GSLG1_CHICK
ID GSLG1_CHICK Reviewed; 1142 AA.
AC Q02391; Q91019;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Golgi apparatus protein 1;
DE AltName: Full=Cysteine-rich fibroblast growth factor receptor;
DE Flags: Precursor;
GN Name=GLG1; Synonyms=CFR;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Embryonic brain;
RX PubMed=1448090; DOI=10.1128/mcb.12.12.5600-5609.1992;
RA Burrus L.W., Zuber M.E., Lueddecke B.A., Olwin B.B.;
RT "Identification of a cysteine-rich receptor for fibroblast growth
RT factors.";
RL Mol. Cell. Biol. 12:5600-5609(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 1042-CYS--ARG-1142.
RX PubMed=9066777;
RX DOI=10.1002/(sici)1097-4652(199703)170:3<217::aid-jcp1>3.0.co;2-r;
RA Zuber M.E., Zhou Z., Burrus L.W., Olwin B.B.;
RT "Cysteine-rich FGF receptor regulates intracellular FGF-1 and FGF-2
RT levels.";
RL J. Cell. Physiol. 170:217-227(1997).
RN [3]
RP GLYCOSYLATION.
RX PubMed=2553717; DOI=10.1016/s0021-9258(18)51516-7;
RA Burrus L.W., Olwin B.B.;
RT "Isolation of a receptor for acidic and basic fibroblast growth factor from
RT embryonic chick.";
RL J. Biol. Chem. 264:18647-18653(1989).
CC -!- FUNCTION: Binds fibroblast growth factor and E-selectin (cell-adhesion
CC lectin on endothelial cells mediating the binding of neutrophils) (By
CC similarity). Binds fibroblast growth factor (FGF). May be involved in
CC intracellular FGF trafficking and the regulation of cellular responses
CC to FGFS (PubMed:1448090). {ECO:0000250|UniProtKB:Q92896,
CC ECO:0000269|PubMed:1448090}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:9066777}; 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:0000269|PubMed:2553717}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M95766; AAA48769.1; -; mRNA.
DR EMBL; U48395; AAB39211.1; -; mRNA.
DR PIR; A45031; A45031.
DR RefSeq; NP_990827.1; NM_205496.1.
DR AlphaFoldDB; Q02391; -.
DR BioGRID; 676739; 1.
DR STRING; 9031.ENSGALP00000004317; -.
DR PaxDb; Q02391; -.
DR PRIDE; Q02391; -.
DR GeneID; 396492; -.
DR KEGG; gga:396492; -.
DR CTD; 2734; -.
DR VEuPathDB; HostDB:geneid_396492; -.
DR eggNOG; KOG3648; Eukaryota.
DR InParanoid; Q02391; -.
DR OrthoDB; 189325at2759; -.
DR PhylomeDB; Q02391; -.
DR PRO; PR:Q02391; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017134; F:fibroblast growth factor binding; IBA:GO_Central.
DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR GO; GO:0010955; P:negative regulation of protein processing; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Repeat; Sialic acid; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1142
FT /note="Golgi apparatus protein 1"
FT /id="PRO_0000011123"
FT TOPO_DOM 30..1108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1109..1129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1130..1142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 81..112
FT /note="Cys-rich GLG1 1"
FT REPEAT 113..175
FT /note="Cys-rich GLG1 2"
FT REPEAT 178..241
FT /note="Cys-rich GLG1 3"
FT REPEAT 249..309
FT /note="Cys-rich GLG1 4"
FT REPEAT 310..376
FT /note="Cys-rich GLG1 5"
FT REPEAT 377..436
FT /note="Cys-rich GLG1 6"
FT REPEAT 438..500
FT /note="Cys-rich GLG1 7"
FT REPEAT 501..567
FT /note="Cys-rich GLG1 8"
FT REPEAT 572..631
FT /note="Cys-rich GLG1 9"
FT REPEAT 633..691
FT /note="Cys-rich GLG1 10"
FT REPEAT 692..751
FT /note="Cys-rich GLG1 11"
FT REPEAT 759..819
FT /note="Cys-rich GLG1 12"
FT REPEAT 821..874
FT /note="Cys-rich GLG1 13"
FT REPEAT 875..942
FT /note="Cys-rich GLG1 14"
FT REPEAT 943..998
FT /note="Cys-rich GLG1 15"
FT REPEAT 1004..1064
FT /note="Cys-rich GLG1 16"
FT REGION 45..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 1042..1142
FT /note="CAAIPPGRGRQMSCLMEALEDKRVRLQPECKKRLNDRIEMWSYAAKVAPAEG
FT FSDLAMQVMTSPSKNYILSVITVGICVLFLIGLMCGRITKRVTRELKDR->IVLKCGAM
FT LQRLPQRKASLTLPCKLRPLRPRITYCL: In CHO.MUTCFR mutant; unable
FT to regulate FGF levels and is detected throughout the
FT cell."
FT /evidence="ECO:0000269|PubMed:9066777"
SQ SEQUENCE 1142 AA; 129711 MW; 91CC9BE8D53CABB8 CRC64;
MAPCGRVRSR CPGPALLLLL ALAARPALAG PPAAALQAGP GLNAAGQPAQ GAAPGAAGPR
GARGGGGGSG GGWKLSEEAV CREDVVRLCS KHSWANNLAV LECLQDVREP DNEISSDCNH
LLWNYKLNLT TDPKFESVAR EVCKSTIAEI KECADEPVGK GFLVSCLVDH RGNITEYQCH
QYITKMTAII FSDYRLICGF MDDCKADINL LKCGSIRPGE KDAHSQGEVV ACLEKGLVKE
AEENDPRVQV SDQCKKAILR VAELSSDDFH LDRHLYFACR DDRERFCENT QAGEGRVYKC
LFNHKFEESM SEKCRDALTT RQKLIAQDYK VSYSLAKSCK SDLKKYRCNV ENLPRSREAR
LSYLLMCLES AVHRGRQVSS ECQGEMLDYR RMLMEDFSLS PEIILSCRGE IEHHCSGLHR
KGRTLHCLMK VVRGEKGNVG LNCQQALQTL IQETDPGADY RIDRALNEAC ESVIQTACKH
IRSGDPMILS CLMEHLYTEK MVEDCEHRLL ELQYFISRDW KLDVVLYRKC QGDASRLCHT
HGWNETSELM PPGAVFSCLY RHAYRTEEQG RRLSRECRAE VQRILHQRAM DVKLDPALQD
KCMIDLGKWC SEKTETGQEL ECLQDHLDDL VSDCRDIVGN LTELESEDIQ IEALLMRACE
PIIQTFCHEV ADNQIDSGDL MECLIQNKHQ KEMNEKCAIG VTHFQLVQMK DFRFSYKFKM
ACKEDVLKLC PNIKKKVDVV ICLSTTVRND TLQDAKEHRV SLKCRKQLRV EELEMTEDIR
LEPELYEACK SDIKNYCQNV PYGNAQIIEC LKEIKKQLST RCHQKVFKLQ ETEMMDPELD
YTLMRVCKQM IKRFCPEADS KNMLQCLKQN KNSEVMDPKC KQMITKRQIT QNTDYRLNPV
LRKACKADIP KFCQNILNRA KDDTELEGQV ISCLKLKYAD QRLSPDCEDQ IRVIIQESAL
DYRLDPQLQM HCSEEISSLC AEEAAAQEQT GQVEECLKVN LLKIKTEMCK KEVLNMLKES
KADIFVDPVL HTACALDIKH HCAAIPPGRG RQMSCLMEAL EDKRVRLQPE CKKRLNDRIE
MWSYAAKVAP AEGFSDLAMQ VMTSPSKNYI LSVITVGICV LFLIGLMCGR ITKRVTRELK
DR
