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Protein

Scavenger receptor class F member 2

Gene

Scarf2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probable adhesion protein, which mediates homophilic and heterophilic interactions. In contrast to SCARF1, it poorly mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL).

GO - Molecular functioni

  • scavenger receptor activity Source: MGI

GO - Biological processi

  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: MGI
  • receptor-mediated endocytosis Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Scavenger receptor class F member 2
Alternative name(s):
Scavenger receptor expressed by endothelial cells 2 protein
Short name:
SREC-II
Gene namesi
Name:Scarf2
Synonyms:Srec2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1858430. Scarf2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini34 – 433400ExtracellularSequence analysisAdd
BLAST
Transmembranei434 – 45421HelicalSequence analysisAdd
BLAST
Topological domaini455 – 833379CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence analysisAdd
BLAST
Chaini34 – 833800Scavenger receptor class F member 2PRO_0000007740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi67 ↔ 78PROSITE-ProRule annotation
Disulfide bondi72 ↔ 90PROSITE-ProRule annotation
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence analysis
Disulfide bondi92 ↔ 101PROSITE-ProRule annotation
Disulfide bondi118 ↔ 126PROSITE-ProRule annotation
Disulfide bondi120 ↔ 133PROSITE-ProRule annotation
Disulfide bondi135 ↔ 144PROSITE-ProRule annotation
Disulfide bondi148 ↔ 155PROSITE-ProRule annotation
Disulfide bondi150 ↔ 162PROSITE-ProRule annotation
Disulfide bondi164 ↔ 173PROSITE-ProRule annotation
Disulfide bondi177 ↔ 185PROSITE-ProRule annotation
Disulfide bondi179 ↔ 192PROSITE-ProRule annotation
Disulfide bondi194 ↔ 203PROSITE-ProRule annotation
Disulfide bondi207 ↔ 214PROSITE-ProRule annotation
Disulfide bondi209 ↔ 221PROSITE-ProRule annotation
Disulfide bondi223 ↔ 232PROSITE-ProRule annotation
Disulfide bondi236 ↔ 243PROSITE-ProRule annotation
Disulfide bondi238 ↔ 250PROSITE-ProRule annotation
Disulfide bondi252 ↔ 261PROSITE-ProRule annotation
Glycosylationi302 – 3021N-linked (GlcNAc...)Sequence analysis
Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence analysis
Disulfide bondi368 ↔ 376PROSITE-ProRule annotation
Disulfide bondi371 ↔ 383PROSITE-ProRule annotation
Disulfide bondi385 ↔ 394PROSITE-ProRule annotation
Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence analysis
Modified residuei538 – 5381PhosphoserineCombined sources
Modified residuei600 – 6001PhosphoserineBy similarity
Modified residuei615 – 6151PhosphotyrosineCombined sources
Modified residuei638 – 6381PhosphoserineCombined sources
Modified residuei640 – 6401PhosphoserineCombined sources
Modified residuei695 – 6951PhosphoserineCombined sources
Modified residuei712 – 7121PhosphothreonineCombined sources

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP59222.
PRIDEiP59222.

PTM databases

iPTMnetiP59222.
PhosphoSiteiP59222.
SwissPalmiP59222.

Expressioni

Gene expression databases

BgeeiP59222.
CleanExiMM_SCARF2.
ExpressionAtlasiP59222. baseline and differential.
GenevisibleiP59222. MM.

Interactioni

Subunit structurei

Homophilic and heterophilic interaction via its extracellular domain. Interacts with SCARF1. The heterophilic interaction with SCARF1, which is stronger than the homophilic interaction with itself, is suppressed by the presence of SCARF1 ligand such as Ac-LDL.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000012161.

Structurei

3D structure databases

ProteinModelPortaliP59222.
SMRiP59222. Positions 48-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 10240EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini114 – 14532EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini140 – 17435EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini175 – 20430EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini205 – 23329EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini228 – 26235EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini364 – 39532EGF-like 7PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi639 – 71476Pro-richAdd
BLAST

Sequence similaritiesi

Contains 7 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IRWF. Eukaryota.
ENOG410YKEF. LUCA.
HOGENOMiHOG000015093.
HOVERGENiHBG023166.
InParanoidiP59222.
OMAiCEQFTGR.
OrthoDBiEOG77HDD8.
PhylomeDBiP59222.
TreeFamiTF332598.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR009030. Growth_fac_rcpt_.
IPR002049. Laminin_EGF.
IPR033327. Scarf2.
[Graphical view]
PANTHERiPTHR24043:SF5. PTHR24043:SF5. 1 hit.
PfamiPF00053. Laminin_EGF. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. EGF_Lam. 6 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P59222-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGAGSRGAG PARRQGARGL GLLLLLWLLP GLAAPQDLNP RGRNVCRTPG
60 70 80 90 100
SQVLTCCAGW RQLGDECGIA VCEGNSTCSE NEVCVRPGEC RCRHGYFGAN
110 120 130 140 150
CDTKCPRQFW GPDCKERCSC HPHGQCEDVT GQCTCHARRW GARCEHACQC
160 170 180 190 200
QHGTCHPRSG ACRCEPGWWG AQCASACYCS ATSRCDPQTG ACLCHVGWWG
210 220 230 240 250
RSCNNQCACN SSPCEQQSGR CQCRERMFGA RCDRYCQCSH GRCHPVDGTC
260 270 280 290 300
ACDPGYRGKY CREPCPAGFY GPGCRRRCGQ CKGQQPCTVV EGRCLTCEPG
310 320 330 340 350
WNGTKCDQPC ATGFYGEGCG HRCPPCRDGH ACNHVTGKCT HCNAGWIGDR
360 370 380 390 400
CETKCSNGTY GEDCAFVCSD CGSGHCDFQS GRCLCSPGVH GPHCNVTCPA
410 420 430 440 450
GLHGVDCAQA CSCHEESCDP VTGACHLETN QRKGVMGAGA LLTLLLGLLL
460 470 480 490 500
SLLGCCCACR GKDSARRELT LGRKKAPQRF CGSFSRISMK LPRIPLRRQK
510 520 530 540 550
LPKVVVAHHD LDNTLNCSFL DPPSGLEQPS PSWSSRASFS SFDTTDEGPV
560 570 580 590 600
YCVPHEEATA DSRDLEATAA LTEVAAVSLE PTGTSTPGEE AAVLPASSDS
610 620 630 640 650
ERSASSVEGP SGALYARVAR REARPARTRN EAGGLSLSPS PERRKPPPPD
660 670 680 690 700
PATKPKVSWI HGKHSAAAAA PSPPPAGRKA APSPSGRKRT PSNSSVQPPG
710 720 730 740 750
LTEEAPGPAS PTPPRARARG RGLGLSEPTD AGGPPRSAPE AASMLAAELR
760 770 780 790 800
DKTRSLGRAE KPPPPQKAKR SVLPAATVRT ASASEASGSE KAAASAPAPE
810 820 830
TPRKKTPIQK PPRKKSREAA GEPSRAGTAP GAS
Length:833
Mass (Da):87,871
Last modified:January 17, 2003 - v1
Checksum:i51EADEEAACAFF005
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF522197 mRNA. Translation: AAN45862.1.
CCDSiCCDS28010.1.
RefSeqiNP_722485.1. NM_153790.3.
UniGeneiMm.194950.

Genome annotation databases

EnsembliENSMUST00000012161; ENSMUSP00000012161; ENSMUSG00000012017.
GeneIDi224024.
KEGGimmu:224024.
UCSCiuc007ymd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF522197 mRNA. Translation: AAN45862.1.
CCDSiCCDS28010.1.
RefSeqiNP_722485.1. NM_153790.3.
UniGeneiMm.194950.

3D structure databases

ProteinModelPortaliP59222.
SMRiP59222. Positions 48-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000012161.

PTM databases

iPTMnetiP59222.
PhosphoSiteiP59222.
SwissPalmiP59222.

Proteomic databases

PaxDbiP59222.
PRIDEiP59222.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000012161; ENSMUSP00000012161; ENSMUSG00000012017.
GeneIDi224024.
KEGGimmu:224024.
UCSCiuc007ymd.1. mouse.

Organism-specific databases

CTDi91179.
MGIiMGI:1858430. Scarf2.

Phylogenomic databases

eggNOGiENOG410IRWF. Eukaryota.
ENOG410YKEF. LUCA.
HOGENOMiHOG000015093.
HOVERGENiHBG023166.
InParanoidiP59222.
OMAiCEQFTGR.
OrthoDBiEOG77HDD8.
PhylomeDBiP59222.
TreeFamiTF332598.

Miscellaneous databases

ChiTaRSiScarf2. mouse.
NextBioi377021.
PROiP59222.
SOURCEiSearch...

Gene expression databases

BgeeiP59222.
CleanExiMM_SCARF2.
ExpressionAtlasiP59222. baseline and differential.
GenevisibleiP59222. MM.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR009030. Growth_fac_rcpt_.
IPR002049. Laminin_EGF.
IPR033327. Scarf2.
[Graphical view]
PANTHERiPTHR24043:SF5. PTHR24043:SF5. 1 hit.
PfamiPF00053. Laminin_EGF. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. EGF_Lam. 6 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SREC-II, a new member of the scavenger receptor type F family, trans-interacts with SREC-I through its extracellular domain."
    Ishii J., Adachi H., Aoki J., Koizumi H., Tomita S., Suzuki T., Tsujimoto M., Inoue K., Arai H.
    J. Biol. Chem. 277:39696-39702(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Strain: C57BL/6J.
  2. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-615, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-638; SER-640; SER-695 AND THR-712, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Lung and Spleen.

Entry informationi

Entry nameiSREC2_MOUSE
AccessioniPrimary (citable) accession number: P59222
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: January 17, 2003
Last modified: May 11, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.