ID CMGA_HUMAN STANDARD; PRT; 457 AA. AC P10645; Q96E84; Q96GL7; Q9BQB5; DT 01-JUL-1989 (Rel. 11, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 01-FEB-2005 (Rel. 46, Last annotation update) DE Chromogranin A precursor (CgA) (Pituitary secretory protein I) (SP-I) DE [Contains: Vasostatin-1 (Vasostatin I); Vasostatin-2 (Vasostatin II); DE EA-92; ES-43; Pancreastatin; SS-18; WA-8; WE-14; LF-19; AL-11; GV-19; DE GR-44; ER-37]. GN Name=CHGA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=88298816; 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 [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=88059106; 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 [3] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Liver; RX MEDLINE=94165095; 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. RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP PROTEIN SEQUENCE OF 19-46. RC TISSUE=Adrenal gland; RX MEDLINE=86206941; 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. 13:207-233(1986). RN [7] RP PROTEIN SEQUENCE OF 134-319. RC TISSUE=Pancreas; RX MEDLINE=90336639; PubMed=2165909; 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 [8] RP PROTEIN SEQUENCE OF 291-319. RC TISSUE=Pancreas; RX MEDLINE=88137586; 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 [9] RP PROTEIN SEQUENCE OF 342-355. RX MEDLINE=92249591; 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 [10] RP PROTEIN SEQUENCE OF DERIVED PEPTIDES. RX MEDLINE=22329543; 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 [11] RP CARBOHYDRATE-LINKAGE SITES THR-181; THR-183 AND THR-251, AND RP PHOSPHORYLATION SITES SER-218; SER-270 AND SER-333. RX MEDLINE=99069397; 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 [12] RP PHOSPHORYLATION SITE 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). CC -!- FUNCTION: Pancreastatin strongly inhibits glucose induced insulin CC release from the pancreas. CC -!- SUBCELLULAR LOCATION: Neuroendocrine and endocrine secretory CC granules. CC -!- PTM: Sulfated on tyrosine residues and/or contains sulfated CC glycans. CC -!- MISCELLANEOUS: Binds calcium with a low-affinity. CC -!- SIMILARITY: Belongs to the chromogranin / secretogranin protein CC family. 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; J03915; AAA52018.1; -. DR EMBL; J03483; AAA52017.1; -. DR EMBL; U03749; AAB53685.1; -. DR EMBL; U03742; AAB53685.1; JOINED. DR EMBL; U03743; AAB53685.1; JOINED. DR EMBL; U03744; AAB53685.1; JOINED. DR EMBL; U03748; AAB53685.1; JOINED. DR EMBL; U03745; AAB53685.1; JOINED. DR EMBL; U03746; AAB53685.1; JOINED. DR EMBL; U03747; AAB53685.1; JOINED. DR EMBL; BC001059; AAH01059.1; -. DR EMBL; BC006459; AAH06459.1; -. DR EMBL; BC009384; AAH09384.2; -. DR EMBL; BC012755; AAH12755.2; -. DR PIR; A54376; A28468. DR PDB; 1LV4; NMR; A=370-390. DR GlycoSuiteDB; P10645; -. DR Ensembl; ENSG00000100604; Homo sapiens. DR Genew; HGNC:1929; CHGA. DR MIM; 118910; -. DR GO; GO:0008217; P:regulation of blood pressure; TAS. DR InterPro; IPR001819; Chromogranin_AB. DR InterPro; IPR001990; Granin. DR Pfam; PF01271; Granin; 1. DR PRINTS; PR00659; CHROMOGRANIN. DR PROSITE; PS00422; GRANINS_1; 1. DR PROSITE; PS00423; GRANINS_2; 1. KW 3D-structure; Amidation; Calcium-binding; Direct protein sequencing; KW Glycoprotein; Phosphorylation; Signal; Sulfation. FT SIGNAL 1 18 FT CHAIN 19 457 Chromogranin A. FT PEPTIDE 19 94 Vasostatin-1. FT PEPTIDE 19 131 Vasostatin-2. FT PEPTIDE 134 225 EA-92. FT PEPTIDE 228 260 ES-43. FT PEPTIDE 272 319 Pancreastatin. FT PEPTIDE 322 339 SS-18. FT PEPTIDE 342 349 WA-8. FT PEPTIDE 342 355 WE-14. FT PEPTIDE 358 376 LF-19. FT PEPTIDE 380 390 AL-11. FT PEPTIDE 393 411 GV-19. FT PEPTIDE 413 456 GR-44. FT PEPTIDE 420 456 ER-37. FT DISULFID 35 56 By similarity. FT MOD_RES 218 218 Phosphoserine. FT MOD_RES 270 270 Phosphoserine. FT MOD_RES 322 322 Phosphoserine. FT MOD_RES 333 333 Phosphoserine. FT MOD_RES 319 319 Glycine amide (G-320 provides amide FT group). FT MOD_RES 456 456 Arginine amide (G-457 provides amide FT group). FT CARBOHYD 181 181 O-linked (GalNAc...). FT /FTId=CAR_000116. FT CARBOHYD 183 183 O-linked (GalNAc...). FT /FTId=CAR_000117. FT CARBOHYD 251 251 O-linked (GalNAc...). FT /FTId=CAR_000118. FT CONFLICT 41 41 S -> Y (in Ref. 1). FT CONFLICT 54 54 Q -> K (in Ref. 1). FT CONFLICT 87 87 A -> R (in Ref. 1). FT CONFLICT 119 119 E -> Q (in Ref. 1). FT CONFLICT 167 167 N -> K (in Ref. 1). FT CONFLICT 200 200 E -> K (in Ref. 1). FT CONFLICT 219 219 A -> V (in Ref. 1). FT CONFLICT 339 340 SK -> TN (in Ref. 1). FT CONFLICT 370 370 S -> R (in Ref. 1). FT CONFLICT 373 373 K -> R (in Ref. 1). FT CONFLICT 380 380 A -> G (in Ref. 1). FT CONFLICT 394 394 W -> S (in Ref. 1). FT CONFLICT 397 397 S -> N (in Ref. 1). FT CONFLICT 398 398 R -> S (in Ref. 1 and 5). FT CONFLICT 399 399 E -> R (in Ref. 5). FT CONFLICT 399 399 E -> W (in Ref. 1). FT CONFLICT 416 416 E -> Q (in Ref. 1). SQ SEQUENCE 457 AA; 50730 MW; 2F63590C82E81DB0 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 RRGWRPSREE DSLEAGLPLQ VRGYPEEKKE EEGSANRRPE DQELESLSAI EAELEKVAHQ LQALRRG //