MSRE_BOVIN
ID MSRE_BOVIN Reviewed; 453 AA.
AC P21758; A5PJV2;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Macrophage scavenger receptor types I and II;
DE AltName: Full=Macrophage acetylated LDL receptor I and II;
DE AltName: CD_antigen=CD204;
GN Name=MSR1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lung;
RX PubMed=2300204; DOI=10.1038/343531a0;
RA Kodama T., Freeman M., Rohrer L., Zabrecky J., Matsudaira P., Krieger M.;
RT "Type I macrophage scavenger receptor contains alpha-helical and collagen-
RT like coiled coils.";
RL Nature 343:531-535(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II).
RC TISSUE=Lung;
RX PubMed=2300208; DOI=10.1038/343570a0;
RA Rohrer L., Freeman M., Kodama T., Penman M., Krieger M.;
RT "Coiled-coil fibrous domains mediate ligand binding by macrophage scavenger
RT receptor type II.";
RL Nature 343:570-572(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Membrane glycoproteins implicated in the pathologic
CC deposition of cholesterol in arterial walls during atherogenesis. Two
CC types of receptor subunits exist. These receptors mediate the
CC endocytosis of a diverse group of macromolecules, including modified
CC low density lipoproteins (LDL). {ECO:0000250|UniProtKB:P21757}.
CC -!- SUBUNIT: Homotrimer. Interacts with MYO18A.
CC {ECO:0000250|UniProtKB:P21757, ECO:0000250|UniProtKB:P30204}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=I;
CC IsoId=P21758-1; Sequence=Displayed;
CC Name=II;
CC IsoId=P21758-2; Sequence=VSP_006227, VSP_006228;
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DR EMBL; X51689; CAA35987.1; -; mRNA.
DR EMBL; X54183; CAA38108.1; -; mRNA.
DR EMBL; BC142250; AAI42251.1; -; mRNA.
DR PIR; S08276; S08276.
DR PIR; S08278; S08278.
DR RefSeq; NP_001106711.1; NM_001113240.1. [P21758-1]
DR RefSeq; NP_776538.1; NM_174113.2. [P21758-2]
DR AlphaFoldDB; P21758; -.
DR SMR; P21758; -.
DR STRING; 9913.ENSBTAP00000003751; -.
DR PaxDb; P21758; -.
DR PRIDE; P21758; -.
DR Ensembl; ENSBTAT00000003751; ENSBTAP00000003751; ENSBTAG00000002885. [P21758-1]
DR Ensembl; ENSBTAT00000003755; ENSBTAP00000003755; ENSBTAG00000002885. [P21758-2]
DR GeneID; 281311; -.
DR KEGG; bta:281311; -.
DR CTD; 4481; -.
DR VEuPathDB; HostDB:ENSBTAG00000002885; -.
DR eggNOG; ENOG502QUW0; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_041152_2_0_1; -.
DR InParanoid; P21758; -.
DR OMA; RGPHEGR; -.
DR OrthoDB; 711951at2759; -.
DR TreeFam; TF330855; -.
DR Proteomes; UP000009136; Chromosome 27.
DR Bgee; ENSBTAG00000002885; Expressed in omental fat pad and 105 other tissues.
DR ExpressionAtlas; P21758; baseline and differential.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:CAFA.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:CAFA.
DR GO; GO:0042802; F:identical protein binding; IMP:CAFA.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IEA:Ensembl.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0097242; P:amyloid-beta clearance; IEA:Ensembl.
DR GO; GO:0030301; P:cholesterol transport; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0042953; P:lipoprotein transport; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006911; P:phagocytosis, engulfment; IEA:Ensembl.
DR GO; GO:0034381; P:plasma lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; IEA:Ensembl.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0070207; P:protein homotrimerization; IMP:CAFA.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR DisProt; DP00246; -.
DR Gene3D; 3.10.250.10; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR003543; SR-AI/II.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR19331:SF440; PTHR19331:SF440; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF03523; Macscav_rec; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR01408; MACSCAVRCPTR.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Collagen; Direct protein sequencing;
KW Disulfide bond; Endocytosis; Glycoprotein; LDL; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..453
FT /note="Macrophage scavenger receptor types I and II"
FT /id="PRO_0000181626"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..76
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..453
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 272..343
FT /note="Collagen-like"
FT DOMAIN 352..452
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 77..108
FT /note="Spacer"
FT /evidence="ECO:0000305"
FT REGION 267..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 194..255
FT /evidence="ECO:0000255"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30204"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 377..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 390..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 421..431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT VAR_SEQ 348..349
FT /note="QS -> PG (in isoform II)"
FT /evidence="ECO:0000303|PubMed:2300208"
FT /id="VSP_006227"
FT VAR_SEQ 350..453
FT /note="Missing (in isoform II)"
FT /evidence="ECO:0000303|PubMed:2300208"
FT /id="VSP_006228"
SQ SEQUENCE 453 AA; 50057 MW; 77A0EFEE48B00A21 CRC64;
MAQWDDFPDQ QEDTDSCTES VKFDARSVTA LLPPHPKNGP TLQERMKSYK TALITLYLIV
FVVLVPIIGI VAAQLLKWET KNCTVGSVNA DISPSPEGKG NGSEDEMRFR EAVMERMSNM
ESRIQYLSDN EANLLDAKNF QNFSITTDQR FNDVLFQLNS LLSSIQEHEN IIGDISKSLV
GLNTTVLDLQ FSIETLNGRV QENAFKQQEE MRKLEERIYN ASAEIKSLDE KQVYLEQEIK
GEMKLLNNIT NDLRLKDWEH SQTLKNITLL QGPPGPPGEK GDRGPPGQNG IPGFPGLIGT
PGLKGDRGIS GLPGVRGFPG PMGKTGKPGL NGQKGQKGEK GSGSMQRQSN TVRLVGGSGP
HEGRVEIFHE GQWGTVCDDR WELRGGLVVC RSLGYKGVQS VHKRAYFGKG TGPIWLNEVF
CFGKESSIEE CRIRQWGVRA CSHDEDAGVT CTT
