ID   CMGA_HUMAN              Reviewed;         457 AA.
AC   P10645; B2R9E9; Q53FA8; Q6NR84; Q96E84; Q96GL7; Q9BQB5;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 7.
DT   22-JAN-2014, entry version 154.
DE   RecName: Full=Chromogranin-A;
DE            Short=CgA;
DE   AltName: Full=Pituitary secretory protein I;
DE            Short=SP-I;
DE   Contains:
DE     RecName: Full=Vasostatin-1;
DE     AltName: Full=Vasostatin I;
DE   Contains:
DE     RecName: Full=Vasostatin-2;
DE     AltName: Full=Vasostatin II;
DE   Contains:
DE     RecName: Full=EA-92;
DE   Contains:
DE     RecName: Full=ES-43;
DE   Contains:
DE     RecName: Full=Pancreastatin;
DE   Contains:
DE     RecName: Full=SS-18;
DE   Contains:
DE     RecName: Full=WA-8;
DE   Contains:
DE     RecName: Full=WE-14;
DE   Contains:
DE     RecName: Full=LF-19;
DE   Contains:
DE     RecName: Full=AL-11;
DE   Contains:
DE     RecName: Full=GV-19;
DE   Contains:
DE     RecName: Full=GR-44;
DE   Contains:
DE     RecName: Full=ER-37;
DE   Flags: Precursor;
GN   Name=CHGA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DISULFIDE BOND, AND VARIANT TRP-399.
RX   PubMed=2445752;
RA   Konecki D.S., Benedum U.M., Gerdes H.-H., Huttner W.B.;
RT   "The primary structure of human chromogranin A and pancreastatin.";
RL   J. Biol. Chem. 262:17026-17030(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3403545;
RA   Helman L.J., Ahn T.G., Levine M.A., Allison A., Cohen P.S.,
RA   Cooper M.J., Cohn D.V., Israel M.A.;
RT   "Molecular cloning and primary structure of human chromogranin A
RT   (secretory protein I) cDNA.";
RL   J. Biol. Chem. 263:11559-11563(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TRP-399.
RC   TISSUE=Liver;
RX   PubMed=8120054;
RA   Mouland A.J., Bevan S., White J.H., Hendy G.N.;
RT   "Human chromogranin A gene. Molecular cloning, structural analysis,
RT   and neuroendocrine cell-specific expression.";
RL   J. Biol. Chem. 269:6918-6926(1994).
RN   [4]
RP   SEQUENCE REVISION TO 384-397.
RA   Mouland A.J., Bevan S., White J.H., Hendy G.N.;
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-399.
RC   TISSUE=Stomach;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-264.
RC   TISSUE=Gastric mucosa;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   PROTEIN SEQUENCE OF 19-46.
RC   TISSUE=Adrenal gland;
RX   PubMed=3704195; DOI=10.1016/0167-0115(86)90040-6;
RA   Wilson B.S., Phan S.H., Lloyd R.V.;
RT   "Chromogranin from normal human adrenal glands: purification by
RT   monoclonal antibody affinity chromatography and partial N-terminal
RT   amino acid sequence.";
RL   Regul. Pept. 13:207-223(1986).
RN   [12]
RP   PROTEIN SEQUENCE OF 134-319.
RC   TISSUE=Pancreas;
RX   PubMed=2165909; DOI=10.1111/j.1432-1033.1990.tb19090.x;
RA   Tamamura H., Ohta M., Yoshizawa K., Ono Y., Funakoshi A., Miyasaka K.,
RA   Tateishi K., Jimi A., Yajima H., Fujii N., Funakoshi S.;
RT   "Isolation and characterization of a tumor-derived human protein
RT   related to chromogranin A and its in vitro conversion to human
RT   pancreastatin-48.";
RL   Eur. J. Biochem. 191:33-39(1990).
RN   [13]
RP   PROTEIN SEQUENCE OF 291-319.
RC   TISSUE=Pancreas;
RX   PubMed=2830133; DOI=10.1016/0014-5793(88)80606-9;
RA   Sekiya K., Ghatei M.A., Minamino N., Bretherton-Watt D., Matsuo H.,
RA   Bloom S.R.;
RT   "Isolation of human pancreastatin fragment containing the active
RT   sequence from a glucagonoma.";
RL   FEBS Lett. 228:153-156(1988).
RN   [14]
RP   PROTEIN SEQUENCE OF 342-355.
RX   PubMed=1577173; DOI=10.1016/0014-5793(92)80266-J;
RA   Curry W.J., Shaw C., Johnston C.F., Thim L., Buchanan K.D.;
RT   "Isolation and primary structure of a novel chromogranin A-derived
RT   peptide, WE-14, from a human midgut carcinoid tumour.";
RL   FEBS Lett. 301:319-321(1992).
RN   [15]
RP   PROTEIN SEQUENCE OF DERIVED PEPTIDES.
RX   PubMed=12442257;
RX   DOI=10.1002/1615-9861(200211)2:11<1586::AID-PROT1586>3.0.CO;2-K;
RA   Orr D.F., Chen T., Johnsen A.H., Chalk R., Buchanan K.D., Sloan J.M.,
RA   Rao P., Shaw C.;
RT   "The spectrum of endogenous human chromogranin A-derived peptides
RT   identified using a modified proteomic strategy.";
RL   Proteomics 2:1586-1600(2002).
RN   [16]
RP   GLYCOSYLATION AT THR-181; THR-183 AND THR-251, AND PHOSPHORYLATION AT
RP   SER-218; SER-270 AND SER-333.
RX   PubMed=9852066; DOI=10.1074/jbc.273.51.34087;
RA   Gadroy P., Stridsberg M., Capon C., Michalski J.-C., Strub J.-M.,
RA   van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.;
RT   "Phosphorylation and O-glycosylation sites of human chromogranin A
RT   (CGA79-439) from urine of patients with carcinoid tumors.";
RL   J. Biol. Chem. 273:34087-34097(1998).
RN   [17]
RP   PHOSPHORYLATION AT SER-322.
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   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-300; SER-322
RP   AND SER-402, AND MASS SPECTROMETRY.
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   [19]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS], STRUCTURE OF CARBOHYDRATES, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Cerebrospinal fluid;
RX   PubMed=19838169; DOI=10.1038/nmeth.1392;
RA   Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
RA   Brinkmalm G., Larson G.;
RT   "Enrichment of glycopeptides for glycan structure and attachment site
RT   identification.";
RL   Nat. Methods 6:809-811(2009).
RN   [20]
RP   GLYCOSYLATION, AND 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
RT   structures of human cerebrospinal fluid glycoproteins.";
RL   J. Proteome Res. 12:573-584(2013).
RN   [21]
RP   STRUCTURE BY NMR OF 370-390.
RX   PubMed=14759560; DOI=10.1016/j.regpep.2003.10.035;
RA   Preece N.E., Nguyen M., Mahata M., Mahata S.K., Mahapatra N.R.,
RA   Tsigelny I., O'Connor D.T.;
RT   "Conformational preferences and activities of peptides from the
RT   catecholamine release-inhibitory (catestatin) region of chromogranin
RT   A.";
RL   Regul. Pept. 118:75-87(2004).
RN   [22]
RP   VARIANTS SER-382 AND LEU-388.
RX   PubMed=14740315; DOI=10.1086/381399;
RA   Wen G., Mahata S.K., Cadman P., Mahata M., Ghosh S., Mahapatra N.R.,
RA   Rao F., Stridsberg M., Smith D.W., Mahboubi P., Schork N.J.,
RA   O'Connor D.T., Hamilton B.A.;
RT   "Both rare and common polymorphisms contribute functional variation at
RT   CHGA, a regulator of catecholamine physiology.";
RL   Am. J. Hum. Genet. 74:197-207(2004).
CC   -!- FUNCTION: Pancreastatin strongly inhibits glucose induced insulin
CC       release from the pancreas.
CC   -!- SUBUNIT: Interacts with SCG3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen
CC       (By similarity). Cytoplasmic vesicle, secretory vesicle membrane
CC       (By similarity). Secreted. Note=Associated with the secretory
CC       granule membrane through direct interaction to SCG3 that in turn
CC       binds to cholesterol-enriched lipid rafts in intragranular
CC       conditions (By similarity).
CC   -!- PTM: Sulfated on tyrosine residues and/or contains sulfated
CC       glycans.
CC   -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans.
CC   -!- MISCELLANEOUS: Binds calcium with a low-affinity.
CC   -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein
CC       family.
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DR   EMBL; J03483; AAA52017.1; -; mRNA.
DR   EMBL; J03915; AAA52018.1; -; mRNA.
DR   EMBL; U03749; AAB53685.1; -; Genomic_DNA.
DR   EMBL; U03742; AAB53685.1; JOINED; Genomic_DNA.
DR   EMBL; U03743; AAB53685.1; JOINED; Genomic_DNA.
DR   EMBL; U03744; AAB53685.1; JOINED; Genomic_DNA.
DR   EMBL; U03748; AAB53685.1; JOINED; Genomic_DNA.
DR   EMBL; U03745; AAB53685.1; JOINED; Genomic_DNA.
DR   EMBL; U03746; AAB53685.1; JOINED; Genomic_DNA.
DR   EMBL; U03747; AAB53685.1; JOINED; Genomic_DNA.
DR   EMBL; BT006869; AAP35515.1; -; mRNA.
DR   EMBL; AK223381; BAD97101.1; -; mRNA.
DR   EMBL; AL117192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK313757; BAG36496.1; -; mRNA.
DR   EMBL; CH471061; EAW81505.1; -; Genomic_DNA.
DR   EMBL; BC001059; AAH01059.1; -; mRNA.
DR   EMBL; BC006459; AAH06459.1; -; mRNA.
DR   EMBL; BC009384; AAH09384.2; -; mRNA.
DR   EMBL; BC012755; AAH12755.2; -; mRNA.
DR   PIR; A54376; A28468.
DR   RefSeq; NP_001266.1; NM_001275.3.
DR   UniGene; Hs.150793; -.
DR   PDB; 1LV4; NMR; -; A=370-390.
DR   PDBsum; 1LV4; -.
DR   ProteinModelPortal; P10645; -.
DR   IntAct; P10645; 3.
DR   MINT; MINT-4846180; -.
DR   STRING; 9606.ENSP00000216492; -.
DR   PhosphoSite; P10645; -.
DR   UniCarbKB; P10645; -.
DR   DMDM; 215274270; -.
DR   PaxDb; P10645; -.
DR   PRIDE; P10645; -.
DR   DNASU; 1113; -.
DR   Ensembl; ENST00000216492; ENSP00000216492; ENSG00000100604.
DR   GeneID; 1113; -.
DR   KEGG; hsa:1113; -.
DR   UCSC; uc001ybc.4; human.
DR   CTD; 1113; -.
DR   GeneCards; GC14P093389; -.
DR   HGNC; HGNC:1929; CHGA.
DR   HPA; CAB040544; -.
DR   HPA; CAB055506; -.
DR   HPA; HPA017369; -.
DR   MIM; 118910; gene.
DR   neXtProt; NX_P10645; -.
DR   PharmGKB; PA26461; -.
DR   eggNOG; NOG41926; -.
DR   HOVERGEN; HBG001272; -.
DR   InParanoid; P10645; -.
DR   OMA; VNSPMNK; -.
DR   OrthoDB; EOG7V766Z; -.
DR   PhylomeDB; P10645; -.
DR   ChiTaRS; CHGA; human.
DR   EvolutionaryTrace; P10645; -.
DR   GeneWiki; Chromogranin_A; -.
DR   GenomeRNAi; 1113; -.
DR   NextBio; 4618; -.
DR   PMAP-CutDB; Q6NR84; -.
DR   PRO; PR:P10645; -.
DR   ArrayExpress; P10645; -.
DR   Bgee; P10645; -.
DR   CleanEx; HS_CHGA; -.
DR   Genevestigator; P10645; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030141; C:secretory granule; IEA:InterPro.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008217; P:regulation of blood pressure; TAS:ProtInc.
DR   InterPro; IPR001819; Chromogranin_AB.
DR   InterPro; IPR018054; Chromogranin_CS.
DR   InterPro; IPR001990; Granin.
DR   PANTHER; PTHR10583; PTHR10583; 1.
DR   Pfam; PF01271; Granin; 2.
DR   PRINTS; PR00659; CHROMOGRANIN.
DR   PROSITE; PS00422; GRANINS_1; 1.
DR   PROSITE; PS00423; GRANINS_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Cytoplasmic vesicle; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Polymorphism;
KW   Reference proteome; Secreted; Signal; Sulfation.
FT   SIGNAL        1     18
FT   CHAIN        19    457       Chromogranin-A.
FT                                /FTId=PRO_0000005408.
FT   PEPTIDE      19    131       Vasostatin-2.
FT                                /FTId=PRO_0000005409.
FT   PEPTIDE      19     94       Vasostatin-1.
FT                                /FTId=PRO_0000005410.
FT   PEPTIDE     134    225       EA-92.
FT                                /FTId=PRO_0000005411.
FT   PEPTIDE     228    260       ES-43.
FT                                /FTId=PRO_0000005412.
FT   PEPTIDE     272    319       Pancreastatin.
FT                                /FTId=PRO_0000005413.
FT   PEPTIDE     322    339       SS-18.
FT                                /FTId=PRO_0000005414.
FT   PEPTIDE     342    355       WE-14.
FT                                /FTId=PRO_0000005415.
FT   PEPTIDE     342    349       WA-8.
FT                                /FTId=PRO_0000005416.
FT   PEPTIDE     358    376       LF-19.
FT                                /FTId=PRO_0000005417.
FT   PEPTIDE     380    390       AL-11.
FT                                /FTId=PRO_0000005418.
FT   PEPTIDE     393    411       GV-19.
FT                                /FTId=PRO_0000005419.
FT   PEPTIDE     413    456       GR-44.
FT                                /FTId=PRO_0000005420.
FT   PEPTIDE     420    456       ER-37.
FT                                /FTId=PRO_0000005421.
FT   REGION       41     59       O-glycosylated at one site only in
FT                                cerebrospinal fluid.
FT   REGION      181    191       O-glycosylated at one site only in
FT                                cerebrospinal fluid.
FT   MOD_RES     142    142       Phosphoserine (By similarity).
FT   MOD_RES     194    194       Phosphotyrosine (By similarity).
FT   MOD_RES     203    203       Phosphoserine.
FT   MOD_RES     218    218       Phosphoserine.
FT   MOD_RES     270    270       Phosphoserine.
FT   MOD_RES     300    300       Phosphoserine.
FT   MOD_RES     319    319       Glycine amide.
FT   MOD_RES     322    322       Phosphoserine.
FT   MOD_RES     333    333       Phosphoserine.
FT   MOD_RES     398    398       Phosphoserine (By similarity).
FT   MOD_RES     402    402       Phosphoserine.
FT   MOD_RES     456    456       Arginine amide.
FT   CARBOHYD    181    181       O-linked (GalNAc...).
FT                                /FTId=CAR_000116.
FT   CARBOHYD    183    183       O-linked (GalNAc...).
FT                                /FTId=CAR_000117.
FT   CARBOHYD    251    251       O-linked (GalNAc...).
FT                                /FTId=CAR_000118.
FT   DISULFID     35     56
FT   VARIANT      61     61       R -> Q (in dbSNP:rs3742712).
FT                                /FTId=VAR_047417.
FT   VARIANT     176    176       E -> K (in dbSNP:rs9658654).
FT                                /FTId=VAR_025636.
FT   VARIANT     264    264       E -> D (in dbSNP:rs9658655).
FT                                /FTId=VAR_025637.
FT   VARIANT     271    271       R -> W (in dbSNP:rs9658662).
FT                                /FTId=VAR_025638.
FT   VARIANT     274    274       A -> G (in dbSNP:rs9658663).
FT                                /FTId=VAR_025639.
FT   VARIANT     315    315       G -> S (in dbSNP:rs9658664).
FT                                /FTId=VAR_025640.
FT   VARIANT     332    332       L -> P (in dbSNP:rs9658665).
FT                                /FTId=VAR_025641.
FT   VARIANT     369    369       D -> N (in dbSNP:rs2228575).
FT                                /FTId=VAR_025642.
FT   VARIANT     382    382       G -> S (reduces activity 4.7 fold;
FT                                dbSNP:rs9658667).
FT                                /FTId=VAR_025643.
FT   VARIANT     388    388       P -> L (increases activity 2.3 fold;
FT                                dbSNP:rs9658668).
FT                                /FTId=VAR_025644.
FT   VARIANT     399    399       R -> W (in dbSNP:rs729940).
FT                                /FTId=VAR_025645.
FT   CONFLICT     41     41       S -> Y (in Ref. 1; AAA52018).
FT   CONFLICT     54     54       Q -> K (in Ref. 1; AAA52018).
FT   CONFLICT     87     87       A -> R (in Ref. 1; AAA52018).
FT   CONFLICT    119    119       E -> Q (in Ref. 1; AAA52018).
FT   CONFLICT    167    167       N -> K (in Ref. 1; AAA52018).
FT   CONFLICT    200    200       E -> K (in Ref. 1; AAA52018).
FT   CONFLICT    219    219       A -> V (in Ref. 1; AAA52018).
FT   CONFLICT    339    340       SK -> TN (in Ref. 1; AAA52018).
FT   CONFLICT    370    370       S -> R (in Ref. 1; AAA52018).
FT   CONFLICT    373    373       K -> R (in Ref. 1; AAA52018).
FT   CONFLICT    380    380       A -> G (in Ref. 1; AAA52018).
FT   CONFLICT    394    394       W -> S (in Ref. 1; AAA52018).
FT   CONFLICT    397    397       S -> N (in Ref. 1; AAA52018).
FT   CONFLICT    416    416       E -> Q (in Ref. 1; AAA52018).
FT   STRAND      380    383
FT   STRAND      385    387
SQ   SEQUENCE   457 AA;  50688 MW;  2F634E1A83FF0BB1 CRC64;
     MRSAAVLALL LCAGQVTALP VNSPMNKGDT EVMKCIVEVI SDTLSKPSPM PVSQECFETL
     RGDERILSIL RHQNLLKELQ DLALQGAKER AHQQKKHSGF EDELSEVLEN QSSQAELKEA
     VEEPSSKDVM EKREDSKEAE KSGEATDGAR PQALPEPMQE SKAEGNNQAP GEEEEEEEEA
     TNTHPPASLP SQKYPGPQAE GDSEGLSQGL VDREKGLSAE PGWQAKREEE EEEEEEAEAG
     EEAVPEEEGP TVVLNPHPSL GYKEIRKGES RSEALAVDGA GKPGAEEAQD PEGKGEQEHS
     QQKEEEEEMA VVPQGLFRGG KSGELEQEEE RLSKEWEDSK RWSKMDQLAK ELTAEKRLEG
     QEEEEDNRDS SMKLSFRARA YGFRGPGPQL RRGWRPSSRE DSLEAGLPLQ VRGYPEEKKE
     EEGSANRRPE DQELESLSAI EAELEKVAHQ LQALRRG
//