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 16-MAR-2016, entry version 174. 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; 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, 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 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, 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 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, AND AMIDATION AT ARG-456 RP (PEPTIDE 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., RA Saria A., Gasser R.W., Hogue-Angeletti R., Fischer-Colbrie R., RA Winkler H.; RT "Molecular characterization of immunoreactivities of peptides derived RT from chromogranin A (GE-25) and from secretogranin II (secretoneurin) RT in human 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 RT (CGA79-439) 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 RT from chromogranin A. Determination of proteolytic cleavage sites in RT hormone 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 RP AND SER-402, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 RT function 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., 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 [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., RA Ogawa H., Okumura K.; RT "Catestatin, a neuroendocrine antimicrobial peptide, induces human RT mast cell migration, degranulation and production of cytokines and RT 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 RT structures 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 RT effect 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 RP 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [29] 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 [30] 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). RN [31] 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., RA Hamilton B.A., O'Connor D.T.; RT "The catecholamine release-inhibitory 'catestatin' fragment of RT chromogranin a: naturally occurring human variants with different RT potencies for multiple chromaffin cell nicotinic cholinergic RT responses."; RL Mol. Pharmacol. 66:1180-1191(2004). RN [32] 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., RA Mahata M., Kennedy B.P., Salem R.M., Stridsberg M., Abel K., RA Smith D.W., Eskin E., Schork N.J., Hamilton B.A., Ziegler M.G., RA Mahata S.K., O'Connor D.T.; RT "Catecholamine release-inhibitory peptide catestatin (chromogranin RT A(352-372)): naturally occurring amino acid variant Gly364Ser causes RT profound changes in human autonomic activity and alters risk for RT hypertension."; RL Circulation 115:2271-2281(2007). RN [33] RP VARIANTS SER-382; LEU-388 AND GLN-392, CHARACTERIZATION OF VARIANTS RP SER-382; LEU-388 AND GLN-392, PROTEOLYTIC PROCESSING, AND MASS RP SPECTROMETRY. RX PubMed=17991725; DOI=10.1210/en.2007-0838; RA Biswas N., Vaingankar S.M., Mahata M., Das M., Gayen J.R., RA Taupenot L., 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 RT region 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 CC chromaffin cells and noradrenergic neurons by acting as a non- CC competitive nicotinic cholinergic antagonist (PubMed:15326220). CC Displays antibacterial activity against Gram-positive bacteria CC S.aureus and M.luteus, and Gram-negative bacteria E.coli and CC P.aeruginosa (PubMed:15723172 and PubMed:24723458). Can induce CC mast cell migration, degranulation and production of cytokines and CC chemokines (PubMed:21214543). Acts as a potent scavenger of free CC radicals in vitro (PubMed:24723458). May play a role in the CC regulation of cardiac function and blood pressure CC (PubMed:18541522). {ECO:0000269|PubMed:15326220, CC ECO:0000269|PubMed:15723172, ECO:0000269|PubMed:21214543, CC ECO:0000269|PubMed:24723458, ECO:0000303|PubMed:18541522}. CC -!- FUNCTION: Serpinin: Regulates granule biogenesis in endocrine CC cells by up-regulating the transcription of protease nexin 1 CC (SERPINE2) via a cAMP-PKA-SP1 pathway. This leads to inhibition of CC granule protein degradation in the Golgi complex which in turn CC promotes granule formation. {ECO:0000250|UniProtKB:P26339}. CC -!- SUBUNIT: Interacts with SCG3. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen CC {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle membrane CC {ECO:0000250}. 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. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Serpinin: Secreted CC {ECO:0000250|UniProtKB:P26339}. Cytoplasmic vesicle, secretory CC vesicle {ECO:0000250|UniProtKB:P26339}. Note=Pyroglutaminated CC serpinin localizes to secretory vesicle. CC {ECO:0000250|UniProtKB:P26339}. CC -!- TISSUE SPECIFICITY: GE-25 is found in the brain. CC {ECO:0000269|PubMed:7535395}. 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 {ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23234360, CC ECO:0000269|PubMed:9852066}. CC -!- PTM: Proteolytic processing gives rise to an additional longer CC form of catestatin (residues 358-390) which displays a less potent CC catecholamine release-inhibitory activity (PubMed:10781584). CC Plasmin-mediated proteolytic processing can give rise to CC additional shorter and longer forms of catestatin peptides CC (PubMed:17991725). {ECO:0000269|PubMed:10781584, CC ECO:0000269|PubMed:17991725}. CC -!- MASS SPECTROMETRY: Mass=2051.89; Method=MALDI; Range=357-373; CC Evidence={ECO:0000269|PubMed:17991725}; CC -!- MASS SPECTROMETRY: Mass=3770; Method=MALDI; Range=358-390; CC Evidence={ECO:0000269|PubMed:10781584}; CC -!- MASS SPECTROMETRY: Mass=3787; Method=MALDI; Range=358-390; CC Note=With methionine sulfoxide at Met-372.; CC Evidence={ECO:0000269|PubMed:10781584}; CC -!- MASS SPECTROMETRY: Mass=1070.54; Method=MALDI; Range=369-377; CC Evidence={ECO:0000269|PubMed:17991725}; CC -!- MASS SPECTROMETRY: Mass=840.45; Method=MALDI; Range=378-384; CC Evidence={ECO:0000269|PubMed:17991725}; CC -!- MASS SPECTROMETRY: Mass=1389.74; Method=MALDI; Range=378-390; CC Evidence={ECO:0000269|PubMed:17991725}; CC -!- MASS SPECTROMETRY: Mass=1419.8; Method=MALDI; Range=378-390; CC Note=With variant Ser-382.; CC Evidence={ECO:0000269|PubMed:17991725}; CC -!- MASS SPECTROMETRY: Mass=1545.84; Method=MALDI; Range=378-391; CC Evidence={ECO:0000269|PubMed:17991725}; CC -!- MASS SPECTROMETRY: Mass=1575.9; Method=MALDI; Range=378-391; CC Note=With variant Ser-382.; CC Evidence={ECO:0000269|PubMed:17991725}; CC -!- MASS SPECTROMETRY: Mass=1701.96; Method=MALDI; Range=378-392; CC Evidence={ECO:0000269|PubMed:17991725}; CC -!- MASS SPECTROMETRY: Mass=1318.71; Method=MALDI; Range=380-391; CC Evidence={ECO:0000269|PubMed:17991725}; CC -!- MISCELLANEOUS: Binds calcium with a low-affinity. CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 RefSeq; XP_011544942.1; XM_011546640.1. DR UniGene; Hs.150793; -. DR PDB; 1LV4; NMR; -; A=370-390. DR PDBsum; 1LV4; -. DR ProteinModelPortal; P10645; -. DR BioGrid; 107538; 10. DR IntAct; P10645; 3. DR MINT; MINT-4846180; -. DR STRING; 9606.ENSP00000216492; -. DR iPTMnet; P10645; -. DR PhosphoSite; P10645; -. DR UniCarbKB; P10645; -. DR BioMuta; CHGA; -. DR DMDM; 215274270; -. DR PaxDb; P10645; -. DR PRIDE; P10645; -. DR TopDownProteomics; P10645; -. DR DNASU; 1113; -. DR Ensembl; ENST00000216492; ENSP00000216492; ENSG00000100604. DR Ensembl; ENST00000613166; ENSP00000478198; ENSG00000276781. DR GeneID; 1113; -. DR KEGG; hsa:1113; -. DR UCSC; uc001ybc.6; human. DR CTD; 1113; -. DR GeneCards; CHGA; -. DR HGNC; HGNC:1929; CHGA. DR HPA; CAB000023; -. DR HPA; CAB040544; -. DR HPA; CAB055506; -. DR HPA; CAB058688; -. DR HPA; HPA017369; -. DR MIM; 118910; gene. DR neXtProt; NX_P10645; -. DR PharmGKB; PA26461; -. DR eggNOG; ENOG410II3Z; Eukaryota. DR eggNOG; ENOG410YGBX; LUCA. DR GeneTree; ENSGT00730000111266; -. DR HOVERGEN; HBG001272; -. DR InParanoid; P10645; -. DR OMA; VNSPMNK; -. DR OrthoDB; EOG7V766Z; -. DR PhylomeDB; P10645; -. DR TreeFam; TF336596; -. 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 Proteomes; UP000005640; Chromosome 14. DR Bgee; P10645; -. DR CleanEx; HS_CHGA; -. DR ExpressionAtlas; P10645; baseline and differential. DR Genevisible; P10645; HS. DR GO; GO:0042583; C:chromaffin granule; IEA:Ensembl. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0042629; C:mast cell granule; IDA:GOC. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell. 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 other 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:0032762; P:mast cell cytokine production; 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:1901215; P:negative regulation of neuron death; IEA:Ensembl. DR GO; GO:0045908; P:negative regulation of vasodilation; IEA:Ensembl. DR GO; GO:0006996; P:organelle organization; IEA:Ensembl. DR GO; GO:0042698; P:ovulation cycle; IEA:Ensembl. DR GO; GO:0030816; P:positive regulation of cAMP metabolic process; IEA:Ensembl. 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; 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; IEA:Ensembl. 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; Antibiotic; Antimicrobial; Calcium; KW Cleavage on pair of basic residues; Complete proteome; KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond; KW Fungicide; Glycoprotein; Membrane; Oxidation; Phosphoprotein; KW Polymorphism; Pyrrolidone carboxylic acid; Reference proteome; KW Secreted; Signal; Sulfation. FT SIGNAL 1 18 {ECO:0000269|PubMed:12442257, FT ECO:0000269|PubMed:3704195}. FT CHAIN 19 457 Chromogranin-A. FT /FTId=PRO_0000005408. FT PEPTIDE 19 131 Vasostatin-2. FT {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005409. FT PEPTIDE 19 94 Vasostatin-1. FT {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005410. FT PEPTIDE 134 225 EA-92. {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005411. FT PEPTIDE 228 260 ES-43. {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005412. FT PEPTIDE 272 319 Pancreastatin. FT {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005413. FT PEPTIDE 322 339 SS-18. {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005414. FT PEPTIDE 342 355 WE-14. {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005415. FT PEPTIDE 342 349 WA-8. {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005416. FT PEPTIDE 358 376 LF-19. {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005417. FT PEPTIDE 370 390 Catestatin. FT {ECO:0000269|PubMed:10781584}. FT /FTId=PRO_0000432682. FT PEPTIDE 380 390 AL-11. {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005418. FT PEPTIDE 393 417 GE-25. {ECO:0000303|PubMed:7535395}. FT /FTId=PRO_0000432683. FT PEPTIDE 393 411 GV-19. {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005419. FT PEPTIDE 413 456 GR-44. {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005420. FT PEPTIDE 420 456 ER-37. {ECO:0000269|PubMed:12442257}. FT /FTId=PRO_0000005421. FT PEPTIDE 429 457 Serpinin-RRG. FT {ECO:0000250|UniProtKB:P10354}. FT /FTId=PRO_0000432684. FT PEPTIDE 429 454 Serpinin. {ECO:0000250|UniProtKB:P26339}. FT /FTId=PRO_0000432685. FT PEPTIDE 432 454 p-Glu serpinin precursor. FT {ECO:0000250|UniProtKB:P26339}. FT /FTId=PRO_0000432686. 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. FT {ECO:0000250|UniProtKB:P05059}. FT MOD_RES 194 194 Phosphotyrosine. FT {ECO:0000250|UniProtKB:P05059}. FT MOD_RES 203 203 Phosphoserine. FT {ECO:0000244|PubMed:16807684}. FT MOD_RES 218 218 Phosphoserine. FT {ECO:0000269|PubMed:9852066}. FT MOD_RES 270 270 Phosphoserine. FT {ECO:0000269|PubMed:9852066}. FT MOD_RES 300 300 Phosphoserine. FT {ECO:0000244|PubMed:16807684}. FT MOD_RES 319 319 Glycine amide. FT {ECO:0000269|PubMed:2165909, FT ECO:0000269|PubMed:2830133}. FT MOD_RES 322 322 Phosphoserine. FT {ECO:0000244|PubMed:16807684, FT ECO:0000244|PubMed:24275569, FT ECO:0000269|PubMed:14997482}. FT MOD_RES 333 333 Phosphoserine. FT {ECO:0000269|PubMed:9852066}. FT MOD_RES 371 371 Phosphoserine. FT {ECO:0000250|UniProtKB:P10354}. FT MOD_RES 372 372 Methionine sulfoxide. FT {ECO:0000269|PubMed:17991725}. FT MOD_RES 398 398 Phosphoserine. FT {ECO:0000250|UniProtKB:P05059}. FT MOD_RES 402 402 Phosphoserine. FT {ECO:0000244|PubMed:16807684}. FT MOD_RES 424 424 Phosphoserine. FT {ECO:0000250|UniProtKB:P10354}. FT MOD_RES 432 432 Pyrrolidone carboxylic acid. FT {ECO:0000250|UniProtKB:P26339}. FT MOD_RES 438 438 Phosphoserine. FT {ECO:0000250|UniProtKB:P10354}. FT MOD_RES 456 456 Arginine amide. FT {ECO:0000269|PubMed:12442257}. FT CARBOHYD 181 181 O-linked (GalNAc...). FT {ECO:0000269|PubMed:9852066}. FT /FTId=CAR_000116. FT CARBOHYD 183 183 O-linked (GalNAc...). FT {ECO:0000269|PubMed:9852066}. FT /FTId=CAR_000117. FT CARBOHYD 251 251 O-linked (GalNAc...). FT {ECO:0000269|PubMed:9852066}. FT /FTId=CAR_000118. FT DISULFID 35 56 {ECO:0000269|PubMed:2445752}. 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 {ECO:0000269|Ref.7}. 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 (polymorphism; may be associated FT with a reduced risk for hypertension FT especially in men; reduces activity 4.7 FT fold; no effect on plasmin-mediated FT proteolytic processing; increase in FT ability to inhibit nicotine-evoked FT catecholamine secretion in vitro; FT displays alterations in baroreceptor FT function; dbSNP:rs9658667). FT {ECO:0000269|PubMed:14740315, FT ECO:0000269|PubMed:15326220, FT ECO:0000269|PubMed:17438154, FT ECO:0000269|PubMed:17991725}. FT /FTId=VAR_025643. FT VARIANT 388 388 P -> L (polymorphism; increases activity FT 2.3 fold; decrease in plasmin-mediated FT proteolytic processing; decrease in FT ability to inhibit nicotine-evoked FT catecholamine secretion in vitro; FT dbSNP:rs9658668). FT {ECO:0000269|PubMed:14740315, FT ECO:0000269|PubMed:15326220, FT ECO:0000269|PubMed:17991725}. FT /FTId=VAR_025644. FT VARIANT 392 392 R -> Q (polymorphism; no effect on FT plasmin-mediated proteolytic processing; FT decrease in ability to inhibit nicotine- FT evoked catecholamine secretion in vitro). FT {ECO:0000269|PubMed:15326220, FT ECO:0000269|PubMed:17991725}. FT /FTId=VAR_072687. FT VARIANT 399 399 R -> W (in dbSNP:rs729940). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:2445752, FT ECO:0000269|PubMed:8120054}. FT /FTId=VAR_025645. FT CONFLICT 41 41 S -> Y (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 54 54 Q -> K (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 87 87 A -> R (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 119 119 E -> Q (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 167 167 N -> K (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 200 200 E -> K (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 219 219 A -> V (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 339 340 SK -> TN (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 370 370 S -> R (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 373 373 K -> R (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 380 380 A -> G (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 394 394 W -> S (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 397 397 S -> N (in Ref. 1; AAA52018). FT {ECO:0000305}. FT CONFLICT 416 416 E -> Q (in Ref. 1; AAA52018). FT {ECO:0000305}. FT STRAND 380 383 {ECO:0000244|PDB:1LV4}. FT STRAND 385 387 {ECO:0000244|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 //