MSRE_RABIT
ID MSRE_RABIT Reviewed; 454 AA.
AC Q05585;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 115.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1401078; DOI=10.1172/jci116012;
RA Bickel P.E., Freeman M.W.;
RT "Rabbit aortic smooth muscle cells express inducible macrophage scavenger
RT receptor messenger RNA that is absent from endothelial cells.";
RL J. Clin. Invest. 90:1450-1457(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8380589; DOI=10.1016/s0021-9258(18)53971-5;
RA Doi T., Wada Y., Kodama T., Higashi K.I., Kurihara Y., Miyazaki T.,
RA Nakamura H., Uesugi S., Imanishi T., Kawabe Y., Itakura H., Yazaki Y.,
RA Matsumoto A.;
RT "Charged collagen structure mediates the recognition of negatively charged
RT macromolecules by macrophage scavenger receptors.";
RL J. Biol. Chem. 268:2126-2133(1993).
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=Q05585-1; Sequence=Displayed;
CC Name=II;
CC IsoId=Q05585-2; Sequence=VSP_006233, VSP_006234;
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DR EMBL; L11693; AAA31402.1; -; mRNA.
DR EMBL; L11692; AAA31403.1; -; mRNA.
DR EMBL; D13381; BAA02649.1; -; mRNA.
DR PIR; A44407; A44407.
DR PIR; I46862; I46862.
DR PIR; I46863; I46863.
DR RefSeq; NP_001075717.1; NM_001082248.1. [Q05585-1]
DR AlphaFoldDB; Q05585; -.
DR SMR; Q05585; -.
DR STRING; 9986.ENSOCUP00000020109; -.
DR GeneID; 100009067; -.
DR KEGG; ocu:100009067; -.
DR CTD; 4481; -.
DR eggNOG; ENOG502QUW0; Eukaryota.
DR InParanoid; Q05585; -.
DR OrthoDB; 711951at2759; -.
DR Proteomes; UP000001811; Unplaced.
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:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Collagen; Disulfide bond; Endocytosis;
KW Glycoprotein; LDL; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..454
FT /note="Macrophage scavenger receptor types I and II"
FT /id="PRO_0000181629"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..73
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..454
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 273..344
FT /note="Collagen-like"
FT DOMAIN 353..453
FT /note="SRCR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..109
FT /note="Spacer"
FT /evidence="ECO:0000305"
FT REGION 267..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 199..256
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 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 378..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 391..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT DISULFID 422..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196"
FT VAR_SEQ 348..354
FT /note="TPSATVR -> RPVQLTP (in isoform II)"
FT /evidence="ECO:0000305"
FT /id="VSP_006233"
FT VAR_SEQ 355..454
FT /note="Missing (in isoform II)"
FT /evidence="ECO:0000305"
FT /id="VSP_006234"
FT CONFLICT 106
FT /note="H -> D (in Ref. 2; BAA02649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 49745 MW; 527A79692EA76429 CRC64;
MAQWDSFTDQ QEDTDSCSES VKFDARSNTA LLPPNPKNGP PLQEKLKSFK AALIALYLLV
FAVLIPIIAI MAAQLLKWEM KNCTVGSINA NSVSSSLLGR GNDSEHEVRF REVVMEHISK
MEKRIQYISD TEENLVDSEH FQNFSVTTDQ RFADVLLQLS TLVPTVQGHG NAVDEITRSL
ISLNTTLLDL HLYVETLNVK FQENTLKGQE EISKLKERVH NASAEIMSMK EEQVHLEQEI
KREVKVLNNI TNDLRLKDWE HSQTLRNITL IQGPPGPPGE KGDRGPTGES GPPGVPGPVG
PPGLKGDRGS IGFPGSRGYP GQSGKTGRTG YPGPKGQKGE KGSGSILTPS ATVRLVGGRG
PHEGRVEILH NGQWGTVCDD HWELRAGQVV CRSLGYRGVK SVHKKAYFGQ GTGPIWLNEV
PCLGMESSIE ECKIRQWGVR VCSHGEDAGV TCTL
