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   27-MAR-2024, entry version 226.
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=Catestatin {ECO:0000303|PubMed:10781584, ECO:0000303|PubMed:17991725};
DE     AltName: Full=SL21 {ECO:0000303|PubMed:24723458};
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   Contains:
DE     RecName: Full=GE-25 {ECO:0000303|PubMed:7535395};
DE   Contains:
DE     RecName: Full=Serpinin-RRG;
DE   Contains:
DE     RecName: Full=Serpinin;
DE   Contains:
DE     RecName: Full=p-Glu serpinin precursor;
DE   Flags: Precursor;
GN   Name=CHGA;
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], DISULFIDE BOND, AND VARIANT TRP-399.
RX   PubMed=2445752; DOI=10.1016/s0021-9258(18)45486-5;
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; DOI=10.1016/s0021-9258(18)37995-x;
RA   Helman L.J., Ahn T.G., Levine M.A., Allison A., Cohen P.S., Cooper M.J.,
RA   Cohn D.V., Israel M.A.;
RT   "Molecular cloning and primary structure of human chromogranin A (secretory
RT   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; DOI=10.1016/s0021-9258(17)37462-8;
RA   Mouland A.J., Bevan S., White J.H., Hendy G.N.;
RT   "Human chromogranin A gene. Molecular cloning, structural analysis, and
RT   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 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., 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   [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., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., 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., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   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., 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 (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 project:
RT   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 monoclonal
RT   antibody affinity chromatography and partial N-terminal amino acid
RT   sequence.";
RL   Regul. Pept. 13:207-223(1986).
RN   [12]
RP   PROTEIN SEQUENCE OF 134-319, AND AMIDATION AT GLY-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 related to
RT   chromogranin A and its in vitro conversion to human pancreastatin-48.";
RL   Eur. J. Biochem. 191:33-39(1990).
RN   [13]
RP   PROTEIN SEQUENCE OF 291-319, AND AMIDATION AT GLY-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 sequence
RT   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 peptide,
RT   WE-14, from a human midgut carcinoid tumour.";
RL   FEBS Lett. 301:319-321(1992).
RN   [15]
RP   PROTEIN SEQUENCE OF DERIVED PEPTIDES, AND AMIDATION AT ARG-456 (PEPTIDE
RP   GR-44 AND PEPTIDE ER-37).
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   CHARACTERIZATION OF GE-25, AND TISSUE SPECIFICITY.
RX   PubMed=7535395; DOI=10.1016/0306-4522(94)90582-7;
RA   Kirchmair R., Benzer A., Troger J., Miller C., Marksteiner J., Saria A.,
RA   Gasser R.W., Hogue-Angeletti R., Fischer-Colbrie R., Winkler H.;
RT   "Molecular characterization of immunoreactivities of peptides derived from
RT   chromogranin A (GE-25) and from secretogranin II (secretoneurin) in human
RT   and bovine cerebrospinal fluid.";
RL   Neuroscience 63:1179-1187(1994).
RN   [17]
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 (CGA79-
RT   439) from urine of patients with carcinoid tumors.";
RL   J. Biol. Chem. 273:34087-34097(1998).
RN   [18]
RP   MASS SPECTROMETRY, PROTEOLYTIC PROCESSING, AND OXIDATION AT MET-372.
RX   PubMed=10781584; DOI=10.1074/jbc.m001232200;
RA   Taylor C.V., Taupenot L., Mahata S.K., Mahata M., Wu H.,
RA   Yasothornsrikul S., Toneff T., Caporale C., Jiang Q., Parmer R.J.,
RA   Hook V.Y., O'Connor D.T.;
RT   "Formation of the catecholamine release-inhibitory peptide catestatin from
RT   chromogranin A. Determination of proteolytic cleavage sites in hormone
RT   storage granules.";
RL   J. Biol. Chem. 275:22905-22915(2000).
RN   [19]
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   [20]
RP   FUNCTION (CATESTATIN).
RX   PubMed=15723172; DOI=10.1007/s00018-004-4461-9;
RA   Briolat J., Wu S.D., Mahata S.K., Gonthier B., Bagnard D.,
RA   Chasserot-Golaz S., Helle K.B., Aunis D., Metz-Boutigue M.H.;
RT   "New antimicrobial activity for the catecholamine release-inhibitory
RT   peptide from chromogranin A.";
RL   Cell. Mol. Life Sci. 62:377-385(2005).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-300; SER-322 AND
RP   SER-402, AND IDENTIFICATION BY MASS 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   [22]
RP   REVIEW.
RX   PubMed=18541522; DOI=10.1093/cvr/cvn155;
RA   Mahapatra N.R.;
RT   "Catestatin is a novel endogenous peptide that regulates cardiac function
RT   and blood pressure.";
RL   Cardiovasc. Res. 80:330-338(2008).
RN   [23]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS], AND STRUCTURE OF CARBOHYDRATES.
RC   TISSUE=Cerebrospinal fluid;
RX   PubMed=19838169; DOI=10.1038/nmeth.1392;
RA   Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA   Larson G.;
RT   "Enrichment of glycopeptides for glycan structure and attachment site
RT   identification.";
RL   Nat. Methods 6:809-811(2009).
RN   [24]
RP   REVIEW.
RX   PubMed=20116404; DOI=10.1016/j.regpep.2010.01.006;
RA   Mahata S.K., Mahata M., Fung M.M., O'Connor D.T.;
RT   "Catestatin: a multifunctional peptide from chromogranin A.";
RL   Regul. Pept. 162:33-43(2010).
RN   [25]
RP   FUNCTION (CATESTATIN).
RX   PubMed=21214543; DOI=10.1111/j.1365-2567.2010.03395.x;
RA   Aung G., Niyonsaba F., Ushio H., Kajiwara N., Saito H., Ikeda S., Ogawa H.,
RA   Okumura K.;
RT   "Catestatin, a neuroendocrine antimicrobial peptide, induces human mast
RT   cell migration, degranulation and production of cytokines and chemokines.";
RL   Immunology 132:527-539(2011).
RN   [26]
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   [27]
RP   FUNCTION (CATESTATIN).
RX   PubMed=24723458; DOI=10.1002/psc.2634;
RA   Mohseni S., Emtenani S., Emtenani S., Asoodeh A.;
RT   "Antioxidant properties of a human neuropeptide and its protective effect
RT   on free radical-induced DNA damage.";
RL   J. Pept. Sci. 20:429-437(2014).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, AND IDENTIFICATION BY
RP   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   [29]
RP   SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT
RP   SER-424.
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   [30]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-424.
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).
RN   [31]
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 A.";
RL   Regul. Pept. 118:75-87(2004).
RN   [32]
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., O'Connor D.T.,
RA   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).
RN   [33]
RP   VARIANTS SER-382; LEU-388 AND GLN-392, CHARACTERIZATION OF VARIANTS
RP   SER-382; LEU-388 AND GLN-392, AND FUNCTION (CATESTATIN).
RX   PubMed=15326220; DOI=10.1124/mol.104.002139;
RA   Mahata S.K., Mahata M., Wen G., Wong W.B., Mahapatra N.R., Hamilton B.A.,
RA   O'Connor D.T.;
RT   "The catecholamine release-inhibitory 'catestatin' fragment of chromogranin
RT   a: naturally occurring human variants with different potencies for multiple
RT   chromaffin cell nicotinic cholinergic responses.";
RL   Mol. Pharmacol. 66:1180-1191(2004).
RN   [34]
RP   VARIANT SER-382, AND CHARACTERIZATION OF VARIANT SER-382.
RX   PubMed=17438154; DOI=10.1161/circulationaha.106.628859;
RA   Rao F., Wen G., Gayen J.R., Das M., Vaingankar S.M., Rana B.K., Mahata M.,
RA   Kennedy B.P., Salem R.M., Stridsberg M., Abel K., Smith D.W., Eskin E.,
RA   Schork N.J., Hamilton B.A., Ziegler M.G., Mahata S.K., O'Connor D.T.;
RT   "Catecholamine release-inhibitory peptide catestatin (chromogranin A(352-
RT   372)): naturally occurring amino acid variant Gly364Ser causes profound
RT   changes in human autonomic activity and alters risk for hypertension.";
RL   Circulation 115:2271-2281(2007).
RN   [35]
RP   VARIANTS SER-382; LEU-388 AND GLN-392, CHARACTERIZATION OF VARIANTS
RP   SER-382; LEU-388 AND GLN-392, AND PROTEOLYTIC PROCESSING.
RX   PubMed=17991725; DOI=10.1210/en.2007-0838;
RA   Biswas N., Vaingankar S.M., Mahata M., Das M., Gayen J.R., Taupenot L.,
RA   Torpey J.W., O'Connor D.T., Mahata S.K.;
RT   "Proteolytic cleavage of human chromogranin a containing naturally
RT   occurring catestatin variants: differential processing at catestatin region
RT   by plasmin.";
RL   Endocrinology 149:749-757(2008).
CC   -!- FUNCTION: [Pancreastatin]: Strongly inhibits glucose induced insulin
CC       release from the pancreas.
CC   -!- FUNCTION: [Catestatin]: Inhibits catecholamine release from chromaffin
CC       cells and noradrenergic neurons by acting as a non-competitive
CC       nicotinic cholinergic antagonist (PubMed:15326220). Displays
CC       antibacterial activity against Gram-positive bacteria S.aureus and
CC       M.luteus, and Gram-negative bacteria E.coli and P.aeruginosa
CC       (PubMed:15723172, PubMed:24723458). Can induce mast cell migration,
CC       degranulation and production of cytokines and chemokines
CC       (PubMed:21214543). Acts as a potent scavenger of free radicals in vitro
CC       (PubMed:24723458). May play a role in the regulation of cardiac
CC       function and blood pressure (PubMed:18541522).
CC       {ECO:0000269|PubMed:15326220, ECO:0000269|PubMed:15723172,
CC       ECO:0000269|PubMed:21214543, ECO:0000269|PubMed:24723458,
CC       ECO:0000303|PubMed:18541522}.
CC   -!- FUNCTION: [Serpinin]: Regulates granule biogenesis in endocrine cells
CC       by up-regulating the transcription of protease nexin 1 (SERPINE2) via a
CC       cAMP-PKA-SP1 pathway. This leads to inhibition of granule protein
CC       degradation in the Golgi complex which in turn promotes granule
CC       formation. {ECO:0000250|UniProtKB:P26339}.
CC   -!- SUBUNIT: Self-interacts; self-assembly is promoted in vitro by
CC       chondroitin sulfate attachment which occurs at mildly acidic pH
CC       conditions (PubMed:25326458). Interacts with SCG3 (By similarity).
CC       {ECO:0000250|UniProtKB:P26339, ECO:0000269|PubMed:25326458}.
CC   -!- SUBCELLULAR LOCATION: [Serpinin]: Secreted
CC       {ECO:0000250|UniProtKB:P26339}. Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000250|UniProtKB:P26339}. Note=Pyroglutaminated serpinin
CC       localizes to secretory vesicle. {ECO:0000250|UniProtKB:P26339}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000250|UniProtKB:P10354}. Cytoplasmic vesicle, secretory vesicle,
CC       neuronal dense core vesicle {ECO:0000250|UniProtKB:P10354}. Secreted
CC       {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:37453717}.
CC       Note=Associated with the secretory granule membrane through direct
CC       interaction to SCG3 that in turn binds to cholesterol-enriched lipid
CC       rafts in intragranular conditions. In pituitary gonadotropes, located
CC       in large secretory granules. {ECO:0000250|UniProtKB:P10354}.
CC   -!- TISSUE SPECIFICITY: Detected in cerebrospinal fluid (at protein level)
CC       (PubMed:25326458). Detected in urine (at protein level)
CC       (PubMed:37453717). {ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:37453717}.
CC   -!- TISSUE SPECIFICITY: [GE-25]: Found in the brain.
CC       {ECO:0000269|PubMed:7535395}.
CC   -!- PTM: Sulfated on tyrosine residues and/or contains sulfated glycans.
CC   -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans
CC       (PubMed:9852066, PubMed:19838169, PubMed:23234360). Contains
CC       chondroitin sulfate (CS); CS attachment is pH-dependent, being observed
CC       at mildly acidic conditions of pH 5 but not at neutral pH, and promotes
CC       self-assembly in vitro (PubMed:25326458). {ECO:0000269|PubMed:19838169,
CC       ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:9852066}.
CC   -!- PTM: Proteolytic processing gives rise to an additional longer form of
CC       catestatin (residues 358-390) which displays a less potent
CC       catecholamine release-inhibitory activity (PubMed:10781584). Plasmin-
CC       mediated proteolytic processing can give rise to additional shorter and
CC       longer forms of catestatin peptides (PubMed:17991725).
CC       {ECO:0000269|PubMed:10781584, ECO:0000269|PubMed:17991725}.
CC   -!- MISCELLANEOUS: Binds calcium with a low-affinity.
CC   -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC       {ECO:0000305}.
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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   CCDS; CCDS9906.1; -.
DR   PIR; A54376; A28468.
DR   RefSeq; NP_001266.1; NM_001275.3.
DR   RefSeq; NP_001288619.1; NM_001301690.1.
DR   RefSeq; XP_011534672.1; XM_011536370.1.
DR   PDB; 1LV4; NMR; -; A=370-390.
DR   PDB; 6R2X; NMR; -; A=57-81.
DR   PDBsum; 1LV4; -.
DR   PDBsum; 6R2X; -.
DR   AlphaFoldDB; P10645; -.
DR   BMRB; P10645; -.
DR   SMR; P10645; -.
DR   BioGRID; 107538; 18.
DR   IntAct; P10645; 7.
DR   MINT; P10645; -.
DR   STRING; 9606.ENSP00000216492; -.
DR   GlyConnect; 93; 4 O-Linked glycans (3 sites).
DR   GlyCosmos; P10645; 5 sites, 8 glycans.
DR   GlyGen; P10645; 6 sites, 8 O-linked glycans (5 sites).
DR   iPTMnet; P10645; -.
DR   PhosphoSitePlus; P10645; -.
DR   BioMuta; CHGA; -.
DR   DMDM; 215274270; -.
DR   EPD; P10645; -.
DR   jPOST; P10645; -.
DR   MassIVE; P10645; -.
DR   PaxDb; 9606-ENSP00000216492; -.
DR   PeptideAtlas; P10645; -.
DR   ProteomicsDB; 52635; -.
DR   TopDownProteomics; P10645; -.
DR   Antibodypedia; 738; 3219 antibodies from 51 providers.
DR   CPTC; P10645; 3 antibodies.
DR   DNASU; 1113; -.
DR   Ensembl; ENST00000216492.10; ENSP00000216492.5; ENSG00000100604.13.
DR   Ensembl; ENST00000613166.3; ENSP00000478198.1; ENSG00000276781.3.
DR   GeneID; 1113; -.
DR   KEGG; hsa:1113; -.
DR   MANE-Select; ENST00000216492.10; ENSP00000216492.5; NM_001275.4; NP_001266.1.
DR   UCSC; uc001ybc.6; human.
DR   AGR; HGNC:1929; -.
DR   CTD; 1113; -.
DR   DisGeNET; 1113; -.
DR   GeneCards; CHGA; -.
DR   HGNC; HGNC:1929; CHGA.
DR   HPA; ENSG00000100604; Tissue enriched (parathyroid).
DR   MIM; 118910; gene.
DR   neXtProt; NX_P10645; -.
DR   OpenTargets; ENSG00000100604; -.
DR   PharmGKB; PA26461; -.
DR   VEuPathDB; HostDB:ENSG00000100604; -.
DR   eggNOG; ENOG502RZBD; Eukaryota.
DR   GeneTree; ENSGT00940000154206; -.
DR   InParanoid; P10645; -.
DR   OMA; ANTHPPA; -.
DR   OrthoDB; 4262934at2759; -.
DR   PhylomeDB; P10645; -.
DR   TreeFam; TF336596; -.
DR   PathwayCommons; P10645; -.
DR   Reactome; R-HSA-6803157; Antimicrobial peptides.
DR   SignaLink; P10645; -.
DR   SIGNOR; P10645; -.
DR   BioGRID-ORCS; 1113; 178 hits in 1147 CRISPR screens.
DR   ChiTaRS; CHGA; human.
DR   EvolutionaryTrace; P10645; -.
DR   GeneWiki; Chromogranin_A; -.
DR   GenomeRNAi; 1113; -.
DR   Pharos; P10645; Tbio.
DR   PRO; PR:P10645; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; P10645; Protein.
DR   Bgee; ENSG00000100604; Expressed in islet of Langerhans and 98 other cell types or tissues.
DR   ExpressionAtlas; P10645; baseline and differential.
DR   GO; GO:0042583; C:chromaffin granule; ISS:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; ISS:BHF-UCL.
DR   GO; GO:0098992; C:neuronal dense core vesicle; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030141; C:secretory granule; ISS:BHF-UCL.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; TAS:BHF-UCL.
DR   GO; GO:0086030; P:adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation; IBA:GO_Central.
DR   GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0045576; P:mast cell activation; IDA:UniProtKB.
DR   GO; GO:0002551; P:mast cell chemotaxis; IDA:UniProtKB.
DR   GO; GO:0043303; P:mast cell degranulation; IDA:UniProtKB.
DR   GO; GO:0033604; P:negative regulation of catecholamine secretion; IDA:UniProtKB.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IBA:GO_Central.
DR   GO; GO:0006996; P:organelle organization; ISS:BHF-UCL.
DR   GO; GO:0060452; P:positive regulation of cardiac muscle contraction; ISS:BHF-UCL.
DR   GO; GO:2000707; P:positive regulation of dense core granule biogenesis; ISS:UniProtKB.
DR   GO; GO:1900738; P:positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:BHF-UCL.
DR   GO; GO:1901899; P:positive regulation of relaxation of cardiac muscle; ISS:BHF-UCL.
DR   GO; GO:0033366; P:protein localization to secretory granule; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; TAS:ProtInc.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; ISS:BHF-UCL.
DR   InterPro; IPR001819; Chromogranin_AB.
DR   InterPro; IPR018054; Chromogranin_CS.
DR   InterPro; IPR001990; Granin.
DR   PANTHER; PTHR10583; CHROMOGRANIN; 1.
DR   PANTHER; PTHR10583:SF1; CHROMOGRANIN-A; 1.
DR   Pfam; PF01271; Granin; 2.
DR   PRINTS; PR00659; CHROMOGRANIN.
DR   PROSITE; PS00422; GRANINS_1; 1.
DR   PROSITE; PS00423; GRANINS_2; 1.
DR   Genevisible; P10645; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Antibiotic; Antimicrobial; Calcium;
KW   Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Glycoprotein;
KW   Oxidation; Phosphoprotein; Proteoglycan; Reference proteome; Secreted;
KW   Signal; Sulfation.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:12442257,
FT                   ECO:0000269|PubMed:3704195"
FT   CHAIN           19..457
FT                   /note="Chromogranin-A"
FT                   /id="PRO_0000005408"
FT   PEPTIDE         19..131
FT                   /note="Vasostatin-2"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005409"
FT   PEPTIDE         19..94
FT                   /note="Vasostatin-1"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005410"
FT   PEPTIDE         134..225
FT                   /note="EA-92"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005411"
FT   PEPTIDE         228..260
FT                   /note="ES-43"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005412"
FT   PEPTIDE         272..319
FT                   /note="Pancreastatin"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005413"
FT   PEPTIDE         322..339
FT                   /note="SS-18"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005414"
FT   PEPTIDE         342..355
FT                   /note="WE-14"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005415"
FT   PEPTIDE         342..349
FT                   /note="WA-8"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005416"
FT   PEPTIDE         358..376
FT                   /note="LF-19"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005417"
FT   PEPTIDE         370..390
FT                   /note="Catestatin"
FT                   /evidence="ECO:0000269|PubMed:10781584"
FT                   /id="PRO_0000432682"
FT   PEPTIDE         380..390
FT                   /note="AL-11"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005418"
FT   PEPTIDE         393..417
FT                   /note="GE-25"
FT                   /evidence="ECO:0000303|PubMed:7535395"
FT                   /id="PRO_0000432683"
FT   PEPTIDE         393..411
FT                   /note="GV-19"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005419"
FT   PEPTIDE         413..456
FT                   /note="GR-44"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005420"
FT   PEPTIDE         420..456
FT                   /note="ER-37"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT                   /id="PRO_0000005421"
FT   PEPTIDE         429..457
FT                   /note="Serpinin-RRG"
FT                   /evidence="ECO:0000250|UniProtKB:P10354"
FT                   /id="PRO_0000432684"
FT   PEPTIDE         429..454
FT                   /note="Serpinin"
FT                   /evidence="ECO:0000250|UniProtKB:P26339"
FT                   /id="PRO_0000432685"
FT   PEPTIDE         432..454
FT                   /note="p-Glu serpinin precursor"
FT                   /evidence="ECO:0000250|UniProtKB:P26339"
FT                   /id="PRO_0000432686"
FT   REGION          41..59
FT                   /note="O-glycosylated at one site only in cerebrospinal
FT                   fluid"
FT   REGION          88..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..191
FT                   /note="O-glycosylated at one site only in cerebrospinal
FT                   fluid"
FT   COMPBIAS        88..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..245
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..440
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05059"
FT   MOD_RES         194
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P05059"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16807684"
FT   MOD_RES         218
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9852066"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9852066"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16807684"
FT   MOD_RES         319
FT                   /note="Glycine amide"
FT                   /evidence="ECO:0000269|PubMed:2165909,
FT                   ECO:0000269|PubMed:2830133"
FT   MOD_RES         322
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:14997482,
FT                   ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:24275569"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9852066"
FT   MOD_RES         371
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10354"
FT   MOD_RES         372
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:17991725"
FT   MOD_RES         398
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05059"
FT   MOD_RES         402
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16807684"
FT   MOD_RES         424
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10354"
FT   MOD_RES         438
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10354"
FT   MOD_RES         456
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:12442257"
FT   CARBOHYD        181
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:9852066"
FT                   /id="CAR_000116"
FT   CARBOHYD        183
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:9852066"
FT                   /id="CAR_000117"
FT   CARBOHYD        251
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:9852066"
FT                   /id="CAR_000118"
FT   CARBOHYD        424
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:25326458,
FT                   ECO:0000269|PubMed:37453717"
FT   DISULFID        35..56
FT                   /evidence="ECO:0000269|PubMed:2445752"
FT   VARIANT         61
FT                   /note="R -> Q (in dbSNP:rs3742712)"
FT                   /id="VAR_047417"
FT   VARIANT         176
FT                   /note="E -> K (in dbSNP:rs9658654)"
FT                   /id="VAR_025636"
FT   VARIANT         264
FT                   /note="E -> D (in dbSNP:rs9658655)"
FT                   /evidence="ECO:0000269|Ref.7"
FT                   /id="VAR_025637"
FT   VARIANT         271
FT                   /note="R -> W (in dbSNP:rs9658662)"
FT                   /id="VAR_025638"
FT   VARIANT         274
FT                   /note="A -> G (in dbSNP:rs9658663)"
FT                   /id="VAR_025639"
FT   VARIANT         315
FT                   /note="G -> S (in dbSNP:rs9658664)"
FT                   /id="VAR_025640"
FT   VARIANT         332
FT                   /note="L -> P (in dbSNP:rs9658665)"
FT                   /id="VAR_025641"
FT   VARIANT         369
FT                   /note="D -> N (in dbSNP:rs2228575)"
FT                   /id="VAR_025642"
FT   VARIANT         382
FT                   /note="G -> S (probable protective factor against
FT                   hypertension; reduces activity 4.7 fold; no effect on
FT                   plasmin-mediated proteolytic processing; increase in
FT                   ability to inhibit nicotine-evoked catecholamine secretion
FT                   in vitro; displays alterations in baroreceptor function;
FT                   dbSNP:rs9658667)"
FT                   /evidence="ECO:0000269|PubMed:14740315,
FT                   ECO:0000269|PubMed:15326220, ECO:0000269|PubMed:17438154,
FT                   ECO:0000269|PubMed:17991725"
FT                   /id="VAR_025643"
FT   VARIANT         388
FT                   /note="P -> L (increases activity 2.3 fold; decrease in
FT                   plasmin-mediated proteolytic processing; decrease in
FT                   ability to inhibit nicotine-evoked catecholamine secretion
FT                   in vitro; dbSNP:rs9658668)"
FT                   /evidence="ECO:0000269|PubMed:14740315,
FT                   ECO:0000269|PubMed:15326220, ECO:0000269|PubMed:17991725"
FT                   /id="VAR_025644"
FT   VARIANT         392
FT                   /note="R -> Q (no effect on plasmin-mediated proteolytic
FT                   processing; decrease in ability to inhibit nicotine-evoked
FT                   catecholamine secretion in vitro; dbSNP:rs9658669)"
FT                   /evidence="ECO:0000269|PubMed:15326220,
FT                   ECO:0000269|PubMed:17991725"
FT                   /id="VAR_072687"
FT   VARIANT         399
FT                   /note="R -> W (in dbSNP:rs729940)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:2445752, ECO:0000269|PubMed:8120054"
FT                   /id="VAR_025645"
FT   CONFLICT        41
FT                   /note="S -> Y (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54
FT                   /note="Q -> K (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="A -> R (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="E -> Q (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        167
FT                   /note="N -> K (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        200
FT                   /note="E -> K (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        219
FT                   /note="A -> V (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339..340
FT                   /note="SK -> TN (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370
FT                   /note="S -> R (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        373
FT                   /note="K -> R (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380
FT                   /note="A -> G (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        394
FT                   /note="W -> S (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        397
FT                   /note="S -> N (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="E -> Q (in Ref. 1; AAA52018)"
FT                   /evidence="ECO:0000305"
FT   HELIX           63..76
FT                   /evidence="ECO:0007829|PDB:6R2X"
FT   STRAND          380..383
FT                   /evidence="ECO:0007829|PDB:1LV4"
FT   STRAND          385..387
FT                   /evidence="ECO:0007829|PDB:1LV4"
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
//