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CD2-associated protein (Mesenchyme-to-epithelium transition protein with SH3 domains 1) (METS-1)

 CD2AP_MOUSE             Reviewed;         637 AA.
Q9JLQ0; E9QL86; O88903; Q8K4Z1; Q8VCI9;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
25-OCT-2017, entry version 148.
RecName: Full=CD2-associated protein;
AltName: Full=Mesenchyme-to-epithelium transition protein with SH3 domains 1;
Short=METS-1;
Name=Cd2ap; Synonyms=Mets1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CD2.
PubMed=9741631; DOI=10.1016/S0092-8674(00)81608-6;
Dustin M.L., Olszowy M.W., Holdorf A.D., Li J., Bromley S., Desai N.,
Widder P., Rosenberger F., van der Merwe P.A., Allen P.M., Shaw A.S.;
"A novel adaptor protein orchestrates receptor patterning and
cytoskeletal polarity in T-cell contacts.";
Cell 94:667-677(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PKD2.
PubMed=10913159; DOI=10.1074/jbc.M006624200;
Lehtonen S., Ora A., Olkkonen V.M., Geng L., Zerial M., Somlo S.,
Lehtonen E.;
"In vivo interaction of the adapter protein CD2-associated protein
with the type 2 polycystic kidney disease protein, polycystin-2.";
J. Biol. Chem. 275:32888-32893(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Meton I., Le Marchand-Brustel Y., Cormont M.;
"Role of the interaction between CD2AP and c-Cbl.";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 394-637.
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NPHS1, AND DISRUPTION
PHENOTYPE.
PubMed=10514378; DOI=10.1126/science.286.5438.312;
Shih N.Y., Li J., Karpitskii V., Nguyen A., Dustin M.L., Kanagawa O.,
Miner J.H., Shaw A.S.;
"Congenital nephrotic syndrome in mice lacking CD2-associated
protein.";
Science 286:312-315(1999).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH NPHS1.
PubMed=11733379; DOI=10.1016/S0002-9440(10)63080-5;
Shih N.Y., Li J., Cotran R., Mundel P., Miner J.H., Shaw A.S.;
"CD2AP localizes to the slit diaphragm and binds to nephrin via a
novel C-terminal domain.";
Am. J. Pathol. 159:2303-2308(2001).
[8]
INTERACTION WITH NPHS1 AND NPHS2.
PubMed=11733557; DOI=10.1172/JCI200112849;
Schwarz K., Simons M., Reiser J., Saleem M.A., Faul C., Kriz W.,
Shaw A.S., Holzman L.B., Mundel P.;
"Podocin, a raft-associated component of the glomerular slit
diaphragm, interacts with CD2AP and nephrin.";
J. Clin. Invest. 108:1621-1629(2001).
[9]
INTERACTION WITH F-ACTIN.
PubMed=12217865; DOI=10.1152/ajprenal.00312.2001;
Lehtonen S., Zhao F., Lehtonen E.;
"CD2-associated protein directly interacts with the actin
cytoskeleton.";
Am. J. Physiol. 283:F734-F743(2002).
[10]
INTERACTION WITH WTIP.
PubMed=14736876; DOI=10.1074/jbc.M314155200;
Srichai M.B., Konieczkowski M., Padiyar A., Konieczkowski D.J.,
Mukherjee A., Hayden P.S., Kamat S., El-Meanawy M.A., Khan S.,
Mundel P., Lee S.B., Bruggeman L.A., Schelling J.R., Sedor J.R.;
"A WT1 co-regulator controls podocyte phenotype by shuttling between
adhesion structures and nucleus.";
J. Biol. Chem. 279:14398-14408(2004).
[11]
INTERACTION WITH DDN.
PubMed=17537921; DOI=10.1073/pnas.0700917104;
Asanuma K., Campbell K.N., Kim K., Faul C., Mundel P.;
"Nuclear relocation of the nephrin and CD2AP-binding protein dendrin
promotes apoptosis of podocytes.";
Proc. Natl. Acad. Sci. U.S.A. 104:10134-10139(2007).
[12]
INTERACTION WITH RET, AND TISSUE SPECIFICITY.
PubMed=18753381; DOI=10.1523/JNEUROSCI.2738-08.2008;
Tsui C.C., Pierchala B.A.;
"CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the
regulation of ret signal transduction.";
J. Neurosci. 28:8789-8800(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-458; SER-510
AND SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
STRUCTURE BY NMR OF 270-329.
PubMed=17922258; DOI=10.1007/s10858-007-9201-7;
Ortega Roldan J.L., Romero Romero M.L., Ora A., Ab E.,
Lopez Mayorga O., Azuaga A.I., van Nuland N.A.;
"The high resolution NMR structure of the third SH3 domain of CD2AP.";
J. Biomol. NMR 39:331-336(2007).
-!- FUNCTION: Seems to act as an adapter protein between membrane
proteins and the actin cytoskeleton (By similarity). In
collaboration with CBLC, modulates the rate of RET turnover and
may act as regulatory checkpoint that limits the potency of GDNF
on neuronal survival. Controls CBLC function, converting it from
an inhibitor to a promoter of RET degradation (By similarity). May
play a role in receptor clustering and cytoskeletal polarity in
the junction between T-cell and antigen-presenting cell
(PubMed:9741631). May anchor the podocyte slit diaphragm to the
actin cytoskeleton in renal glomerolus (PubMed:10514378). Also
required for cytokinesis. Plays a role in epithelial cell
junctions formation (By similarity).
{ECO:0000250|UniProtKB:F1LRS8, ECO:0000250|UniProtKB:Q9Y5K6,
ECO:0000269|PubMed:10514378, ECO:0000269|PubMed:9741631}.
-!- SUBUNIT: Homodimer. Interacts with F-actin, PKD2, NPHS1 and NPHS2.
Interacts with WTIP. Interacts with DDN; interaction is direct.
Interacts (via SH3 2 domain) with CBL (via phosphorylated C-
terminus). Interacts with BCAR1/p130Cas (via SH3 domain).
Interacts with MVB12A and ARHGAP17. Interacts with ANLN, CD2 and
CBLB. Interacts with PDCD6IP and TSG101. Interacts with RIN3.
Interacts directly with RET (inactive) and CBLC; upon RET
activation by GDNF suggested to dissociate from RET as CBLC:CD2AP
complex. Interacts with CGNL1 and SH3BP1; probably part of a
complex at cell junctions. Interacts with CAPZA1.
{ECO:0000250|UniProtKB:Q9Y5K6, ECO:0000269|PubMed:10514378,
ECO:0000269|PubMed:10913159, ECO:0000269|PubMed:11733379,
ECO:0000269|PubMed:11733557, ECO:0000269|PubMed:12217865,
ECO:0000269|PubMed:14736876, ECO:0000269|PubMed:17537921,
ECO:0000269|PubMed:18753381, ECO:0000269|PubMed:9741631,
ECO:0000305}.
-!- INTERACTION:
P22682:Cbl; NbExp=5; IntAct=EBI-644807, EBI-640919;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q9Y5K6}. Cell projection, ruffle
{ECO:0000250|UniProtKB:Q9Y5K6}. Cell junction
{ECO:0000250|UniProtKB:Q9Y5K6}. Note=Colocalizes with F-actin and
BCAR1/p130Cas in membrane ruffles (By similarity). Located at
podocyte slit diaphragm between podocyte foot processes
(PubMed:10514378, PubMed:11733379). During late anaphase and
telophase, concentrates in the vicinity of the midzone
microtubules and in the midbody in late telophase (By similarity).
{ECO:0000250|UniProtKB:Q9Y5K6, ECO:0000269|PubMed:10514378,
ECO:0000269|PubMed:11733379}.
-!- TISSUE SPECIFICITY: Expressed in podocytes (at protein level).
{ECO:0000269|PubMed:18753381}.
-!- DOMAIN: Potential homodimerization is mediated by the coiled coil
domain. {ECO:0000250}.
-!- PTM: Phosphorylated on tyrosine residues; probably by c-Abl, Fyn
and c-Src. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Death at 6 to 7 weeks of age from renal
failure. Mice show defects in epithelial foot processes,
accompanied by mesangial cell hyperplasia and extracellular matrix
deposition. {ECO:0000269|PubMed:10514378}.
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EMBL; AF077003; AAC36099.1; -; mRNA.
EMBL; AF149092; AAF73150.1; -; mRNA.
EMBL; AJ459109; CAD30510.1; -; mRNA.
EMBL; AC111082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC019744; AAH19744.1; -; mRNA.
CCDS; CCDS50114.1; -.
RefSeq; NP_033977.3; NM_009847.3.
UniGene; Mm.218637; -.
PDB; 2JTE; NMR; -; A=270-329.
PDB; 2KRM; NMR; -; A=2-58.
PDB; 2KRN; NMR; -; A=111-166.
PDB; 2KRO; NMR; -; A=270-329.
PDB; 2LZ6; NMR; -; B=270-329.
PDB; 2MCN; NMR; -; A=2-62.
PDBsum; 2JTE; -.
PDBsum; 2KRM; -.
PDBsum; 2KRN; -.
PDBsum; 2KRO; -.
PDBsum; 2LZ6; -.
PDBsum; 2MCN; -.
ProteinModelPortal; Q9JLQ0; -.
SMR; Q9JLQ0; -.
BioGrid; 198584; 81.
CORUM; Q9JLQ0; -.
IntAct; Q9JLQ0; 82.
MINT; MINT-255809; -.
STRING; 10090.ENSMUSP00000024709; -.
iPTMnet; Q9JLQ0; -.
PhosphoSitePlus; Q9JLQ0; -.
EPD; Q9JLQ0; -.
MaxQB; Q9JLQ0; -.
PaxDb; Q9JLQ0; -.
PeptideAtlas; Q9JLQ0; -.
PRIDE; Q9JLQ0; -.
Ensembl; ENSMUST00000024709; ENSMUSP00000024709; ENSMUSG00000061665.
GeneID; 12488; -.
KEGG; mmu:12488; -.
UCSC; uc008cot.1; mouse.
CTD; 23607; -.
MGI; MGI:1330281; Cd2ap.
eggNOG; KOG4348; Eukaryota.
eggNOG; ENOG410XQBY; LUCA.
GeneTree; ENSGT00530000063594; -.
HOGENOM; HOG000231405; -.
HOVERGEN; HBG057824; -.
InParanoid; Q9JLQ0; -.
KO; K13738; -.
OMA; YDAVHDD; -.
OrthoDB; EOG091G041Q; -.
TreeFam; TF350191; -.
Reactome; R-MMU-373753; Nephrin family interactions.
ChiTaRS; Cd2ap; mouse.
EvolutionaryTrace; Q9JLQ0; -.
PRO; PR:Q9JLQ0; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000061665; -.
CleanEx; MM_CD2AP; -.
Genevisible; Q9JLQ0; MM.
GO; GO:0005938; C:cell cortex; ISO:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031941; C:filamentous actin; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0001726; C:ruffle; ISO:MGI.
GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
GO; GO:0005172; F:vascular endothelial growth factor receptor binding; IEA:Ensembl.
GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IEA:Ensembl.
GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
GO; GO:0032911; P:negative regulation of transforming growth factor beta1 production; IGI:MGI.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IGI:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IGI:MGI.
GO; GO:0048259; P:regulation of receptor-mediated endocytosis; IEA:Ensembl.
GO; GO:0016050; P:vesicle organization; IEA:Ensembl.
CDD; cd12053; SH3_CD2AP_1; 1.
CDD; cd12054; SH3_CD2AP_2; 1.
CDD; cd12056; SH3_CD2AP_3; 1.
InterPro; IPR028445; CD2AP.
InterPro; IPR035775; CD2AP_SH3_1.
InterPro; IPR035777; CD2AP_SH3_3.
InterPro; IPR035776; CD2AP_SH_2.
InterPro; IPR036028; SH3-like_dom.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR14167:SF23; PTHR14167:SF23; 1.
Pfam; PF00018; SH3_1; 1.
Pfam; PF14604; SH3_9; 2.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 3.
SUPFAM; SSF50044; SSF50044; 3.
PROSITE; PS50002; SH3; 3.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Cell junction;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Isopeptide bond; Mitosis; Phosphoprotein;
Reference proteome; Repeat; SH3 domain; SH3-binding; Ubl conjugation.
CHAIN 1 637 CD2-associated protein.
/FTId=PRO_0000089436.
DOMAIN 1 59 SH3 1; truncated. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 108 167 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 269 330 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 1 175 Interaction with ANLN and localization to
the midbody. {ECO:0000250}.
COILED 578 636 {ECO:0000255}.
MOTIF 336 352 SH3-binding. {ECO:0000255}.
MOTIF 378 397 SH3-binding. {ECO:0000255}.
MOTIF 410 422 SH3-binding. {ECO:0000255}.
COMPBIAS 336 422 Pro-rich.
MOD_RES 80 80 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y5K6}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y5K6}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 458 458 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000250|UniProtKB:F1LRS8}.
MOD_RES 510 510 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 514 514 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 563 563 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Y5K6}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y5K6}.
CROSSLNK 58 58 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y5K6}.
CROSSLNK 523 523 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y5K6}.
CONFLICT 78 78 V -> E (in Ref. 2; AAF73150).
{ECO:0000305}.
CONFLICT 107 107 Missing (in Ref. 1; AAC36099).
{ECO:0000305}.
CONFLICT 110 110 K -> Q (in Ref. 1; AAC36099).
{ECO:0000305}.
CONFLICT 244 244 P -> R (in Ref. 1; AAC36099).
{ECO:0000305}.
CONFLICT 295 297 IIH -> LS (in Ref. 1; AAC36099).
{ECO:0000305}.
CONFLICT 392 392 P -> PTAPTKA (in Ref. 1; AAC36099).
{ECO:0000305}.
CONFLICT 545 545 S -> P (in Ref. 2; AAF73150, 3; CAD30510
and 5; AAH19744). {ECO:0000305}.
CONFLICT 578 578 R -> K (in Ref. 2; AAF73150, 3; CAD30510
and 5; AAH19744). {ECO:0000305}.
STRAND 4 6 {ECO:0000244|PDB:2KRM}.
STRAND 8 10 {ECO:0000244|PDB:2MCN}.
STRAND 14 17 {ECO:0000244|PDB:2KRM}.
STRAND 25 31 {ECO:0000244|PDB:2KRM}.
STRAND 37 42 {ECO:0000244|PDB:2KRM}.
STRAND 45 50 {ECO:0000244|PDB:2KRM}.
HELIX 51 53 {ECO:0000244|PDB:2KRM}.
STRAND 54 56 {ECO:0000244|PDB:2KRM}.
STRAND 113 115 {ECO:0000244|PDB:2KRN}.
STRAND 134 142 {ECO:0000244|PDB:2KRN}.
STRAND 145 150 {ECO:0000244|PDB:2KRN}.
STRAND 153 158 {ECO:0000244|PDB:2KRN}.
TURN 159 161 {ECO:0000244|PDB:2KRN}.
STRAND 270 278 {ECO:0000244|PDB:2JTE}.
STRAND 283 287 {ECO:0000244|PDB:2JTE}.
STRAND 295 301 {ECO:0000244|PDB:2JTE}.
STRAND 303 313 {ECO:0000244|PDB:2JTE}.
STRAND 316 321 {ECO:0000244|PDB:2JTE}.
HELIX 322 324 {ECO:0000244|PDB:2JTE}.
STRAND 325 329 {ECO:0000244|PDB:2JTE}.
SEQUENCE 637 AA; 70450 MW; 0B618FE82AF12332 CRC64;
MVDYIVEYDY DAVHDDELTI RVGEIIRNVK KLQEEGWLEG ELNGRRGMFP DNFVKEIKRE
TEPKDDNLPI KRERQGNVAS LVQRISTYGL PAGGIQPHPQ TKAIKKKTKK RQCKVLFDYS
PQNEDELELI VGDVIDVIEE VEEGWWSGTL NNKLGLFPSN FVKELESTED GETHNAQEES
EVPLTGPTSP LPSPGNGSEP APGSVAQPKK IRGIGFGDIF KEGSVKLRTR TSSSETEEKK
TEKPLILQPL GSRTQNVEVT KPDVDGKIKA KEYCRTLFPY TGTNEDELTF REGEIIHLIS
KETGEAGWWK GELNGKEGVF PDNFAVQISE LDKDFPKPKK PPPPAKGPAP KPDLSAAEKK
AFPLKAEEKD EKSLLEQKPS KPAAPQVPPK KPTAPTKASN LLRSPGAVYP KRPEKPVPPP
PPAAKINGEV SIISSKIDTE PVSKPKLDPE QLPVRPKSVD LDAFVARNSK ETDDVNFDDI
ASSENLLHLT ANRPKMPGRR LPGRFNGGHS PTQSPEKTLK LPKEDDSGNL KPLEFKKDAS
YSSKSSLSTP SSASKVNTAA FLTPLELKAK AEADDGKRNS VDELRAQIIE LLCIVDALKK
DHGKELEKLR KELEEEKAMR SNLEVEIAKL KKAVLLS


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EIAAB38670 Homo sapiens,Human,KIAA0813,MEGF4,Multiple EGF-like domains protein 4,Multiple epidermal growth factor-like domains protein 4,SLIL1,Slit homolog 1 protein,SLIT1,Slit-1
EIAAB38671 Megf4,Multiple EGF-like domains protein 4,Multiple epidermal growth factor-like domains protein 4,Rat,Rattus norvegicus,Slit homolog 1 protein,Slit1,Slit-1
EIAAB38674 Megf5,Multiple EGF-like domains protein 5,Multiple epidermal growth factor-like domains protein 5,Rat,Rattus norvegicus,Slit homolog 3 protein,Slit3,Slit-3
EIAAB12605 EGFL7,EGF-like protein 7,Epidermal growth factor-like protein 7,Homo sapiens,Human,MEGF7,Multiple EGF-like domains protein 7,Multiple epidermal growth factor-like domains protein 7,NOTCH4-like protein
EIAAB14453 Fat2,Fath2,Megf1,Multiple EGF-like domains protein 1,Multiple epidermal growth factor-like domains protein 1,Protocadherin Fat 2,Rat,Rattus norvegicus
EIAAB12603 Egfl7,EGF-like protein 7,Epidermal growth factor-like protein 7,Megf7,Mouse,Multiple EGF-like domains protein 7,Multiple epidermal growth factor-like domains protein 7,Mus musculus,NOTCH4-like protein
EIAAB06751 Cadherin EGF LAG seven-pass G-type receptor 3,Celsr3,Megf2,Multiple EGF-like domains protein 2,Multiple epidermal growth factor-like domains protein 2,Rat,Rattus norvegicus
EIAAB06748 Cadherin EGF LAG seven-pass G-type receptor 2,Celsr2,Megf3,Multiple EGF-like domains protein 3,Multiple epidermal growth factor-like domains protein 3,Rat,Rattus norvegicus
SMC-328D SHANK2, S23b-6 Monoclonals AntibodiesS23b-6 Fusion protein amino acids 84-309 (SH3_PDZ domains) of rat Shank2 (SH3 and multiple ankyrin repeat domains protein 2 (accession number Q9QX74) 100ug


 

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