ID   SCG1_HUMAN              Reviewed;         677 AA.
AC   P05060; A8K021; Q59EU9; Q6IBS6; Q9BQV6; Q9UC25; Q9UJA6;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 2.
DT   27-MAR-2024, entry version 214.
DE   RecName: Full=Secretogranin-1;
DE   AltName: Full=Chromogranin-B;
DE            Short=CgB;
DE   AltName: Full=Secretogranin I;
DE            Short=SgI;
DE   Contains:
DE     RecName: Full=PE-11;
DE   Contains:
DE     RecName: Full=GAWK peptide;
DE   Contains:
DE     RecName: Full=CCB peptide;
DE   Flags: Precursor;
GN   Name=CHGB; Synonyms=SCG1;
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], PROTEIN SEQUENCE OF 21-34; 85-93; 334-340 AND
RP   347-355, TISSUE SPECIFICITY, AND VARIANT ALA-243.
RC   TISSUE=Adrenal medulla;
RX   PubMed=3608978; DOI=10.1002/j.1460-2075.1987.tb02355.x;
RA   Benedum U.M., Lamouroux A., Konecki D.S., Hille A., Baeuerle P.A.,
RA   Frank R., Lottspeich F., Mallet J., Huttner W.B.;
RT   "The primary structure of human secretogranin I (chromogranin B):
RT   comparison with chromogranin A reveals homologous terminal domains and a
RT   large intervening variable region.";
RL   EMBO J. 6:1203-1211(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-93; GLN-178;
RP   ALA-243; GLY-353 AND HIS-417.
RC   TISSUE=Adrenal gland;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-243.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-93; GLN-178;
RP   ALA-243; GLY-353 AND HIS-417.
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-243.
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-243.
RC   TISSUE=Lung;
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   [8]
RP   PROTEIN SEQUENCE OF 21-48.
RX   PubMed=1882087; DOI=10.1016/0167-0115(91)90216-4;
RA   Gill B.M., Barbosa J.A., Dinh T.Q., Garrod S., O'Connor D.T.;
RT   "Chromogranin B: isolation from pheochromocytoma, N-terminal sequence,
RT   tissue distribution and secretory vesicle processing.";
RL   Regul. Pept. 33:223-235(1991).
RN   [9]
RP   PROTEIN SEQUENCE OF 334-385.
RX   PubMed=7784254; DOI=10.1016/0196-9781(94)00176-6;
RA   Woussen-Colle M.-C., Gourlet P., Vandermeers A., Vandermeers-Piret M.-C.,
RA   D'Haens J., Velkeniers B., Robberecht P.;
RT   "Identification of a new chromogranin B fragment (314-365) in endocrine
RT   tumors.";
RL   Peptides 16:231-236(1995).
RN   [10]
RP   PROTEIN SEQUENCE OF 440-513.
RC   TISSUE=Pituitary;
RX   PubMed=3970711; DOI=10.1016/0006-291x(85)90648-5;
RA   Benjannet S., Leduc R., Lazure C., Seidah N.G., Marcinkiewicz M.,
RA   Chretien M.;
RT   "GAWK, a novel human pituitary polypeptide: isolation, immunocytochemical
RT   localization and complete amino acid sequence.";
RL   Biochem. Biophys. Res. Commun. 126:602-609(1985).
RN   [11]
RP   PROTEIN SEQUENCE OF 617-673.
RC   TISSUE=Pituitary;
RX   PubMed=3678488; DOI=10.1016/0014-5793(87)80438-6;
RA   Benjannet S., Leduc R., Adrouche N., Falgueyret J.P., Marcinkiewicz M.,
RA   Seidah N.G., Mbikay M., Lazure C., Chretien M.;
RT   "Chromogranin B (secretogranin I), a putative precursor of two novel
RT   pituitary peptides through processing at paired basic residues.";
RL   FEBS Lett. 224:142-148(1987).
RN   [12]
RP   PHOSPHORYLATION AT SER-149 AND SER-405.
RC   TISSUE=Pituitary;
RX   PubMed=14997482; DOI=10.1002/pmic.200300584;
RA   Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.;
RT   "Identification and characterization of phosphorylated proteins in the
RT   human pituitary.";
RL   Proteomics 4:587-598(2004).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-259; SER-263;
RP   SER-311; SER-335; SER-405 AND SER-617, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pituitary;
RX   PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA   Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT   "Phosphoproteomic analysis of the human pituitary.";
RL   Pituitary 9:109-120(2006).
RN   [14]
RP   GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=23234360; DOI=10.1021/pr300963h;
RA   Halim A., Ruetschi U., Larson G., Nilsson J.;
RT   "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT   of human cerebrospinal fluid glycoproteins.";
RL   J. Proteome Res. 12:573-584(2013).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-405, AND
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   [16]
RP   PHOSPHORYLATION AT SER-130; SER-225; SER-367; SER-377; SER-380 AND TYR-401.
RX   PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA   Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA   Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA   Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT   "A single kinase generates the majority of the secreted phosphoproteome.";
RL   Cell 161:1619-1632(2015).
RN   [17]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-93 AND
RP   SER-239.
RX   PubMed=25326458; DOI=10.1074/mcp.m114.043703;
RA   Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L.,
RA   Nilsson J., Larson G.;
RT   "Identification of chondroitin sulfate linkage region glycopeptides reveals
RT   prohormones as a novel class of proteoglycans.";
RL   Mol. Cell. Proteomics 14:41-49(2015).
RN   [18]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-93.
RX   PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617;
RA   Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.;
RT   "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected
RT   Correlation Between Glycan Sulfation and Attachment Site Characteristics.";
RL   Mol. Cell. Proteomics 22:100617-100617(2023).
CC   -!- FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule
CC       protein, which may be the precursor for other biologically active
CC       peptides.
CC   -!- INTERACTION:
CC       P05060; Q8IXL6: FAM20C; NbExp=2; IntAct=EBI-712619, EBI-7147442;
CC       P05060; Q5S007: LRRK2; NbExp=3; IntAct=EBI-712619, EBI-5323863;
CC       P05060; Q15796: SMAD2; NbExp=2; IntAct=EBI-712619, EBI-1040141;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:37453717}. Note=Neuroendocrine and endocrine
CC       secretory granules.
CC   -!- TISSUE SPECIFICITY: Detected in cerebrospinal fluid and urine (at
CC       protein level) (PubMed:25326458, PubMed:37453717). Expressed in the
CC       adrenal medulla, and in pheochromocytoma. Not expressed in liver.
CC       {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:3608978}.
CC   -!- PTM: Extensively processed by limited proteolysis at conserved basic
CC       residues. Alternative processing are seen in different tissues (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23234360,
CC       ECO:0000269|PubMed:25326458}.
CC   -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92949.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Y00064; CAA68271.1; -; mRNA.
DR   EMBL; AK289386; BAF82075.1; -; mRNA.
DR   EMBL; CR456726; CAG33007.1; -; mRNA.
DR   EMBL; AB209712; BAD92949.1; ALT_INIT; mRNA.
DR   EMBL; AL035461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471133; EAX10410.1; -; Genomic_DNA.
DR   EMBL; BC000375; AAH00375.1; -; mRNA.
DR   CCDS; CCDS13092.1; -.
DR   PIR; A29264; CNHUB.
DR   RefSeq; NP_001810.2; NM_001819.2.
DR   AlphaFoldDB; P05060; -.
DR   BioGRID; 107539; 37.
DR   IntAct; P05060; 38.
DR   MINT; P05060; -.
DR   STRING; 9606.ENSP00000368244; -.
DR   TCDB; 1.A.139.1.1; the chromogranin b/secretogranin-1 (cb/s1) family.
DR   GlyConnect; 1727; 1 N-Linked glycan (1 site).
DR   GlyCosmos; P05060; 1 site, 1 glycan.
DR   GlyGen; P05060; 4 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; P05060; -.
DR   PhosphoSitePlus; P05060; -.
DR   BioMuta; CHGB; -.
DR   DMDM; 311033509; -.
DR   EPD; P05060; -.
DR   jPOST; P05060; -.
DR   MassIVE; P05060; -.
DR   PaxDb; 9606-ENSP00000368244; -.
DR   PeptideAtlas; P05060; -.
DR   ProteomicsDB; 51772; -.
DR   Antibodypedia; 2170; 280 antibodies from 33 providers.
DR   DNASU; 1114; -.
DR   Ensembl; ENST00000378961.9; ENSP00000368244.4; ENSG00000089199.10.
DR   GeneID; 1114; -.
DR   KEGG; hsa:1114; -.
DR   MANE-Select; ENST00000378961.9; ENSP00000368244.4; NM_001819.3; NP_001810.2.
DR   UCSC; uc002wmg.4; human.
DR   AGR; HGNC:1930; -.
DR   CTD; 1114; -.
DR   DisGeNET; 1114; -.
DR   GeneCards; CHGB; -.
DR   HGNC; HGNC:1930; CHGB.
DR   HPA; ENSG00000089199; Tissue enhanced (adrenal gland, brain, pituitary gland).
DR   MIM; 118920; gene.
DR   neXtProt; NX_P05060; -.
DR   OpenTargets; ENSG00000089199; -.
DR   PharmGKB; PA26462; -.
DR   VEuPathDB; HostDB:ENSG00000089199; -.
DR   eggNOG; ENOG502QRBF; Eukaryota.
DR   GeneTree; ENSGT00940000154206; -.
DR   HOGENOM; CLU_026095_0_0_1; -.
DR   InParanoid; P05060; -.
DR   OMA; RPGHKHQ; -.
DR   OrthoDB; 5324197at2759; -.
DR   PhylomeDB; P05060; -.
DR   TreeFam; TF336596; -.
DR   PathwayCommons; P05060; -.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR   SignaLink; P05060; -.
DR   BioGRID-ORCS; 1114; 15 hits in 1150 CRISPR screens.
DR   ChiTaRS; CHGB; human.
DR   GeneWiki; Secretoneurin; -.
DR   GenomeRNAi; 1114; -.
DR   Pharos; P05060; Tbio.
DR   PRO; PR:P05060; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; P05060; Protein.
DR   Bgee; ENSG00000089199; Expressed in paraflocculus and 142 other cell types or tissues.
DR   ExpressionAtlas; P05060; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0005179; F:hormone activity; TAS:ProtInc.
DR   InterPro; IPR001819; Chromogranin_AB.
DR   InterPro; IPR018054; Chromogranin_CS.
DR   InterPro; IPR001990; Granin.
DR   PANTHER; PTHR10583; CHROMOGRANIN; 1.
DR   PANTHER; PTHR10583:SF4; SECRETOGRANIN-1; 1.
DR   Pfam; PF01271; Granin; 1.
DR   PRINTS; PR00659; CHROMOGRANIN.
DR   PROSITE; PS00422; GRANINS_1; 1.
DR   PROSITE; PS00423; GRANINS_2; 1.
DR   Genevisible; P05060; HS.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Phosphoprotein; Proteoglycan;
KW   Reference proteome; Secreted; Signal; Sulfation.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:1882087,
FT                   ECO:0000269|PubMed:3608978"
FT   CHAIN           21..677
FT                   /note="Secretogranin-1"
FT                   /id="PRO_0000005438"
FT   PEPTIDE         440..513
FT                   /note="GAWK peptide"
FT                   /id="PRO_0000005439"
FT   PEPTIDE         575..585
FT                   /note="PE-11"
FT                   /evidence="ECO:0000250|UniProtKB:P16014"
FT                   /id="PRO_0000432730"
FT   PEPTIDE         617..673
FT                   /note="CCB peptide"
FT                   /id="PRO_0000005440"
FT   REGION          64..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..120
FT                   /note="O-glycosylated at one site"
FT   REGION          475..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        114..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..344
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         79
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35314"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         130
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14997482,
FT                   ECO:0007744|PubMed:16807684"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23389"
FT   MOD_RES         225
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16807684"
FT   MOD_RES         263
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16807684"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         311
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16807684"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16807684"
FT   MOD_RES         341
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O35314"
FT   MOD_RES         367
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         377
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         380
FT                   /note="Phosphoserine; by FAM20C"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         401
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:26091039"
FT   MOD_RES         405
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14997482,
FT                   ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:24275569"
FT   MOD_RES         474
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P23389"
FT   MOD_RES         533
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         534
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         566
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P23389"
FT   MOD_RES         617
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16807684"
FT   MOD_RES         624
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O35314"
FT   MOD_RES         626
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23389"
FT   MOD_RES         631
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23389"
FT   CARBOHYD        93
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:25326458,
FT                   ECO:0000269|PubMed:37453717"
FT   CARBOHYD        239
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:25326458"
FT   DISULFID        36..57
FT   VARIANT         93
FT                   /note="S -> T (in dbSNP:rs6085324)"
FT                   /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT                   /id="VAR_043578"
FT   VARIANT         117
FT                   /note="K -> N (in dbSNP:rs236150)"
FT                   /id="VAR_024414"
FT   VARIANT         145
FT                   /note="D -> N (in dbSNP:rs6133278)"
FT                   /id="VAR_028235"
FT   VARIANT         178
FT                   /note="R -> Q (in dbSNP:rs910122)"
FT                   /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT                   /id="VAR_020287"
FT   VARIANT         200
FT                   /note="N -> H (in dbSNP:rs881118)"
FT                   /id="VAR_028236"
FT   VARIANT         232
FT                   /note="R -> Q (in dbSNP:rs6139873)"
FT                   /id="VAR_028237"
FT   VARIANT         243
FT                   /note="T -> A (in dbSNP:rs236151)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:3608978,
FT                   ECO:0000269|Ref.3, ECO:0000269|Ref.4, ECO:0000269|Ref.6"
FT                   /id="VAR_024415"
FT   VARIANT         353
FT                   /note="A -> G (in dbSNP:rs236152)"
FT                   /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT                   /id="VAR_024416"
FT   VARIANT         413
FT                   /note="P -> L (in dbSNP:rs742710)"
FT                   /id="VAR_028238"
FT   VARIANT         417
FT                   /note="R -> H (in dbSNP:rs742711)"
FT                   /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4"
FT                   /id="VAR_022012"
FT   CONFLICT        24
FT                   /note="D -> E (in Ref. 2; BAF82075)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   677 AA;  78276 MW;  BFDC97F7B21245B3 CRC64;
     MQPTLLLSLL GAVGLAAVNS MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV
     LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT
     EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE
     DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG
     EETGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP
     SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE
     RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR
     GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP
     GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD
     NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ
     YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA
     AMDLELQKIA EKFSQRG
//