GSLG1_CRIGR
ID GSLG1_CRIGR Reviewed; 1160 AA.
AC Q9Z1E9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 93.
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;
DE AltName: Full=Latent TGF-beta complexed protein 1;
DE Short=LTCP-1;
DE Flags: Precursor;
GN Name=GLG1; Synonyms=ESL1, MG160;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 80-87; 180-201;
RP 215-223; 240-252; 266-273; 342-348; 442-448; 527-536; 632-645; 847-858;
RP 930-937 AND 961-977.
RC TISSUE=Ovary;
RX PubMed=9182700; DOI=10.1042/bj3240427;
RA Olofsson A., Hellman U., Ten Dijke P., Grimsby S., Ichijo H., Moren A.,
RA Miyazono K., Heldin C.-H.;
RT "Latent transforming growth factor-beta complex in Chinese hamster ovary
RT cells contains the multifunctional cysteine-rich fibroblast growth factor
RT receptor, also termed E-selectin-ligand or MG-160.";
RL Biochem. J. 324:427-434(1997).
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:0000250|UniProtKB:Q62638}; Single-pass type I membrane protein
CC {ECO:0000255}. Golgi outpost {ECO:0000250|UniProtKB:Q62638}. Cytoplasm,
CC cytoskeleton, microtubule organizing center
CC {ECO:0000250|UniProtKB:Q62638}. Note=Golgi medial cisternae. Localizes
CC to the postsynaptic Golgi apparatus region, also named Golgi outpost,
CC which shapes dendrite morphology by functioning as sites of
CC acentrosomal microtubule nucleation. {ECO:0000250|UniProtKB:Q62638}.
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:0000250|UniProtKB:Q62638}.
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DR EMBL; U51162; AAD00079.1; -; mRNA.
DR RefSeq; NP_001231202.1; NM_001244273.1.
DR AlphaFoldDB; Q9Z1E9; -.
DR SMR; Q9Z1E9; -.
DR STRING; 10029.NP_001231202.1; -.
DR GeneID; 100689240; -.
DR KEGG; cge:100689240; -.
DR CTD; 2734; -.
DR eggNOG; KOG3648; Eukaryota.
DR OrthoDB; 189325at2759; -.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Repeat; Sialic acid; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1160
FT /note="Golgi apparatus protein 1"
FT /id="PRO_0000011119"
FT TOPO_DOM 19..1126
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1127..1147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1148..1160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 97..130
FT /note="Cys-rich GLG1 1"
FT REPEAT 131..193
FT /note="Cys-rich GLG1 2"
FT REPEAT 196..259
FT /note="Cys-rich GLG1 3"
FT REPEAT 267..327
FT /note="Cys-rich GLG1 4"
FT REPEAT 328..394
FT /note="Cys-rich GLG1 5"
FT REPEAT 395..454
FT /note="Cys-rich GLG1 6"
FT REPEAT 456..518
FT /note="Cys-rich GLG1 7"
FT REPEAT 519..585
FT /note="Cys-rich GLG1 8"
FT REPEAT 590..649
FT /note="Cys-rich GLG1 9"
FT REPEAT 651..709
FT /note="Cys-rich GLG1 10"
FT REPEAT 710..769
FT /note="Cys-rich GLG1 11"
FT REPEAT 777..837
FT /note="Cys-rich GLG1 12"
FT REPEAT 839..892
FT /note="Cys-rich GLG1 13"
FT REPEAT 893..960
FT /note="Cys-rich GLG1 14"
FT REPEAT 961..1016
FT /note="Cys-rich GLG1 15"
FT REPEAT 1022..1082
FT /note="Cys-rich GLG1 16"
FT REGION 52..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 942
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61543"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1160 AA; 132326 MW; 9D30E2D1DAAC03CB CRC64;
MFRLSAALQL LLLAATGAQN NHGQVQVPGA NIGPLLGQAE GGSPAGQQLL QLSQQQKQPP
QQQQQQQPAF PAGGPPARRG GAGPGGTGGG WKLAEEESCR EDVTRVCPKH TWSNNLAVLE
CLQDVREPEN EISSDCNHLL WNYKLNLTTD PKFESVAREV CKSTISEIKE CAEEPVGKGY
MVSCLVDHRG NITEYQCHQY ITKMTAIIFS DYRLICGFMD DCKNDINLLK CGSIRLGEKD
AHSQGEVVSC LEKGLVKEAE EKEPKIQVSE LCKKAILRVA ELSSDDFHLD RHLYFACRDD
RERFCENTQA GEGRVYKCLF NHKFEESMSE KCREALTTRQ KLIAQDYKVS YSLAKSCKSD
LKKYRCNVEN LPRSREARLS YLLMCLESAV HRGRQVSSEC QGEMLDYRRM LMEDFSLSPE
IILSCRGEIE HHCSGLHRKG RTLHCLMKVI RGEKGNLGMN CQQALQTLIQ ETDPGADYRI
DRALNEACES VIQTACKHIR SGDPMILSCL MEHLYTEKMV EDCEHRLLEL QYFISRDWKL
DPVLYRKCQG DASRLCHTHG WNETSELMPP GAVFSCLYRH AYRTEEQGRR LSRECRAEVQ
RILHQRAMDV KLDPALQDKC LIDLGKWCSE KTETGQELEC LQDHLDDLAV ECRDIVGNLT
ELESEDIQIE ALLMRACEPI IQNFCHDVAD NQIDSGDLME CLIQNKHQKD MNEKCAIGVT
HFQLVQMKDF RFSYKFKMAC KEDVLKLCPN IKKKVDVVIC LSTTVRNDTL QEAKEHRVSL
KCRKQLRVEE LEMTEDIRLE PDLYEACKSD IRGYCSTVQY GNAQIIECLK ENKKQLSTRC
HQKVFKLQET EMMDPELDYT LMRVCKQMIK RFCPEADSKT MLQCLKQNKN SELMDPKCKQ
MITKRQITQN TDYRLNPVLR KACKADIPKF CHGILTKAKD DSELEGQVIS CLKLRYADQR
LSSDCEDQIR IIIQESALDY RLDPQLQLHC SDEIANLCAE EAAAQEQTGQ VEECLKVNLL
KIRTELCKKE VLNMLKESKA DIFVDPVLHT ACALDIKHHC AAITPGRGRQ MSCLMEALED
KRVRLQPECK KRLNDRIEMW SYAAKVAPAD GFSDLAMQVM TSPSKNYILS VISGSICILF
LIGLMCGRIT KRVTRELKDR
