GSLG1_MOUSE
ID GSLG1_MOUSE Reviewed; 1175 AA.
AC Q61543; Q9QZ40;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Golgi apparatus protein 1;
DE AltName: Full=E-selectin ligand 1 {ECO:0000303|PubMed:7531823};
DE Short=ESL-1 {ECO:0000303|PubMed:7531823};
DE Short=Selel;
DE AltName: Full=Golgi sialoglycoprotein MG-160;
DE Flags: Precursor;
GN Name=Glg1; Synonyms=Esl1, Mg160, Selel;
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 [MRNA], FUNCTION, GLYCOSYLATION, AND PROTEIN SEQUENCE
RP OF 255-266; 357-363; 636-641 AND 744-750.
RC TISSUE=Neutrophil;
RX PubMed=7531823; DOI=10.1038/373615a0;
RA Steegmaier M., Levinovitz A., Isenmann S., Borges E., Lenter M.,
RA Kocher H.P., Kleuser B., Vestweber D.;
RT "The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast
RT growth factor.";
RL Nature 373:615-620(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-138.
RC STRAIN=129/Sv; TISSUE=Embryonic stem cell;
RX PubMed=10556428; DOI=10.1007/s003359901166;
RA Willmroth F., Beaudet A.L.;
RT "Structure of the murine E-selectin ligand 1 (ESL-1) gene and assignment to
RT chromosome 8.";
RL Mamm. Genome 10:1085-1088(1999).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9099943; DOI=10.1242/jcs.110.6.687;
RA Steegmaier M., Borges E., Berger J., Schwarz H., Vestweber D.;
RT "The E-selectin-ligand ESL-1 is located in the Golgi as well as on
RT microvilli on the cell surface.";
RL J. Cell Sci. 110:687-694(1997).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-161 AND ASN-673.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-957, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Binds fibroblast growth factor and E-selectin (cell-adhesion
CC lectin on endothelial cells mediating the binding of neutrophils).
CC {ECO:0000269|PubMed:7531823}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9099943};
CC Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:9099943}; Single-pass type I membrane
CC protein {ECO:0000255}. Golgi outpost {ECO:0000250|UniProtKB:Q62638}.
CC Cytoplasm, cytoskeleton, microtubule organizing center
CC {ECO:0000250|UniProtKB:Q62638}. Note=Golgi and microvilli on the cell
CC surface (PubMed:9099943). Localizes to the postsynaptic Golgi apparatus
CC region, also named Golgi outpost, which shapes dendrite morphology by
CC functioning as sites of acentrosomal microtubule nucleation (By
CC similarity). {ECO:0000250|UniProtKB:Q62638,
CC ECO:0000269|PubMed:9099943}.
CC -!- TISSUE SPECIFICITY: Widely expressed; found in myeloid cells,
CC fibroblasts, colon carcinoma, endothelioma, teratocarcinoma, lymphoma,
CC myeloma.
CC -!- PTM: Fucosylation is essential for binding to E-selectin.
CC {ECO:0000269|PubMed:7531823}.
CC -!- PTM: Contains sialic acid residues. {ECO:0000250|UniProtKB:Q62638}.
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DR EMBL; X84037; CAA58855.1; -; mRNA.
DR EMBL; BC021306; AAH21306.1; -; mRNA.
DR EMBL; Y12462; CAA73066.1; -; Genomic_DNA.
DR CCDS; CCDS22671.1; -.
DR PIR; S52417; S52417.
DR RefSeq; NP_033175.1; NM_009149.2.
DR AlphaFoldDB; Q61543; -.
DR BioGRID; 203155; 17.
DR DIP; DIP-59329N; -.
DR IntAct; Q61543; 1.
DR STRING; 10090.ENSMUSP00000131355; -.
DR GlyConnect; 2358; 1 N-Linked glycan (1 site).
DR GlyGen; Q61543; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q61543; -.
DR PhosphoSitePlus; Q61543; -.
DR SwissPalm; Q61543; -.
DR EPD; Q61543; -.
DR jPOST; Q61543; -.
DR MaxQB; Q61543; -.
DR PaxDb; Q61543; -.
DR PRIDE; Q61543; -.
DR ProteomicsDB; 271473; -.
DR Antibodypedia; 2273; 320 antibodies from 27 providers.
DR DNASU; 20340; -.
DR Ensembl; ENSMUST00000169020; ENSMUSP00000131355; ENSMUSG00000003316.
DR GeneID; 20340; -.
DR KEGG; mmu:20340; -.
DR UCSC; uc009nma.1; mouse.
DR CTD; 2734; -.
DR MGI; MGI:104967; Glg1.
DR VEuPathDB; HostDB:ENSMUSG00000003316; -.
DR eggNOG; KOG3648; Eukaryota.
DR GeneTree; ENSGT00390000011262; -.
DR InParanoid; Q61543; -.
DR OMA; FTYKFKE; -.
DR OrthoDB; 189325at2759; -.
DR PhylomeDB; Q61543; -.
DR TreeFam; TF106112; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 20340; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Glg1; mouse.
DR PRO; PR:Q61543; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61543; protein.
DR Bgee; ENSMUSG00000003316; Expressed in secondary palatal shelf and 267 other tissues.
DR ExpressionAtlas; Q61543; baseline and differential.
DR Genevisible; Q61543; MM.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005797; C:Golgi medial cisterna; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISO:MGI.
DR GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR GO; GO:0010955; P:negative regulation of protein processing; IMP:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IMP:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR InterPro; IPR001893; Cys-rich_GLG1_repeat.
DR InterPro; IPR017873; Cys-rich_GLG1_repeat_euk.
DR InterPro; IPR039728; GLG1.
DR PANTHER; PTHR11884; PTHR11884; 1.
DR Pfam; PF00839; Cys_rich_FGFR; 15.
DR PROSITE; PS51289; GLG1_C_RICH; 16.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Glycoprotein; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Sialic acid; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1175
FT /note="Golgi apparatus protein 1"
FT /id="PRO_0000011121"
FT TOPO_DOM 28..1141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1142..1162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1163..1175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 112..145
FT /note="Cys-rich GLG1 1"
FT REPEAT 146..208
FT /note="Cys-rich GLG1 2"
FT REPEAT 211..274
FT /note="Cys-rich GLG1 3"
FT REPEAT 282..342
FT /note="Cys-rich GLG1 4"
FT REPEAT 343..409
FT /note="Cys-rich GLG1 5"
FT REPEAT 410..469
FT /note="Cys-rich GLG1 6"
FT REPEAT 471..533
FT /note="Cys-rich GLG1 7"
FT REPEAT 534..600
FT /note="Cys-rich GLG1 8"
FT REPEAT 605..664
FT /note="Cys-rich GLG1 9"
FT REPEAT 666..724
FT /note="Cys-rich GLG1 10"
FT REPEAT 725..784
FT /note="Cys-rich GLG1 11"
FT REPEAT 792..852
FT /note="Cys-rich GLG1 12"
FT REPEAT 854..907
FT /note="Cys-rich GLG1 13"
FT REPEAT 908..975
FT /note="Cys-rich GLG1 14"
FT REPEAT 976..1031
FT /note="Cys-rich GLG1 15"
FT REPEAT 1037..1097
FT /note="Cys-rich GLG1 16"
FT REGION 30..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 957
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 673
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ 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
