C163A_BOVIN
ID C163A_BOVIN Reviewed; 1129 AA.
AC P85521; C6KEM1;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Scavenger receptor cysteine-rich type 1 protein M130 {ECO:0000250|UniProtKB:Q86VB7};
DE AltName: CD_antigen=CD163 {ECO:0000250|UniProtKB:Q86VB7};
DE Contains:
DE RecName: Full=Soluble CD163 {ECO:0000250|UniProtKB:Q86VB7};
DE Short=sCD163 {ECO:0000250|UniProtKB:Q86VB7};
DE Flags: Precursor;
GN Name=CD163 {ECO:0000250|UniProtKB:Q86VB7};
GN Synonyms=M130 {ECO:0000250|UniProtKB:Q86VB7};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein; TISSUE=Alveolar macrophage;
RA Long M.K., Lakritz J., Lu P., Premanandan C., Rajala-Schultz P.J.;
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [3] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RA Lakritz J., Gerspach C., Bannikov G.A., Premanandan C., Marsh A.E.,
RA Green-Church K.B.;
RT "Characterization of haptoglobin receptor (CD163) expression, protein
RT sequence and binding of hp-MMP 9 complexes to CD163 by Bovine alveolar
RT macrophages.";
RL Submitted (APR-2008) to UniProtKB.
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|UniProtKB:Q86VB7}.
CC -!- FUNCTION: After shedding, the soluble form (sCD163) may play an anti-
CC inflammatory role. {ECO:0000250|UniProtKB:Q86VB7}.
CC -!- SUBUNIT: Interacts with CSNK2B. {ECO:0000250|UniProtKB:Q86VB7}.
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 ECO:0000269|Ref.3}.
CC -!- DOMAIN: The SRCR domain 3 mediates calcium-sensitive interaction with
CC hemoglobin/haptoglobin complexes. {ECO:0000250|UniProtKB:Q86VB7}.
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|UniProtKB:Q86VB7}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q86VB7}.
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DR EMBL; GQ184570; ACS87934.1; -; mRNA.
DR EMBL; AAFC03037181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03037182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001156885.1; NM_001163413.1.
DR AlphaFoldDB; P85521; -.
DR SMR; P85521; -.
DR STRING; 9913.ENSBTAP00000026215; -.
DR PaxDb; P85521; -.
DR PRIDE; P85521; -.
DR Ensembl; ENSBTAT00000026215; ENSBTAP00000026215; ENSBTAG00000019669.
DR GeneID; 533844; -.
DR KEGG; bta:533844; -.
DR CTD; 9332; -.
DR VEuPathDB; HostDB:ENSBTAG00000019669; -.
DR eggNOG; ENOG502QQ5W; Eukaryota.
DR GeneTree; ENSGT00940000155987; -.
DR HOGENOM; CLU_258459_0_0_1; -.
DR InParanoid; P85521; -.
DR OMA; GCADKGN; -.
DR OrthoDB; 1095487at2759; -.
DR TreeFam; TF329295; -.
DR Reactome; R-BTA-2168880; Scavenging of heme from plasma.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000019669; Expressed in lung and 106 other tissues.
DR ExpressionAtlas; P85521; baseline.
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:0097110; F:scaffold protein binding; IEA:Ensembl.
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; 5.
DR PROSITE; PS50287; SRCR_2; 9.
PE 1: Evidence at protein level;
KW Acute phase; Cell membrane; Disulfide bond; Glycoprotein;
KW Inflammatory response; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..1129
FT /note="Scavenger receptor cysteine-rich type 1 protein
FT M130"
FT /evidence="ECO:0000250"
FT /id="PRO_0000376852"
FT CHAIN 41..?
FT /note="Soluble CD163"
FT /evidence="ECO:0000250"
FT /id="PRO_0000376853"
FT TOPO_DOM 41..1039
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1040..1060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1061..1129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..146
FT /note="SRCR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 153..253
FT /note="SRCR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 260..360
FT /note="SRCR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 367..467
FT /note="SRCR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 472..572
FT /note="SRCR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 577..677
FT /note="SRCR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 713..813
FT /note="SRCR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 818..920
FT /note="SRCR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DOMAIN 923..1023
FT /note="SRCR 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT MOTIF 1085..1088
FT /note="Internalization signal"
FT /evidence="ECO:0000250"
FT SITE 263..264
FT /note="Cleavage; in calcium-free condition"
FT /evidence="ECO:0000250"
FT SITE 275..276
FT /note="Cleavage; in calcium-free condition"
FT /evidence="ECO:0000250"
FT SITE 327..328
FT /note="Cleavage; in calcium-free condition"
FT /evidence="ECO:0000250"
FT SITE 354..355
FT /note="Cleavage; in calcium-free condition"
FT /evidence="ECO:0000250"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 995
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 84..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 115..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 178..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 191..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 222..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 285..349
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 298..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 329..339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 392..456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 405..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 436..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 497..561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 510..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 541..551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 602..666
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 615..676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 646..656
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 738..802
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 751..812
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 782..792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 858..919
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 889..899
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 948..1012
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 961..1022
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 992..1002
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT CONFLICT 4..6
FT /note="HDN -> LED (in Ref. 1; ACS87934)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="I -> V (in Ref. 1; ACS87934)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="A -> T (in Ref. 1; ACS87934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1129 AA; 121806 MW; 2479FF57C3DC21BB CRC64;
MVLHDNSGSA GFKRCSVHFG PFTLAVVSVL YACLITSALG GTDKELRLVA GQTKCSGRVE
VKVQEEWGTV CNTGWDLAAV SVVCKQLGCP SVIKATGWTN SSAGTGRIWM DHVSCRGNES
ALWDCKHEGW GKHNCTHQQD VGVTCSDGSD LEMRLMNGGN RCSGRIEIKF QGQWGTVCDD
NFNLDHASVV CKQLGCGSAV SFSGSANFGE GSGPIWFDDL VCHGNESALW NCRHEGWGKH
NCDHAEDAGV ICLEGADLSL RLVDGVTKCS GRLEVRFQGE WGTVCDDGWD SDDAAVACQQ
LGCPTAITAV GRVNASEGTG HIWLDSVSCQ GHESAVWQCR HHEWGKHYCN HNEDAGVTCS
DGSDLELRLK GGGSRCAGTV EVEIQKLIGK VCDRSWGLKE ADVVCKQLGC GSALRTSYQV
YSKIQATNTW LFLNNCNGNE TSIWDCKNWQ WGGLSCEHYH EAKVTCSAHR EPRLVGGDIP
CSGRVEVKHG DTWGTICDSD FSLESASVLC RELECGSVVS ILGGAHFGEG NGQIWAEEFQ
CEGNESHLSL CPVAPRLDGT CSHSKDIGVV CSRYTEVRLV GGNTPCEGRV EVKILGTWGP
LCNSHWDMED AHVLCQQLKC GVAASIPGRA PFGKGSGQPW RHMFHCTGTE QHMGDCPVTA
LGASLCPEGQ VASVICSGNR SQTLYPCNSS SSDPESSVVL EENGVPCIGS GQLRLVNGGG
RCAGRIEVYH EGSWGTICDD SWDLDDAHVV CRQLGCGVAI NATGSAHFGE GSGPIWLDEV
NCNGKEPRIS QCRSHGWGRQ NCRHKEDAGV ICSEFMSLRL ISDSSSETCA GRLEVFYNGA
WGSVGKSDMS ATTVGVVCRQ LGCTDKGSIR PAPSDKVENR YMWVDNVRCP KGPETLWQCP
SSPWKRRLAS PSEETWITCA DKIRLQEGTT NCSGRVEVWH GGSWGTVCDD SWDLNDAQVV
CRQLGCGLAL EAGKEAAFGQ GTGPIWLNEV KCKGNESSLW DCPARSWGHS DCGHKEDASV
KCSEIAESKG SVKAAGHSST VALGILGVIL LAFLIATLLW IQRRRQRQRL AVSSRGENSV
HEIQYREMNS CLKADDLDLY NSSGLWVLRG SIALGFRLVT AAEAERHST
