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Exostosin-like 3 (EC 2.4.1.223) (EXT-related protein 1) (Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase) (Hereditary multiple exostoses gene isolog) (Multiple exostosis-like protein 3) (Putative tumor suppressor protein EXTL3)

 EXTL3_HUMAN             Reviewed;         919 AA.
O43909; D3DST8; O00225; Q53XT3;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-OCT-2017, entry version 165.
RecName: Full=Exostosin-like 3 {ECO:0000303|PubMed:9479495};
EC=2.4.1.223 {ECO:0000305|PubMed:28132690, ECO:0000305|PubMed:28148688};
AltName: Full=EXT-related protein 1 {ECO:0000303|PubMed:9473480};
AltName: Full=Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase;
AltName: Full=Hereditary multiple exostoses gene isolog {ECO:0000303|Ref.9};
AltName: Full=Multiple exostosis-like protein 3 {ECO:0000303|Ref.6};
AltName: Full=Putative tumor suppressor protein EXTL3 {ECO:0000303|PubMed:9479495};
Name=EXTL3 {ECO:0000312|HGNC:HGNC:3518};
Synonyms=EXTL1L, EXTR1, KIAA0519;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9479495; DOI=10.1006/geno.1997.5101;
van Hul W., Wuyts W., Hendrickx J., Speleman F., Wauters J.,
de Boulle K., van Roy N., Bossuyt P., Willems P.J.;
"Identification of a third EXT-like gene (EXTL3) belonging to the EXT
gene family.";
Genomics 47:230-237(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetus, and Testis;
PubMed=9473480; DOI=10.1006/bbrc.1997.8062;
Saito T., Seki N., Yamauchi M., Tsuji S., Hayashi A., Kozuma S.,
Hori T.-A.;
"Structure, chromosomal location, and expression profile of EXTR1 and
EXTR2, new members of the multiple exostoses gene family.";
Biochem. Biophys. Res. Commun. 243:61-66(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. IX.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:31-39(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Deng H.-X., Xu L., Xia J.-H., Fan C., Pan Q., Liu C.-Y., Ruan Q.-G.;
"Molecular cloning of a candidate gene for multiple exostoses.";
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Sato T.;
"The human EXTL1L/EXTR1/EXTL3 gene at 8p11-p12, the third breast
cancer susceptibility gene locus, is not mutated in breast and various
cancers.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 470-919.
Adams M.D.;
"Human chromosome 8 BAC clone CIT987SK-2A8 complete sequence.";
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[10]
SUBCELLULAR LOCATION.
PubMed=10639137; DOI=10.1073/pnas.97.2.668;
McCormick C., Duncan G., Goutsos K.T., Tufaro F.;
"The putative tumor suppressors EXT1 and EXT2 form a stable complex
that accumulates in the Golgi apparatus and catalyzes the synthesis of
heparan sulfate.";
Proc. Natl. Acad. Sci. U.S.A. 97:668-673(2000).
[11]
FUNCTION, INTERACTION WITH REG3A, AND TISSUE SPECIFICITY.
PubMed=22727489; DOI=10.1016/j.immuni.2012.04.010;
Lai Y., Li D., Li C., Muehleisen B., Radek K.A., Park H.J., Jiang Z.,
Li Z., Lei H., Quan Y., Zhang T., Wu Y., Kotol P., Morizane S.,
Hata T.R., Iwatsuki K., Tang C., Gallo R.L.;
"The antimicrobial protein REG3A regulates keratinocyte proliferation
and differentiation after skin injury.";
Immunity 37:74-84(2012).
[12]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION,
INVOLVEMENT IN ISDNA, VARIANTS ISDNA LEU-461; CYS-513; SER-657 AND
ASP-670, CHARACTERIZATION OF VARIANTS ISDNA LEU-461; CYS-513; SER-657
AND ASP-670, AND VARIANT LEU-442.
PubMed=28132690; DOI=10.1016/j.ajhg.2017.01.013;
Oud M.M., Tuijnenburg P., Hempel M., van Vlies N., Ren Z.,
Ferdinandusse S., Jansen M.H., Santer R., Johannsen J., Bacchelli C.,
Alders M., Li R., Davies R., Dupuis L., Cale C.M., Wanders R.J.,
Pals S.T., Ocaka L., James C., Mueller I., Lehmberg K., Strom T.,
Engels H., Williams H.J., Beales P., Roepman R., Dias P.,
Brunner H.G., Cobben J.M., Hall C., Hartley T., Le Quesne Stabej P.,
Mendoza-Londono R., Davies E.G., de Sousa S.B., Lessel D., Arts H.H.,
Kuijpers T.W.;
"Mutations in EXTL3 cause neuro-immuno-skeletal dysplasia syndrome.";
Am. J. Hum. Genet. 100:281-296(2017).
[13]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, VARIANTS ISDNA TRP-339 AND
LEU-461, AND CHARACTERIZATION OF VARIANTS ISDNA TRP-339 AND LEU-461.
PubMed=28148688; DOI=10.1084/jem.20161525;
Volpi S., Yamazaki Y., Brauer P.M., van Rooijen E., Hayashida A.,
Slavotinek A., Sun Kuehn H., Di Rocco M., Rivolta C., Bortolomai I.,
Du L., Felgentreff K., Ott de Bruin L., Hayashida K., Freedman G.,
Marcovecchio G.E., Capuder K., Rath P., Luche N., Hagedorn E.J.,
Buoncompagni A., Royer-Bertrand B., Giliani S., Poliani P.L.,
Imberti L., Dobbs K., Poulain F.E., Martini A., Manis J.,
Linhardt R.J., Bosticardo M., Rosenzweig S.D., Lee H., Puck J.M.,
Zuniga-Pfluecker J.C., Zon L., Park P.W., Superti-Furga A.,
Notarangelo L.D.;
"EXTL3 mutations cause skeletal dysplasia, immune deficiency, and
developmental delay.";
J. Exp. Med. 214:623-637(2017).
-!- FUNCTION: Glycosyltransferase which regulates the biosynthesis of
heparan sulfate (HS). Important for both skeletal development and
hematopoiesis, through the formation of HS proteoglycans (HSPGs)
(PubMed:28132690, PubMed:28148688). Required for the function of
REG3A in regulating keratinocyte proliferation and differentiation
(PubMed:22727489). {ECO:0000269|PubMed:22727489,
ECO:0000269|PubMed:28132690, ECO:0000269|PubMed:28148688}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + [protein]-
3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-
D-Xyl)-L-serine = UDP + [protein]-3-O-(alpha-D-GlcNAc-(1->4)-beta-
D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-
serine. {ECO:0000305|PubMed:28132690,
ECO:0000305|PubMed:28148688}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:Q9ES89};
-!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
{ECO:0000269|PubMed:28132690, ECO:0000269|PubMed:28148688}.
-!- SUBUNIT: Interacts with REG3A. {ECO:0000269|PubMed:22727489}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10639137}; Single-pass type II membrane
protein {ECO:0000269|PubMed:10639137}. Golgi apparatus
{ECO:0000269|PubMed:28132690}.
-!- TISSUE SPECIFICITY: Ubiquitous. Expressed in keratinocytes.
{ECO:0000269|PubMed:22727489}.
-!- DISEASE: Immunoskeletal dysplasia with neurodevelopmental
abnormalities (ISDNA) [MIM:617425]: An autosomal recessive
disorder characterized by variable skeletal abnormalities and
neurodevelopmental defects. Neurologic manifestations include
intellectual disability and motor delay. Some patients manifest
hypotonia and seizures. Skeletal features include disproportionate
short stature, cervical malformations, epiphyseal and metaphyseal
dysplasia, and rarely premature craniosynostosis with progressive
microcephaly. Severe combined immunodeficiency with a complete
absence of T cells is observed in some patients.
{ECO:0000269|PubMed:28132690, ECO:0000269|PubMed:28148688}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1, Met-6 or Met-20 is the
initiator. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA25445.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Exostosin-like 3;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_531";
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EMBL; AF001690; AAC39598.1; -; mRNA.
EMBL; U76188; AAB93670.1; -; mRNA.
EMBL; AB007042; BAA24080.1; -; mRNA.
EMBL; AB011091; BAA25445.2; ALT_INIT; mRNA.
EMBL; AF029231; AAD01877.1; -; mRNA.
EMBL; AF083551; AAD42041.1; -; mRNA.
EMBL; BT007353; AAP36017.1; -; mRNA.
EMBL; CH471080; EAW63507.1; -; Genomic_DNA.
EMBL; CH471080; EAW63508.1; -; Genomic_DNA.
EMBL; CH471080; EAW63509.1; -; Genomic_DNA.
EMBL; BC006363; AAH06363.1; -; mRNA.
EMBL; U96629; AAB67602.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS6070.1; -.
PIR; JC5934; JC5934.
RefSeq; NP_001431.1; NM_001440.3.
RefSeq; XP_011542742.1; XM_011544440.2.
UniGene; Hs.491354; -.
UniGene; Hs.744019; -.
ProteinModelPortal; O43909; -.
SMR; O43909; -.
BioGrid; 108438; 47.
IntAct; O43909; 8.
STRING; 9606.ENSP00000220562; -.
CAZy; GT47; Glycosyltransferase Family 47.
CAZy; GT64; Glycosyltransferase Family 64.
iPTMnet; O43909; -.
PhosphoSitePlus; O43909; -.
EPD; O43909; -.
MaxQB; O43909; -.
PaxDb; O43909; -.
PeptideAtlas; O43909; -.
PRIDE; O43909; -.
DNASU; 2137; -.
Ensembl; ENST00000220562; ENSP00000220562; ENSG00000012232.
GeneID; 2137; -.
KEGG; hsa:2137; -.
UCSC; uc003xgz.3; human.
CTD; 2137; -.
DisGeNET; 2137; -.
EuPathDB; HostDB:ENSG00000012232.8; -.
GeneCards; EXTL3; -.
HGNC; HGNC:3518; EXTL3.
HPA; CAB025387; -.
MIM; 605744; gene.
MIM; 617425; phenotype.
neXtProt; NX_O43909; -.
OpenTargets; ENSG00000012232; -.
PharmGKB; PA27930; -.
eggNOG; KOG2264; Eukaryota.
eggNOG; ENOG410XNPM; LUCA.
GeneTree; ENSGT00550000074496; -.
HOGENOM; HOG000007975; -.
HOVERGEN; HBG051526; -.
InParanoid; O43909; -.
KO; K02370; -.
OMA; RKSDTQN; -.
OrthoDB; EOG091G03XP; -.
PhylomeDB; O43909; -.
TreeFam; TF314231; -.
BioCyc; MetaCyc:HS00333-MONOMER; -.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
UniPathway; UPA00756; -.
GeneWiki; EXTL3; -.
GenomeRNAi; 2137; -.
PRO; PR:O43909; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000012232; -.
CleanEx; HS_EXTL3; -.
ExpressionAtlas; O43909; baseline and differential.
Genevisible; O43909; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0001888; F:glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004872; F:receptor activity; IEA:Ensembl.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IDA:UniProtKB.
GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IDA:UniProtKB.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR004263; Exostosin.
InterPro; IPR015338; EXT_C.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
Pfam; PF03016; Exostosin; 1.
Pfam; PF09258; Glyco_transf_64; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
Complete proteome; Disease mutation; Disulfide bond; Dwarfism;
Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Manganese; Membrane; Mental retardation;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 919 Exostosin-like 3.
/FTId=PRO_0000149657.
TOPO_DOM 1 30 Cytoplasmic. {ECO:0000255}.
TRANSMEM 31 51 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 52 919 Lumenal. {ECO:0000255}.
REGION 723 728 Substrate binding.
{ECO:0000250|UniProtKB:Q9ES89}.
REGION 744 746 Substrate binding.
{ECO:0000250|UniProtKB:Q9ES89}.
REGION 829 833 Substrate binding.
{ECO:0000250|UniProtKB:Q9ES89}.
ACT_SITE 833 833 {ECO:0000250|UniProtKB:Q9ES89}.
METAL 746 746 Manganese; catalytic.
{ECO:0000250|UniProtKB:Q9ES89}.
BINDING 697 697 Substrate.
{ECO:0000250|UniProtKB:Q9ES89}.
BINDING 774 774 Substrate.
{ECO:0000250|UniProtKB:Q9ES89}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WVL6}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 592 592 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 790 790 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 831 879 {ECO:0000250|UniProtKB:Q9ES89}.
VARIANT 339 339 R -> W (in ISDNA; changed
glycosaminoglycan synthesis).
{ECO:0000269|PubMed:28148688}.
/FTId=VAR_079089.
VARIANT 442 442 V -> L (in dbSNP:rs116659770).
{ECO:0000269|PubMed:28132690}.
/FTId=VAR_079090.
VARIANT 461 461 P -> L (in ISDNA; changed
glycosaminoglycan synthesis;
dbSNP:rs554294508).
{ECO:0000269|PubMed:28132690,
ECO:0000269|PubMed:28148688}.
/FTId=VAR_079091.
VARIANT 513 513 R -> C (in ISDNA; changed
glycosaminoglycan synthesis; no
localization to Golgi apparatus in
patient fibroblasts).
{ECO:0000269|PubMed:28132690}.
/FTId=VAR_079092.
VARIANT 550 550 A -> V (in dbSNP:rs35781576).
/FTId=VAR_061194.
VARIANT 657 657 N -> S (in ISDNA; changed
glycosaminoglycan synthesis).
{ECO:0000269|PubMed:28132690}.
/FTId=VAR_079093.
VARIANT 670 670 Y -> D (in ISDNA; changed
glycosaminoglycan synthesis).
{ECO:0000269|PubMed:28132690}.
/FTId=VAR_079094.
VARIANT 706 706 L -> P (in dbSNP:rs2269452).
/FTId=VAR_049229.
SEQUENCE 919 AA; 104749 MW; 200ADD4DAB4A39FD CRC64;
MTGYTMLRNG GAGNGGQTCM LRWSNRIRLT WLSFTLFVIL VFFPLIAHYY LTTLDEADEA
GKRIFGPRVG NELCEVKHVL DLCRIRESVS EELLQLEAKR QELNSEIAKL NLKIEACKKS
IENAKQDLLQ LKNVISQTEH SYKELMAQNQ PKLSLPIRLL PEKDDAGLPP PKATRGCRLH
NCFDYSRCPL TSGFPVYVYD SDQFVFGSYL DPLVKQAFQA TARANVYVTE NADIACLYVI
LVGEMQEPVV LRPAELEKQL YSLPHWRTDG HNHVIINLSR KSDTQNLLYN VSTGRAMVAQ
STFYTVQYRP GFDLVVSPLV HAMSEPNFME IPPQVPVKRK YLFTFQGEKI ESLRSSLQEA
RSFEEEMEGD PPADYDDRII ATLKAVQDSK LDQVLVEFTC KNQPKPSLPT EWALCGERED
RLELLKLSTF ALIITPGDPR LVISSGCATR LFEALEVGAV PVVLGEQVQL PYQDMLQWNE
AALVVPKPRV TEVHFLLRSL SDSDLLAMRR QGRFLWETYF STADSIFNTV LAMIRTRIQI
PAAPIREEAA AEIPHRSGKA AGTDPNMADN GDLDLGPVET EPPYASPRYL RNFTLTVTDF
YRSWNCAPGP FHLFPHTPFD PVLPSEAKFL GSGTGFRPIG GGAGGSGKEF QAALGGNVPR
EQFTVVMLTY EREEVLMNSL ERLNGLPYLN KVVVVWNSPK LPSEDLLWPD IGVPIMVVRT
EKNSLNNRFL PWNEIETEAI LSIDDDAHLR HDEIMFGFRV WREARDRIVG FPGRYHAWDI
PHQSWLYNSN YSCELSMVLT GAAFFHKYYA YLYSYVMPQA IRDMVDEYIN CEDIAMNFLV
SHITRKPPIK VTSRWTFRCP GCPQALSHDD SHFHERHKCI NFFVKVYGYM PLLYTQFRVD
SVLFKTRLPH DKTKCFKFI


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18-003-42487 Ret finger protein 2 - Leukemia-associated protein 5; B-cell chronic lymphocytic leukemia tumor suppressor Leu5; Putative tumor suppressor RFP2; Tripartite motif-containing protein 13; RING finger pro 0.05 mg Aff Pur
EIAAB31151 67-11-3 protein,Liver-related putative tumor suppressor,Lpts,LPTS1,Mouse,Mus musculus,PIN2_TERF1-interacting telomerase inhibitor 1,Pin2-interacting protein X1,Pinx1,TRF1-interacting protein 1
EIAAB30506 Jagged and Delta protein,Jedi,Megf12,Mouse,mPEAR1,Multiple EGF-like domains protein 12,Multiple epidermal growth factor-like domains protein 12,Mus musculus,Pear1,Platelet endothelial aggregation rece
EIAAB31153 Homo sapiens,Human,Liver-related putative tumor suppressor,LPTL,LPTS,PIN2_TERF1-interacting telomerase inhibitor 1,Pin2-interacting protein X1,PINX1,Protein 67-11-3,TRF1-interacting protein 1
25-807 INADL is a protein with multiple PDZ domains. PDZ domains mediate protein-protein interactions, and proteins with multiple PDZ domains often organize multimeric complexes at the plasma membrane. This 0.05 mg
EIAAB38673 Homo sapiens,Human,KIAA0814,MEGF5,Multiple EGF-like domains protein 5,Multiple epidermal growth factor-like domains protein 5,SLIL2,Slit homolog 3 protein,SLIT3,Slit-3,UNQ691_PRO1336
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


 

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