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Database: UniProt
Entry: P59222
LinkDB: P59222
Original site: P59222 
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   10-APR-2019, entry version 130.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RP   BY 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
RT   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
RP   SCALE 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
RT   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
CC       mediates the binding and degradation of acetylated low density
CC       lipoprotein (Ac-LDL).
CC   -!- SUBUNIT: Homophilic and heterophilic interaction via its
CC       extracellular domain. Interacts with SCARF1. The heterophilic
CC       interaction with SCARF1, which is stronger than the homophilic
CC       interaction with itself, is suppressed by the presence of SCARF1
CC       ligand such as Ac-LDL.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
DR   EMBL; AF522197; AAN45862.1; -; mRNA.
DR   CCDS; CCDS28010.1; -.
DR   RefSeq; NP_722485.1; NM_153790.3.
DR   UniGene; Mm.194950; -.
DR   ProteinModelPortal; P59222; -.
DR   SMR; P59222; -.
DR   STRING; 10090.ENSMUSP00000012161; -.
DR   iPTMnet; P59222; -.
DR   PhosphoSitePlus; P59222; -.
DR   SwissPalm; P59222; -.
DR   jPOST; P59222; -.
DR   PaxDb; P59222; -.
DR   PeptideAtlas; P59222; -.
DR   PRIDE; P59222; -.
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   eggNOG; ENOG410IRWF; Eukaryota.
DR   eggNOG; ENOG410YKEF; LUCA.
DR   GeneTree; ENSGT00950000183101; -.
DR   HOGENOM; HOG000015093; -.
DR   HOVERGEN; HBG023166; -.
DR   InParanoid; P59222; -.
DR   OMA; HCNPGWI; -.
DR   OrthoDB; 110992at2759; -.
DR   PhylomeDB; P59222; -.
DR   TreeFam; TF332598; -.
DR   ChiTaRS; Scarf2; mouse.
DR   PRO; PR:P59222; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000012017; Expressed in 172 organ(s), highest expression level in vault of skull.
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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR033327; Scarf2.
DR   PANTHER; PTHR24043:SF5; PTHR24043:SF5; 1.
DR   Pfam; PF00053; Laminin_EGF; 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; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     33       {ECO:0000255}.
FT   CHAIN        34    833       Scavenger receptor class F member 2.
FT                                /FTId=PRO_0000007740.
FT   TOPO_DOM     34    433       Extracellular. {ECO:0000255}.
FT   TRANSMEM    434    454       Helical. {ECO:0000255}.
FT   TOPO_DOM    455    833       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       63    102       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      114    145       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      140    174       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      175    204       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      205    233       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      228    262       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      364    395       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    639    714       Pro-rich.
FT   MOD_RES     538    538       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     600    600       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q96GP6}.
FT   MOD_RES     615    615       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:15592455}.
FT   MOD_RES     638    638       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     640    640       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     695    695       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     712    712       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD     75     75       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    302    302       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    357    357       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    395    395       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     67     78       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     72     90       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     92    101       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    118    126       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    120    133       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    135    144       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    148    155       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    150    162       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    164    173       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    177    185       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    179    192       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    194    203       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    207    214       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    209    221       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    223    232       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    236    243       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    238    250       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    252    261       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    368    376       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    371    383       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    385    394       {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
//
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