C163A_CANLF
ID C163A_CANLF Reviewed; 1133 AA.
AC Q2VLG6; Q2VLG7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
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.
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=CD163v3;
CC IsoId=Q2VLG6-1; Sequence=Displayed;
CC Name=2; Synonyms=CD163v2;
CC IsoId=Q2VLG6-2; Sequence=VSP_019010;
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; DQ060836; AAY99765.1; -; mRNA.
DR EMBL; DQ060837; AAY99766.1; -; mRNA.
DR RefSeq; NP_001041485.1; NM_001048020.1. [Q2VLG6-1]
DR RefSeq; NP_001300722.1; NM_001313793.1. [Q2VLG6-2]
DR AlphaFoldDB; Q2VLG6; -.
DR SMR; Q2VLG6; -.
DR STRING; 9615.ENSCAFP00000020581; -.
DR PaxDb; Q2VLG6; -.
DR GeneID; 477704; -.
DR KEGG; cfa:477704; -.
DR CTD; 9332; -.
DR eggNOG; ENOG502QQ5W; Eukaryota.
DR InParanoid; Q2VLG6; -.
DR OrthoDB; 1095487at2759; -.
DR Proteomes; UP000002254; 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: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 2: Evidence at transcript 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..47
FT /evidence="ECO:0000255"
FT CHAIN 48..1133
FT /note="Scavenger receptor cysteine-rich type 1 protein
FT M130"
FT /id="PRO_0000238934"
FT CHAIN 48..?
FT /note="Soluble CD163"
FT /id="PRO_0000238935"
FT TOPO_DOM 48..1044
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1045..1065
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1066..1133
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 59
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 331
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 1110..1133
FT /note="YPNESDDFNDAGLISVSKSLPISG -> DHFEVH (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019010"
SQ SEQUENCE 1133 AA; 122460 MW; 54C764545740DCF4 CRC64;
MSKLRMVPHG NSGSADFRRC FALLCPSAVA VVSILSTCLM TNSLGRADKE MRLTDGEDNC
SGRVEVKVQE EWGTVCNNGW GMDEVSVICR QLGCPTAIKA AGWANSRAGS GRIWMDHVSC
RGNESALWDC KHDGWGKHNC SHQQDAGVTC SDGSSLEMRL MNGGNQCSGR IEVKFQGQWG
TVCDDNFNID HASVVCKQLE CGSAVSFSGS ANFGEGSGPI WFDDLVCSGN ESALWNCKHE
GWGKHNCDHA EDVGVICLDG ADLSLRLVDG VTECSGRLEV KFQGEWGTVC DDGWDSNDAA
VVCKQLGCPT AVTAIGRVNA SEGSGHIWLD NLSCQGDESA LWQCRHHEWG KHYCNHNEDA
GVTCSDGSDL ELRLVGGGSR CAGTVEVEIQ KLLGKVCDRG WGLKEADVVC KQLGCGSALK
TSYQRYSKVK ATNTWLFLSR CSGNETSLWD CKNWQWGGLS CDHYEEAKVT CSAHREPRLV
GGDIPCSGRV EVKHGDTWGT VCDSDFSLEA ASVLCRELQC GTVISILGGA HFGEGNGQIW
AEEFQCEGQE SHLSLCSVAS RPDGTCSHSR DVGVVCSRYT EIRLVNGQSP CEGRVELKIL
GNWGSLCNSH WDIEDAHVFC QQLKCGVALS IPGGAHFGKG SGQIWRHMFH CTGTEQHMGD
CPVTALGATL CSAGQVASVI CSGNQSQTLS PCNSTSLDPT RSTTSEESAV ACIASGQLRL
VNGGGRCAGR IEVYHEGSWG TICDDSWDLS DAHVVCRQLG CGVAINATGS AHFGEGTGPI
WLDEVNCNGK ESHIWQCRSH GWGQHNCRHK EDAGVICSEF MSLRLIDETS RDICAGRLEV
FYNGAWGSVG KSNMSATTVE VVCRQLGCAD KGSINPASSD KPMSRHMWVD NVQCPKGPDT
LWQCPSSPWK QRVASSSEET WITCANKIRL QEGTSNCSGR VELWHGGSWG TVCDDSWDLE
DAQVVCRQLG CGPALEALKE AAFGQGTGPI WLNDVKCKGN ESSLWDCPAR PWGHSDCGHK
EDAAVRCSEI AMAQRSSNPR GHSSLVALGI FGVILLAFLI ALLLWTQRRR QQQRLTVSLR
GENSVHQIQY REMNSSLKAD DLDVLTSSEY PNESDDFNDA GLISVSKSLP ISG
