GSLG1_HUMAN
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 03-AUG-2022, entry version 188.
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; 99.
DR CORUM; Q92896; -.
DR DIP; DIP-27582N; -.
DR IntAct; Q92896; 36.
DR MINT; Q92896; -.
DR STRING; 9606.ENSP00000205061; -.
DR GlyConnect; 1280; 42 N-Linked glycans (4 sites).
DR GlyGen; Q92896; 7 sites, 40 N-linked glycans (4 sites), 1 O-linked glycan (2 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; Q92896; -.
DR PeptideAtlas; Q92896; -.
DR PRIDE; Q92896; -.
DR ProteomicsDB; 75578; -. [Q92896-1]
DR ProteomicsDB; 75579; -. [Q92896-2]
DR ProteomicsDB; 75580; -. [Q92896-3]
DR Antibodypedia; 2273; 320 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 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; FTYKFKE; -.
DR OrthoDB; 189325at2759; -.
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; 16 hits in 1079 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 220 other tissues.
DR ExpressionAtlas; Q92896; baseline and differential.
DR Genevisible; Q92896; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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; PTHR11884; 1.
DR Pfam; PF00839; Cys_rich_FGFR; 15.
DR PROSITE; PS51289; GLG1_C_RICH; 16.
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
