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Golgi apparatus protein 1 (E-selectin ligand 1) (ESL-1) (Selel) (Golgi sialoglycoprotein MG-160)

 GSLG1_MOUSE             Reviewed;        1175 AA.
Q61543; Q9QZ40;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-MAY-2017, entry version 145.
RecName: Full=Golgi apparatus protein 1;
AltName: Full=E-selectin ligand 1;
Short=ESL-1;
Short=Selel;
AltName: Full=Golgi sialoglycoprotein MG-160;
Flags: Precursor;
Name=Glg1; Synonyms=Esl1, Mg160, Selel;
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], AND PROTEIN SEQUENCE OF 255-266; 357-363;
636-641 AND 744-750.
TISSUE=Neutrophil;
PubMed=7531823; DOI=10.1038/373615a0;
Steegmaier M., Levinovitz A., Isenmann S., Borges E., Lenter M.,
Kocher H.P., Kleuser B., Vestweber D.;
"The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast
growth factor.";
Nature 373:615-620(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
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).
[3]
NUCLEOTIDE SEQUENCE OF 1-138.
STRAIN=129/Sv; TISSUE=Embryonic stem cell;
PubMed=10556428; DOI=10.1007/s003359901166;
Willmroth F., Beaudet A.L.;
"Structure of the murine E-selectin ligand 1 (ESL-1) gene and
assignment to chromosome 8.";
Mamm. Genome 10:1085-1088(1999).
[4]
SUBCELLULAR LOCATION.
PubMed=9099943;
Steegmaier M., Borges E., Berger J., Schwarz H., Vestweber D.;
"The E-selectin-ligand ESL-1 is located in the Golgi as well as on
microvilli on the cell surface.";
J. Cell Sci. 110:687-694(1997).
[5]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-161 AND ASN-673.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, 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).
-!- FUNCTION: Binds fibroblast growth factor (By similarity). Binds E-
selectin (cell-adhesion lectin on endothelial cells mediating the
binding of neutrophils). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9099943};
Single-pass type I membrane protein {ECO:0000269|PubMed:9099943}.
Golgi apparatus membrane {ECO:0000269|PubMed:9099943}; Single-pass
type I membrane protein {ECO:0000269|PubMed:9099943}. Note=Golgi
and microvilli on the cell surface.
-!- TISSUE SPECIFICITY: Widely expressed; found in myeloid cells,
fibroblasts, colon carcinoma, endothelioma, teratocarcinoma,
lymphoma, myeloma.
-!- PTM: Fucosylation is essential for binding to E-selectin.
-!- PTM: Contains sialic acid residues. {ECO:0000250}.
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EMBL; X84037; CAA58855.1; -; mRNA.
EMBL; BC021306; AAH21306.1; -; mRNA.
EMBL; Y12462; CAA73066.1; -; Genomic_DNA.
CCDS; CCDS22671.1; -.
PIR; S52417; S52417.
RefSeq; NP_033175.1; NM_009149.2.
UniGene; Mm.276271; -.
UniGene; Mm.440619; -.
ProteinModelPortal; Q61543; -.
SMR; Q61543; -.
DIP; DIP-59329N; -.
IntAct; Q61543; 3.
MINT; MINT-1836383; -.
STRING; 10090.ENSMUSP00000131355; -.
iPTMnet; Q61543; -.
PhosphoSitePlus; Q61543; -.
SwissPalm; Q61543; -.
EPD; Q61543; -.
MaxQB; Q61543; -.
PaxDb; Q61543; -.
PRIDE; Q61543; -.
Ensembl; ENSMUST00000169020; ENSMUSP00000131355; ENSMUSG00000003316.
GeneID; 20340; -.
KEGG; mmu:20340; -.
UCSC; uc009nma.1; mouse.
CTD; 2734; -.
MGI; MGI:104967; Glg1.
eggNOG; KOG3648; Eukaryota.
eggNOG; ENOG410XNWV; LUCA.
GeneTree; ENSGT00390000011262; -.
HOGENOM; HOG000047635; -.
HOVERGEN; HBG051850; -.
InParanoid; Q61543; -.
KO; K06816; -.
OMA; NCQQALQ; -.
OrthoDB; EOG091G01KP; -.
PhylomeDB; Q61543; -.
TreeFam; TF106112; -.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
ChiTaRS; Glg1; mouse.
PRO; PR:Q61543; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000003316; -.
CleanEx; MM_GLG1; -.
ExpressionAtlas; Q61543; baseline and differential.
Genevisible; Q61543; MM.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0017134; F:fibroblast growth factor binding; IBA:GO_Central.
GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
GO; GO:0010955; P:negative regulation of protein processing; IMP:MGI.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
GO; GO:0032330; P:regulation of chondrocyte differentiation; IMP:MGI.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR001893; Cys-rich_GLG1_repeat.
InterPro; IPR017873; Cys-rich_GLG1_repeat_euk.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
Pfam; PF00839; Cys_rich_FGFR; 15.
PROSITE; PS51289; GLG1_C_RICH; 16.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Glycoprotein; Golgi apparatus; Membrane; Phosphoprotein;
Reference proteome; Repeat; Sialic acid; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 1175 Golgi apparatus protein 1.
/FTId=PRO_0000011121.
TOPO_DOM 28 1141 Extracellular. {ECO:0000255}.
TRANSMEM 1142 1162 Helical. {ECO:0000255}.
TOPO_DOM 1163 1175 Cytoplasmic. {ECO:0000255}.
REPEAT 112 145 Cys-rich GLG1 1.
REPEAT 146 208 Cys-rich GLG1 2.
REPEAT 211 274 Cys-rich GLG1 3.
REPEAT 282 342 Cys-rich GLG1 4.
REPEAT 343 409 Cys-rich GLG1 5.
REPEAT 410 469 Cys-rich GLG1 6.
REPEAT 471 533 Cys-rich GLG1 7.
REPEAT 534 600 Cys-rich GLG1 8.
REPEAT 605 664 Cys-rich GLG1 9.
REPEAT 666 724 Cys-rich GLG1 10.
REPEAT 725 784 Cys-rich GLG1 11.
REPEAT 792 852 Cys-rich GLG1 12.
REPEAT 854 907 Cys-rich GLG1 13.
REPEAT 908 975 Cys-rich GLG1 14.
REPEAT 976 1031 Cys-rich GLG1 15.
REPEAT 1037 1097 Cys-rich GLG1 16.
COMPBIAS 46 51 Poly-Gly.
COMPBIAS 66 70 Poly-Gln.
COMPBIAS 74 82 Poly-Gln.
MOD_RES 957 957 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 577 577 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 673 673 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 782 782 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 1175 AA; 133734 MW; 105835DD38C7338B CRC64;
MAVCGRVRGM FRLSAALPLL LLAAAGAQNG HGQGQGPGTN FGPFPGQGGG GSPAGQQPPQ
QPQLSQQQQQ PPPQQQQQQQ QQSLFAAGGL PARRGGAGPG GTGGGWKLAE EESCREDVTR
VCPKHTWSNN LAVLECLQDV REPENEISSD CNHLLWNYKL NLTTDPKFES VAREVCKSTI
SEIKECAEEP VGKGYMVSCL VDHRGNITEY QCHQYITKMT AIIFSDYRLI CGFMDDCKND
INLLKCGSIR LGEKDAHSQG EVVSCLEKGL VKEAEEKEPK IQVSELCKKA ILRVAELSSD
DFHLDRHLYF ACRDDRERFC ENTQAGEGRV YKCLFNHKFE ESMSEKCREA LTTRQKLIAQ
DYKVSYSLAK SCKSDLKKYR CNVENLPRSR EARLSYLLMC LESAVHRGRQ VSSECQGEML
DYRRMLMEDF SLSPEIILSC RGEIEHHCSG LHRKGRTLHC LMKVVRGEKG NLGMNCQQAL
QTLIQETDPG ADYRIDRALN EACESVIQTA CKHIRSGDPM ILSCLMEHLY TEKMVEDCEH
RLLELQYFIS RDWKLDPVLY RKCQGDASRL CHTHGWNETS ELMPPGAVFS CLYRHAYRTE
EQGRRLSREC RAEVQRILHQ RAMDVKLDPA LQDKCLIDLG KWCSEKTETG QELECLQDHL
DDLAVECRDI VGNLTELESE DIQIEALLMR ACEPIIQNFC HDVADNQIDS GDLMECLIQN
KHQKDMNEKC AIGVTHFQLV QMKDFRFSYK FKMACKEDVL KLCPNIKKKV DVVICLSTTV
RNDTLQEAKE HRVSLKCRKQ LRVEELEMTE DIRLEPDLYE ACKSDIKNYC STVQYGNAQI
IECLKENKKQ LSTRCHQKVF KLQETEMMDP ELDYTLMRVC KQMIKRFCPE ADSKTMLQCL
KQNKNSELMD PKCKQMITKR QITQNTDYRL NPVLRKACKA DIPKFCHGIL TKAKDDSELE
GQVISCLKLR YADQRLSSDC EDQIRIIIQE SALDYRLDPQ LQLHCSDEIA NLCAEEAAAQ
EQTGQVEECL KVNLLKIKTE LCKKEVLNML KESKADIFVD PVLHTACALD IKHHCAAITP
GRGRQMSCLM EALEDKRVRL QPECKKRLND RIEMWSYAAK VAPADGFSDL AMQVMTSPSK
NYILSVISGS ICILFLIGLM CGRITKRVTR ELKDR


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