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}.
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 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 Genevisible; P10645; HS.
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.
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
//
