ID   GSLG1_HUMAN             Reviewed;        1179 AA.
AC   Q92896; B7Z8Y4; D3DUJ7; Q13221; Q6P9D1;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Golgi apparatus protein 1;
DE   AltName: Full=CFR-1;
DE   AltName: Full=Cysteine-rich fibroblast growth factor receptor;
DE   AltName: Full=E-selectin ligand 1;
DE            Short=ESL-1;
DE   AltName: Full=Golgi sialoglycoprotein MG-160;
DE   Flags: Precursor;
GN   Name=GLG1; Synonyms=CFR1, ESL1, MG160;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC   TISSUE=Fetal brain, and Lymphoblast;
RX   PubMed=8985126; DOI=10.1089/dna.1996.15.1121;
RA   Mourelatos Z., Gonatas J.O., Cinato E., Gonatas N.K.;
RT   "Cloning and sequence analysis of the human MG160, a fibroblast growth
RT   factor and E-selectin binding membrane sialoglycoprotein of the Golgi
RT   apparatus.";
RL   DNA Cell Biol. 15:1121-1128(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Wu M., Chen J., Tan Y.H., Hong W.J., Ting R.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=2355176; DOI=10.1177/38.7.2355176;
RA   Croul S., Mezitis S.G.E., Stieber A., Chen Y.J., Gonatas J.O., Goud B.,
RA   Gonatas N.K.;
RT   "Immunocytochemical visualization of the Golgi apparatus in several
RT   species, including human, and tissues with an antiserum against MG-160, a
RT   sialoglycoprotein of rat Golgi apparatus.";
RL   J. Histochem. Cytochem. 38:957-963(1990).
RN   [8]
RP   TISSUE SPECIFICITY.
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).
RN   [9]
RP   GLYCOSYLATION AT ASN-677.
RX   PubMed=12754519; DOI=10.1038/nbt827;
RA   Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT   "Identification and quantification of N-linked glycoproteins using
RT   hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL   Nat. Biotechnol. 21:660-666(2003).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1201 (ISOFORM 2),
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1190 (ISOFORM 3), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
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:8985126}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:2355176}; 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q92896-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92896-2; Sequence=VSP_035998;
CC       Name=3;
CC         IsoId=Q92896-3; Sequence=VSP_043472, VSP_035998;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highest levels in pancreas,
CC       skeletal muscle, placenta, heart, testis and ovary. Also found in the
CC       kidney, liver, lung and brain. {ECO:0000269|PubMed:9182700}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both in adult and fetal tissues.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB02178.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U64791; AAB06460.1; -; mRNA.
DR   EMBL; U28811; AAB02178.1; ALT_FRAME; mRNA.
DR   EMBL; AK304156; BAH14120.1; -; mRNA.
DR   EMBL; AC009053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC009153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC109599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471114; EAW95683.1; -; Genomic_DNA.
DR   EMBL; CH471114; EAW95682.1; -; Genomic_DNA.
DR   EMBL; CH471114; EAW95686.1; -; Genomic_DNA.
DR   EMBL; BC060822; AAH60822.1; -; mRNA.
DR   CCDS; CCDS32485.1; -. [Q92896-2]
DR   CCDS; CCDS45526.1; -. [Q92896-3]
DR   CCDS; CCDS45527.1; -. [Q92896-1]
DR   RefSeq; NP_001139138.1; NM_001145666.1. [Q92896-3]
DR   RefSeq; NP_001139139.1; NM_001145667.1. [Q92896-1]
DR   RefSeq; NP_036333.2; NM_012201.5. [Q92896-2]
DR   AlphaFoldDB; Q92896; -.
DR   SMR; Q92896; -.
DR   BioGRID; 108996; 129.
DR   CORUM; Q92896; -.
DR   DIP; DIP-27582N; -.
DR   IntAct; Q92896; 38.
DR   MINT; Q92896; -.
DR   STRING; 9606.ENSP00000205061; -.
DR   GlyConnect; 1280; 42 N-Linked glycans (4 sites).
DR   GlyCosmos; Q92896; 7 sites, 41 glycans.
DR   GlyGen; Q92896; 12 sites, 40 N-linked glycans (4 sites), 3 O-linked glycans (7 sites).
DR   iPTMnet; Q92896; -.
DR   MetOSite; Q92896; -.
DR   PhosphoSitePlus; Q92896; -.
DR   SwissPalm; Q92896; -.
DR   BioMuta; GLG1; -.
DR   DMDM; 218512060; -.
DR   EPD; Q92896; -.
DR   jPOST; Q92896; -.
DR   MassIVE; Q92896; -.
DR   MaxQB; Q92896; -.
DR   PaxDb; 9606-ENSP00000205061; -.
DR   PeptideAtlas; Q92896; -.
DR   ProteomicsDB; 75578; -. [Q92896-1]
DR   ProteomicsDB; 75579; -. [Q92896-2]
DR   ProteomicsDB; 75580; -. [Q92896-3]
DR   Pumba; Q92896; -.
DR   Antibodypedia; 2273; 377 antibodies from 27 providers.
DR   DNASU; 2734; -.
DR   Ensembl; ENST00000205061.9; ENSP00000205061.5; ENSG00000090863.12. [Q92896-2]
DR   Ensembl; ENST00000422840.7; ENSP00000405984.3; ENSG00000090863.12. [Q92896-1]
DR   Ensembl; ENST00000447066.6; ENSP00000406946.2; ENSG00000090863.12. [Q92896-3]
DR   GeneID; 2734; -.
DR   KEGG; hsa:2734; -.
DR   MANE-Select; ENST00000422840.7; ENSP00000405984.3; NM_001145667.2; NP_001139139.1.
DR   UCSC; uc002fcw.5; human. [Q92896-1]
DR   AGR; HGNC:4316; -.
DR   CTD; 2734; -.
DR   DisGeNET; 2734; -.
DR   GeneCards; GLG1; -.
DR   HGNC; HGNC:4316; GLG1.
DR   HPA; ENSG00000090863; Low tissue specificity.
DR   MIM; 600753; gene.
DR   neXtProt; NX_Q92896; -.
DR   OpenTargets; ENSG00000090863; -.
DR   PharmGKB; PA28719; -.
DR   VEuPathDB; HostDB:ENSG00000090863; -.
DR   eggNOG; KOG3648; Eukaryota.
DR   GeneTree; ENSGT00390000011262; -.
DR   HOGENOM; CLU_011063_0_0_1; -.
DR   InParanoid; Q92896; -.
DR   OMA; MECLIEH; -.
DR   OrthoDB; 311808at2759; -.
DR   PhylomeDB; Q92896; -.
DR   TreeFam; TF106112; -.
DR   PathwayCommons; Q92896; -.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   SignaLink; Q92896; -.
DR   BioGRID-ORCS; 2734; 18 hits in 1157 CRISPR screens.
DR   ChiTaRS; GLG1; human.
DR   GeneWiki; GLG1; -.
DR   GenomeRNAi; 2734; -.
DR   Pharos; Q92896; Tbio.
DR   PRO; PR:Q92896; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q92896; Protein.
DR   Bgee; ENSG00000090863; Expressed in stromal cell of endometrium and 222 other cell types or tissues.
DR   ExpressionAtlas; Q92896; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0017134; F:fibroblast growth factor binding; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
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:SF1; GOLGI APPARATUS PROTEIN 1; 1.
DR   PANTHER; PTHR11884; SELECTIN LIGAND RELATED; 1.
DR   Pfam; PF00839; Cys_rich_FGFR; 15.
DR   PROSITE; PS51289; GLG1_C_RICH; 16.
DR   Genevisible; Q92896; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Glycoprotein;
KW   Golgi apparatus; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Sialic acid; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..1179
FT                   /note="Golgi apparatus protein 1"
FT                   /id="PRO_0000011120"
FT   TOPO_DOM        30..1145
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1146..1166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1167..1179
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          116..149
FT                   /note="Cys-rich GLG1 1"
FT   REPEAT          150..212
FT                   /note="Cys-rich GLG1 2"
FT   REPEAT          215..278
FT                   /note="Cys-rich GLG1 3"
FT   REPEAT          286..346
FT                   /note="Cys-rich GLG1 4"
FT   REPEAT          347..413
FT                   /note="Cys-rich GLG1 5"
FT   REPEAT          414..473
FT                   /note="Cys-rich GLG1 6"
FT   REPEAT          475..537
FT                   /note="Cys-rich GLG1 7"
FT   REPEAT          538..604
FT                   /note="Cys-rich GLG1 8"
FT   REPEAT          609..668
FT                   /note="Cys-rich GLG1 9"
FT   REPEAT          670..728
FT                   /note="Cys-rich GLG1 10"
FT   REPEAT          729..788
FT                   /note="Cys-rich GLG1 11"
FT   REPEAT          796..856
FT                   /note="Cys-rich GLG1 12"
FT   REPEAT          858..911
FT                   /note="Cys-rich GLG1 13"
FT   REPEAT          912..979
FT                   /note="Cys-rich GLG1 14"
FT   REPEAT          980..1035
FT                   /note="Cys-rich GLG1 15"
FT   REPEAT          1041..1101
FT                   /note="Cys-rich GLG1 16"
FT   REGION          32..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         961
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61543"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        581
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        677
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:12754519"
FT   CARBOHYD        786
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         147..157
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043472"
FT   VAR_SEQ         1179
FT                   /note="R -> RLQYRSETMAYKGLVWSQDVTGSPA (in isoform 2 and
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035998"
FT   CONFLICT        33
FT                   /note="Q -> H (in Ref. 1; AAB06460)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="P -> L (in Ref. 1; AAB06460)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="P -> L (in Ref. 1; AAB06460)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        99
FT                   /note="Missing (in Ref. 2; AAB02178)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        526
FT                   /note="L -> S (in Ref. 2; AAB02178)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        702
FT                   /note="N -> T (in Ref. 2; AAB02178)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        707
FT                   /note="Missing (in Ref. 2; AAB02178)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1082
FT                   /note="I -> L (in Ref. 2; AAB02178)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q92896-2:1201
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         Q92896-3:1190
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
SQ   SEQUENCE   1179 AA;  134552 MW;  390F9923DC83C300 CRC64;
     MAACGRVRRM FRLSAALHLL LLFAAGAEKL PGQGVHSQGQ GPGANFVSFV GQAGGGGPAG
     QQLPQLPQSS QLQQQQQQQQ QQQQPQPPQP PFPAGGPPAR RGGAGAGGGW KLAEEESCRE
     DVTRVCPKHT WSNNLAVLEC LQDVREPENE ISSDCNHLLW NYKLNLTTDP KFESVAREVC
     KSTITEIKEC ADEPVGKGYM VSCLVDHRGN ITEYQCHQYI TKMTAIIFSD YRLICGFMDD
     CKNDINILKC GSIRLGEKDA HSQGEVVSCL EKGLVKEAEE REPKIQVSEL CKKAILRVAE
     LSSDDFHLDR HLYFACRDDR ERFCENTQAG EGRVYKCLFN HKFEESMSEK CREALTTRQK
     LIAQDYKVSY SLAKSCKSDL KKYRCNVENL PRSREARLSY LLMCLESAVH RGRQVSSECQ
     GEMLDYRRML MEDFSLSPEI ILSCRGEIEH HCSGLHRKGR TLHCLMKVVR GEKGNLGMNC
     QQALQTLIQE TDPGADYRID RALNEACESV IQTACKHIRS GDPMILSCLM EHLYTEKMVE
     DCEHRLLELQ YFISRDWKLD PVLYRKCQGD ASRLCHTHGW NETSEFMPQG AVFSCLYRHA
     YRTEEQGRRL SRECRAEVQR ILHQRAMDVK LDPALQDKCL IDLGKWCSEK TETGQELECL
     QDHLDDLVVE CRDIVGNLTE LESEDIQIEA LLMRACEPII QNFCHDVADN QIDSGDLMEC
     LIQNKHQKDM NEKCAIGVTH FQLVQMKDFR FSYKFKMACK EDVLKLCPNI KKKVDVVICL
     STTVRNDTLQ EAKEHRVSLK CRRQLRVEEL EMTEDIRLEP DLYEACKSDI KNFCSAVQYG
     NAQIIECLKE NKKQLSTRCH QKVFKLQETE MMDPELDYTL MRVCKQMIKR FCPEADSKTM
     LQCLKQNKNS ELMDPKCKQM ITKRQITQNT DYRLNPMLRK ACKADIPKFC HGILTKAKDD
     SELEGQVISC LKLRYADQRL SSDCEDQIRI IIQESALDYR LDPQLQLHCS DEISSLCAEE
     AAAQEQTGQV EECLKVNLLK IKTELCKKEV LNMLKESKAD IFVDPVLHTA CALDIKHHCA
     AITPGRGRQM SCLMEALEDK RVRLQPECKK RLNDRIEMWS YAAKVAPADG FSDLAMQVMT
     SPSKNYILSV ISGSICILFL IGLMCGRITK RVTRELKDR
//