SREC2_MOUSE
ID SREC2_MOUSE Reviewed; 833 AA.
AC P59222;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Scavenger receptor class F member 2;
DE AltName: Full=Scavenger receptor expressed by endothelial cells 2 protein;
DE Short=SREC-II;
DE Flags: Precursor;
GN Name=Scarf2; Synonyms=Srec2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=C57BL/6J;
RX PubMed=12154095; DOI=10.1074/jbc.m206140200;
RA Ishii J., Adachi H., Aoki J., Koizumi H., Tomita S., Suzuki T.,
RA Tsujimoto M., Inoue K., Arai H.;
RT "SREC-II, a new member of the scavenger receptor type F family, trans-
RT interacts with SREC-I through its extracellular domain.";
RL J. Biol. Chem. 277:39696-39702(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-615, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-638; SER-640;
RP SER-695 AND THR-712, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probable adhesion protein, which mediates homophilic and
CC heterophilic interactions. In contrast to SCARF1, it poorly mediates
CC the binding and degradation of acetylated low density lipoprotein (Ac-
CC LDL).
CC -!- SUBUNIT: Homophilic and heterophilic interaction via its extracellular
CC domain. Interacts with SCARF1. The heterophilic interaction with
CC SCARF1, which is stronger than the homophilic interaction with itself,
CC is suppressed by the presence of SCARF1 ligand such as Ac-LDL.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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DR EMBL; AF522197; AAN45862.1; -; mRNA.
DR CCDS; CCDS28010.1; -.
DR RefSeq; NP_722485.1; NM_153790.3.
DR AlphaFoldDB; P59222; -.
DR SMR; P59222; -.
DR BioGRID; 230229; 3.
DR STRING; 10090.ENSMUSP00000012161; -.
DR GlyGen; P59222; 4 sites.
DR iPTMnet; P59222; -.
DR PhosphoSitePlus; P59222; -.
DR SwissPalm; P59222; -.
DR CPTAC; non-CPTAC-3498; -.
DR jPOST; P59222; -.
DR PaxDb; P59222; -.
DR PeptideAtlas; P59222; -.
DR PRIDE; P59222; -.
DR ProteomicsDB; 257397; -.
DR Antibodypedia; 51072; 107 antibodies from 23 providers.
DR DNASU; 224024; -.
DR Ensembl; ENSMUST00000012161; ENSMUSP00000012161; ENSMUSG00000012017.
DR GeneID; 224024; -.
DR KEGG; mmu:224024; -.
DR UCSC; uc007ymd.1; mouse.
DR CTD; 91179; -.
DR MGI; MGI:1858430; Scarf2.
DR VEuPathDB; HostDB:ENSMUSG00000012017; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00950000183101; -.
DR HOGENOM; CLU_017821_1_0_1; -.
DR InParanoid; P59222; -.
DR OMA; KCTCHPN; -.
DR OrthoDB; 110992at2759; -.
DR PhylomeDB; P59222; -.
DR TreeFam; TF332598; -.
DR BioGRID-ORCS; 224024; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Scarf2; mouse.
DR PRO; PR:P59222; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P59222; protein.
DR Bgee; ENSMUSG00000012017; Expressed in vault of skull and 158 other tissues.
DR ExpressionAtlas; P59222; baseline and differential.
DR Genevisible; P59222; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005044; F:scavenger receptor activity; IDA:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MGI.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR033327; Scarf2.
DR InterPro; IPR042635; SREC1/2.
DR PANTHER; PTHR24043; PTHR24043; 1.
DR PANTHER; PTHR24043:SF5; PTHR24043:SF5; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 6.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..833
FT /note="Scavenger receptor class F member 2"
FT /id="PRO_0000007740"
FT TOPO_DOM 34..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..833
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 63..102
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 114..145
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 140..174
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 175..204
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 205..233
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 228..262
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 364..395
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 578..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GP6"
FT MOD_RES 615
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 712
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 72..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 92..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 118..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 120..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 135..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 148..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 150..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 164..173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 177..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 179..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 194..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 207..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 209..221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 223..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 236..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 238..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 252..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 368..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 371..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 385..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 833 AA; 87871 MW; 51EADEEAACAFF005 CRC64;
MEGAGSRGAG PARRQGARGL GLLLLLWLLP GLAAPQDLNP RGRNVCRTPG SQVLTCCAGW
RQLGDECGIA VCEGNSTCSE NEVCVRPGEC RCRHGYFGAN CDTKCPRQFW GPDCKERCSC
HPHGQCEDVT GQCTCHARRW GARCEHACQC QHGTCHPRSG ACRCEPGWWG AQCASACYCS
ATSRCDPQTG ACLCHVGWWG RSCNNQCACN SSPCEQQSGR CQCRERMFGA RCDRYCQCSH
GRCHPVDGTC ACDPGYRGKY CREPCPAGFY GPGCRRRCGQ CKGQQPCTVV EGRCLTCEPG
WNGTKCDQPC ATGFYGEGCG HRCPPCRDGH ACNHVTGKCT HCNAGWIGDR CETKCSNGTY
GEDCAFVCSD CGSGHCDFQS GRCLCSPGVH GPHCNVTCPA GLHGVDCAQA CSCHEESCDP
VTGACHLETN QRKGVMGAGA LLTLLLGLLL SLLGCCCACR GKDSARRELT LGRKKAPQRF
CGSFSRISMK LPRIPLRRQK LPKVVVAHHD LDNTLNCSFL DPPSGLEQPS PSWSSRASFS
SFDTTDEGPV YCVPHEEATA DSRDLEATAA LTEVAAVSLE PTGTSTPGEE AAVLPASSDS
ERSASSVEGP SGALYARVAR REARPARTRN EAGGLSLSPS PERRKPPPPD PATKPKVSWI
HGKHSAAAAA PSPPPAGRKA APSPSGRKRT PSNSSVQPPG LTEEAPGPAS PTPPRARARG
RGLGLSEPTD AGGPPRSAPE AASMLAAELR DKTRSLGRAE KPPPPQKAKR SVLPAATVRT
ASASEASGSE KAAASAPAPE TPRKKTPIQK PPRKKSREAA GEPSRAGTAP GAS
