GSLG1_RAT
ID GSLG1_RAT Reviewed; 1171 AA.
AC Q62638;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Golgi apparatus protein 1;
DE AltName: Full=E-selectin ligand 1;
DE Short=ESL-1;
DE AltName: Full=Golgi sialoglycoprotein MG-160 {ECO:0000303|PubMed:2909545};
DE Flags: Precursor;
GN Name=Glg1; Synonyms=Esl1, Mg160 {ECO:0000303|PubMed:2909545};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 90-103; 174-189;
RP 225-241; 494-508; 538-547; 687-700; 993-1010 AND 1104-1115.
RC STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
RX PubMed=7768993; DOI=10.1242/jcs.108.2.457;
RA Gonatas J.O., Mourelatos Z., Stieber A., Lane W.S., Brosius J.,
RA Gonatas N.K.;
RT "MG-160, a membrane sialoglycoprotein of the medial cisternae of the rat
RT Golgi apparatus, binds basic fibroblast growth factor and exhibits a high
RT level of sequence identity to a chicken fibroblast growth factor
RT receptor.";
RL J. Cell Sci. 108:457-467(1995).
RN [2]
RP GLYCOSYLATION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=2909545; DOI=10.1016/s0021-9258(17)31310-8;
RA Gonatas J.O., Mezitis S.G.E., Stieber A., Fleischer B., Gonatas N.K.;
RT "MG-160. A novel sialoglycoprotein of the medial cisternae of the Golgi
RT apparatus.";
RL J. Biol. Chem. 264:646-653(1989).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=31522887; DOI=10.1016/j.cell.2019.08.025;
RA Fu M.M., McAlear T.S., Nguyen H., Oses-Prieto J.A., Valenzuela A.,
RA Shi R.D., Perrino J.J., Huang T.T., Burlingame A.L., Bechstedt S.,
RA Barres B.A.;
RT "The Golgi outpost protein TPPP nucleates microtubules and is critical for
RT myelination.";
RL Cell 0:0-0(2019).
CC -!- FUNCTION: Binds fibroblast growth factor and E-selectin (cell-adhesion
CC lectin on endothelial cells mediating the binding of neutrophils).
CC {ECO:0000250|UniProtKB:Q92896}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:2909545}; Single-pass type I membrane protein
CC {ECO:0000255}. Golgi outpost {ECO:0000269|PubMed:31522887}. Cytoplasm,
CC cytoskeleton, microtubule organizing center
CC {ECO:0000269|PubMed:31522887}. Note=Golgi medial cisternae
CC (PubMed:2909545). Localizes to the postsynaptic Golgi apparatus region,
CC also named Golgi outpost, which shapes dendrite morphology by
CC functioning as sites of acentrosomal microtubule nucleation
CC (PubMed:31522887). {ECO:0000269|PubMed:2909545,
CC ECO:0000269|PubMed:31522887}.
CC -!- TISSUE SPECIFICITY: Widely expressed; found in kidney, pancreatic
CC islets, parathyroid, thyroid, adrenal tissue, brain neurons,
CC astrocytes, adenohypophysis, cultured pheochromocytoma cells.
CC {ECO:0000269|PubMed:2909545}.
CC -!- PTM: Fucosylation is essential for binding to E-selectin.
CC {ECO:0000250|UniProtKB:Q61543}.
CC -!- PTM: N-glycosylated. Contains sialic acid residues.
CC {ECO:0000269|PubMed:2909545}.
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DR EMBL; U08136; AAB03365.1; -; mRNA.
DR RefSeq; NP_058907.1; NM_017211.2.
DR AlphaFoldDB; Q62638; -.
DR BioGRID; 248118; 2.
DR IntAct; Q62638; 1.
DR STRING; 10116.ENSRNOP00000025570; -.
DR CarbonylDB; Q62638; -.
DR GlyGen; Q62638; 5 sites.
DR iPTMnet; Q62638; -.
DR PhosphoSitePlus; Q62638; -.
DR SwissPalm; Q62638; -.
DR jPOST; Q62638; -.
DR PaxDb; Q62638; -.
DR PRIDE; Q62638; -.
DR GeneID; 29476; -.
DR KEGG; rno:29476; -.
DR UCSC; RGD:69345; rat.
DR CTD; 2734; -.
DR RGD; 69345; Glg1.
DR eggNOG; KOG3648; Eukaryota.
DR InParanoid; Q62638; -.
DR OrthoDB; 189325at2759; -.
DR PhylomeDB; Q62638; -.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR PRO; PR:Q62638; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0017134; F:fibroblast growth factor binding; IDA:RGD.
DR GO; GO:0060349; P:bone morphogenesis; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; NAS:RGD.
DR GO; GO:0010955; P:negative regulation of protein processing; ISO:RGD.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; ISO:RGD.
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 Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycoprotein;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Sialic acid; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..1171
FT /note="Golgi apparatus protein 1"
FT /id="PRO_0000011122"
FT TOPO_DOM 33..1137
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1138..1158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1159..1171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 108..141
FT /note="Cys-rich GLG1 1"
FT REPEAT 142..204
FT /note="Cys-rich GLG1 2"
FT REPEAT 207..270
FT /note="Cys-rich GLG1 3"
FT REPEAT 278..338
FT /note="Cys-rich GLG1 4"
FT REPEAT 339..405
FT /note="Cys-rich GLG1 5"
FT REPEAT 406..465
FT /note="Cys-rich GLG1 6"
FT REPEAT 467..529
FT /note="Cys-rich GLG1 7"
FT REPEAT 530..596
FT /note="Cys-rich GLG1 8"
FT REPEAT 601..660
FT /note="Cys-rich GLG1 9"
FT REPEAT 662..720
FT /note="Cys-rich GLG1 10"
FT REPEAT 721..780
FT /note="Cys-rich GLG1 11"
FT REPEAT 788..848
FT /note="Cys-rich GLG1 12"
FT REPEAT 850..903
FT /note="Cys-rich GLG1 13"
FT REPEAT 904..971
FT /note="Cys-rich GLG1 14"
FT REPEAT 972..1027
FT /note="Cys-rich GLG1 15"
FT REPEAT 1033..1093
FT /note="Cys-rich GLG1 16"
FT REGION 43..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61543"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1171 AA; 133557 MW; CDD9D34D109E272F CRC64;
MAVCGRVRRM FRLSAALQLL LLVAAGVQNS HGQGQGLGVN FGPFAGQAGG GNPVGQQPPQ
LPQLSQQQQQ QQPPPQQQQP FPAGGLPARR GGAGPGGTGG GWKLAEEESC REDVTRVCPK
HTWSNNLAVL ECLQDVREPE NEISSDCNHL LWNYKLNLTT DPKFESVARE VCKSTISEIK
ECAEEPVGKG YMVSCLVDHR GNITEYQCHQ YITKMTAIIF SDYRLICGFM DDCKNDINLL
KCGSIRLGEK DAHSQGEVVS CLEKGLVKEA EEKEPKIQVS ELCKKAILRV AELSSDDFHL
DRHLYFACRD DRERFCENTQ AGEGRVYKCL FNHKFEESMS EKCREALTTR QKLIAQDYKV
SYSLAKSCKS DLKKYRCNVE NLPRSREARL SYLLMCLESA VHRGRQVSSE CQGEMLDYRR
MLMEDFSLSP EIILSCRGEI EHHCSGLHRK GRTLHCLMKV VRGEKGSLGM NCQQALQTLI
QETDPGADYR IDRALNEACE SVIQTACKHI RSGDPMILSC LMEHLYTEKM VEDCEHRLLE
LQYFISRDWK LDPVLYRKCQ GDASRLCHTH GWNETSELMP PGAVFSCLYR HAYRTEEQGR
RLSRECRAEV QRILHQRAMD VKLDPALQDK CLIDLGKWCS EKTETGQELE CLQDHLDDLA
VECRDIVGNL TELESEDIQI EALLMRACEP IIHNFCHDVA DNQIDSGDLM ECLIQNKHQK
DMNEKCAIGV THFQLVQMKD FRFSYKFKMA CKEDVLKLCP NIKKKVDVVI CLSTTVRNDT
LQEAKEHRVS LKCRKQLRVE ELEMTEDIRL EPDLYEACKS DIKNYCSTVQ YGNAQIIECL
KENKKQLSTR CHQRVFKLQE TEMMDPELDY TLMRVCKQMI KRFCPEADSK TMLQCLKQNK
NSELMDPKCK QMITKRQITQ NTDYRLNPVL RKACKADIPK FCHGILTKAK DDSELEGQVI
SCLKLRYADQ RLSSDCEDQI RIITQESALD YRLDPQLQLH CSDEIANLCA EEAAAQEQTG
QVEECLKVNL LKIRTELCKK EVLNMLKESK ADIFVDPVLH TACALDIKHH CAAITPGRGR
QMSCLMEALE DKRVRLQPEC KKRLNDRIEM WSYAAKVAPA DGFSDLAMQV MTSPSKNYIL
SVISGSICIL FLIGLMCGRI TKRVTRELKD R
