SREC_MOUSE
ID SREC_MOUSE Reviewed; 820 AA.
AC Q5ND28; Q3V029; Q571H4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Scavenger receptor class F member 1;
DE AltName: Full=Acetyl LDL receptor;
DE AltName: Full=Scavenger receptor expressed by endothelial cells 1 protein;
DE Short=SREC-I;
DE Flags: Precursor;
GN Name=Scarf1; Synonyms=Kiaa0149, Srec;
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 [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP FUNCTION, INTERACTION WITH AVIL, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RX PubMed=15247299; DOI=10.1074/jbc.m403844200;
RA Shibata M., Ishii J., Koizumi H., Shibata N., Dohmae N., Takio K.,
RA Adachi H., Tsujimoto M., Arai H.;
RT "Type F scavenger receptor SREC-I interacts with advillin, a member of the
RT gelsolin/villin family, and induces neurite-like outgrowth.";
RL J. Biol. Chem. 279:40084-40090(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
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: Mediates the binding and degradation of acetylated low
CC density lipoprotein (Ac-LDL). Mediates heterophilic interactions,
CC suggesting a function as adhesion protein (By similarity). Plays a role
CC in the regulation of neurite-like outgrowth. {ECO:0000250,
CC ECO:0000269|PubMed:15247299}.
CC -!- SUBUNIT: Heterophilic interaction with SREC2 via its extracellular
CC domain. The heterophilic interaction is suppressed by the presence of
CC ligand such as Ac-LDL (By similarity). Interacts with AVIL; the
CC interaction occurs in embryonic dorsal root ganglions at 18 dpc and
CC induces neurite-like outgrowth. {ECO:0000250,
CC ECO:0000269|PubMed:15247299}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed weakly in brain, spinal cord and dorsal
CC root ganglions. {ECO:0000269|PubMed:15247299}.
CC -!- DEVELOPMENTAL STAGE: Expressed strongly in brain, spinal cord and
CC dorsal root ganglions at 18 dpc. {ECO:0000269|PubMed:15247299}.
CC -!- DOMAIN: The cytoplasmic domain is necessary for the regulation of
CC neurite-like outgrowth.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90140.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220215; BAD90140.1; ALT_INIT; mRNA.
DR EMBL; AK133477; BAE21676.1; -; mRNA.
DR EMBL; AL591496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS25050.1; -.
DR RefSeq; NP_001004157.2; NM_001004157.2.
DR AlphaFoldDB; Q5ND28; -.
DR SMR; Q5ND28; -.
DR BioGRID; 237612; 4.
DR STRING; 10090.ENSMUSP00000044248; -.
DR GlyGen; Q5ND28; 1 site.
DR iPTMnet; Q5ND28; -.
DR PhosphoSitePlus; Q5ND28; -.
DR SwissPalm; Q5ND28; -.
DR MaxQB; Q5ND28; -.
DR PaxDb; Q5ND28; -.
DR PRIDE; Q5ND28; -.
DR ProteomicsDB; 254559; -.
DR Antibodypedia; 22736; 151 antibodies from 35 providers.
DR DNASU; 380713; -.
DR Ensembl; ENSMUST00000042808; ENSMUSP00000044248; ENSMUSG00000038188.
DR GeneID; 380713; -.
DR KEGG; mmu:380713; -.
DR UCSC; uc007kea.1; mouse.
DR CTD; 8578; -.
DR MGI; MGI:2449455; Scarf1.
DR VEuPathDB; HostDB:ENSMUSG00000038188; -.
DR eggNOG; KOG1218; Eukaryota.
DR GeneTree; ENSGT00950000183101; -.
DR HOGENOM; CLU_017821_0_0_1; -.
DR InParanoid; Q5ND28; -.
DR OMA; CFHGNCH; -.
DR OrthoDB; 110992at2759; -.
DR PhylomeDB; Q5ND28; -.
DR TreeFam; TF332598; -.
DR BioGRID-ORCS; 380713; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Scarf1; mouse.
DR PRO; PR:Q5ND28; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5ND28; protein.
DR Bgee; ENSMUSG00000038188; Expressed in brain blood vessel and 119 other tissues.
DR ExpressionAtlas; Q5ND28; baseline and differential.
DR Genevisible; Q5ND28; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:MGI.
DR GO; GO:0005044; F:scavenger receptor activity; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016358; P:dendrite development; IDA:MGI.
DR GO; GO:0016322; P:neuron remodeling; IMP:UniProtKB.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
DR CDD; cd00055; EGF_Lam; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR033329; SCARF1.
DR InterPro; IPR042635; SREC1/2.
DR PANTHER; PTHR24043; PTHR24043; 1.
DR PANTHER; PTHR24043:SF0; PTHR24043:SF0; 1.
DR Pfam; PF00053; Laminin_EGF; 2.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 3.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 4.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..820
FT /note="Scavenger receptor class F member 1"
FT /id="PRO_0000407314"
FT TOPO_DOM 24..422
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..820
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 56..90
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 98..133
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 163..193
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 217..251
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 304..341
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 353..384
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 549..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14162"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 66..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 80..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 102..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 108..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 123..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 166..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 168..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 183..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 221..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 225..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 241..250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 820
FT /note="H -> N (in Ref. 2; BAE21676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 820 AA; 87464 MW; 769DAAEB56765943 CRC64;
MLAAMGLELV FSLLLLWTQG TQGSTLDPAG QHVCKGSSPS ELQCCPGWRQ KDQECTIPIC
EGPDACRKEE VCVKPGLCRC KPGFFGAQCS SRCPGQYWGH DCRETCPCHP RGQCEPATGD
CQCQPNYWGR LCEFPCTCGP HGQCDPKTGL CHCDPGWWSP TCRRPCQCNP ASRCDQATGT
CVCPPGWWGR RCSFSCNCHT SPCMQDSGRC VCLPGWWGPE CSRKCQCVRG QCSVTSGHCS
CPPGFHGIRC ELPCNPGHYG AQCKESCGHC ELNATCSPVT GNCESCKPGW NGTQCKQPCP
AGTFGERCTG QCPRCRLGEP CQAETGHCQH CDPGWLGHRC ENPCPLGTFG KGCSSTCPAC
AQGTCDAVTG ECVCSAGYWG TSCNSSCPAG FHGNNCSMPC QCPEGLCHPV SGTCQLGRHG
KNALIVGILV PLLLLLMGIV CCAYCCSGTR LDPKDRPERN GAAFFRMKQQ VWGALTNLGS
ALPCGSLSNY KLPWVTVSHH DPEVPFNHSF IEPPSAGWAS DDSFSSDPDS GEEDEAHAYF
VPPREEMVPM AQEESPEASL PGGSFPPPED ASTPFPIPRT SSLARAKRPS VSFAEGTKFA
PQNGRSSGDL SSPIRKPKRL SRGAQPRPEG QEAEESTGPE QVNTEEDAPT ATSSGDPATS
HGQLPPGSQM VAECAETTDG GIQESSGSVA TIYMLAGTPQ KPEGPVWSVF RRLGNYQKDQ
MDPKVKSAIP KPLRRSLGRN QASAGSAPGA VLSQAMESTA VRPEETPRGL GDGIESSGTV
QEPDAGGSSL EQDSQKQAEE KEQEEPLYEN VVPMSVPPQH
