNGGNMCSG RIEIKFQGQW
GTVCDDNFNI NHASVVCKQL ECGSAVSFSG SANFGEGSGP IWFDDLICNG NESALWNCKH
QGWGKHNCDH AEDAGVICSK GADLSLRLVD GVTECSGRLE VRFQGEWGTI CDDGWDSHDA
AVACKQLGCP TAITAIGRVN ASEGFGHIWL DSVSCQGHEP AVWQCKHHEW GKHYCNHNED
AGVTCSDGSD LELRLRGGGS RCAGTVEVEI QRLLGKVCDR GWGLKEADVV CRQLGCGSAL
KTSYQVYSKI QATNMWLFLS SCNGNETSLW DCKNWQWGGL TCDHYEEAKI TCSAHREPRL
VGGDIPCSGR VEVKHGDTWG SVCDSDFSLE AASVLCRELQ CGTVVSILGG AHFGEGNGQI
WTEEFQCEGH ESHLSLCPVA PRPEGTCSHS RDVGVVCSRY TEIRLVNGKT PCEGRVELKT
LNAWGSLCNS HWDIEDAHVL CQQLKCGVAL STPGGAHFGK GNGQVWRHMF HCTGTEQHMG
DCPVTALGAS LCPSGQVASV ICSGNQSQTL SSCNSSSLGP TRPTIPEESA VACIESGQLR
LVNGGGRCAG RVEIYHEGSW GTICDDSWDL SDAHVVCRQL GCGEAINATG SAHFGEGTGP
IWLDEMKCNG KESRIWQCHS HGWGQQNCRH KEDAGVICSE FMSLRLTSEA SREACAGRLE
VFYNGAWGSV GRSNMSETTV GVVCRQLGCA DKGKINSASL DKAMSIPMWV DNVQCPKGPD
TLWQCPSSPW EKRLARPSEE TWITCDNKMR LQEGPTSCSG RVEIWHGGSW GTVCDDSWDL
NDAQVVCQQL GCGPALKAFK EAEFGQGTGP IWLNEVKCKG NESSLWDCPA RRWGHSECGH
KEDAAVNCTD ISTRKTPQKA TTGQSSLIAV GILGVVLLAI FVALFLTQKR RQRQRLTVSS
RGENLVHQIQ YREMNSCLNA DDLDLMNSSE NSNESADFNA AELISVSKFL PISGMEKEAI
LRHTEKENGN L
