SCG1_BOVIN
ID SCG1_BOVIN Reviewed; 646 AA.
AC P23389; O02707;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Secretogranin-1;
DE AltName: Full=Chromogranin-B;
DE Short=CgB;
DE AltName: Full=Secretogranin I;
DE Short=SgI;
DE Contains:
DE RecName: Full=PE-11;
DE Contains:
DE RecName: Full=Secretogranin-1(476-566);
DE Contains:
DE RecName: Full=Peptide BAM-1745;
DE Contains:
DE RecName: Full=Secretolytin;
DE Contains:
DE RecName: Full=CCB peptide;
DE Flags: Precursor;
GN Name=CHGB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-597.
RC TISSUE=Adrenal chromaffin;
RX PubMed=2025642; DOI=10.1016/0167-4781(91)90094-3;
RA Bauer J.W., Fischer-Colbrie R.;
RT "Primary structure of bovine chromogranin B deduced from cDNA sequence.";
RL Biochim. Biophys. Acta 1089:124-126(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal medulla;
RX PubMed=9136897; DOI=10.1016/s0014-5793(97)00276-7;
RA Yoo S.H., Kang Y.K.;
RT "Identification of the secretory vesicle membrane binding region of
RT chromogranin B.";
RL FEBS Lett. 406:259-262(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-646.
RC TISSUE=Adrenal medulla;
RX PubMed=1350945; DOI=10.1007/bf00713372;
RA Grandy D.K., Leduc R., Makam H., Flanagan T., Diliberto E.J., Civelli O.,
RA Viveros O.H.;
RT "Nucleotide and deduced amino acid sequence of bovine adrenal medulla
RT chromogranin B (secretogranin I).";
RL Cell. Mol. Neurobiol. 12:185-192(1992).
RN [4]
RP PROTEIN SEQUENCE OF 239-244 AND 562-565, AND SUBCELLULAR LOCATION.
RX PubMed=8218367; DOI=10.1016/0167-4889(93)90078-4;
RA Yoo S.H.;
RT "pH-dependent binding of chromogranin B and secretory vesicle matrix
RT proteins to the vesicle membrane.";
RL Biochim. Biophys. Acta 1179:239-246(1993).
RN [5]
RP PROTEIN SEQUENCE OF 567-580, AND MASS SPECTROMETRY.
RX PubMed=1554736; DOI=10.1016/0167-4838(92)90430-l;
RA Dillen L., Boel S., De Potter W.P., Claeys M.;
RT "Mass spectrometric characterization of bovine chromaffin granule peptides
RT related to chromogranin B.";
RL Biochim. Biophys. Acta 1120:105-112(1992).
RN [6]
RP PROTEIN SEQUENCE OF 567-580, AND PYROGLUTAMATE FORMATION AT GLN-567.
RX PubMed=1982622; DOI=10.1007/bf00712845;
RA Flanagan T., Taylor L., Poulter L., Viveros O.H., Diliberto E.J. Jr.;
RT "A novel 1745-dalton pyroglutamyl peptide derived from chromogranin B is in
RT the bovine adrenomedullary chromaffin vesicle.";
RL Cell. Mol. Neurobiol. 10:507-523(1990).
RN [7]
RP PROTEIN SEQUENCE OF 21-35; 86-99; 127-145; 146-161; 162-176; 186-194;
RP 235-243; 276-289; 308-314; 340-347; 325-335; 430-444; 584-604 AND 634-646,
RP PYROGLUTAMATE FORMATION AT GLN-634, PROTEOLYTIC PROCESSING, MASS
RP SPECTROMETRY, AND CHARACTERIZATION OF SECRETOLYTIN.
RC TISSUE=Adrenal chromaffin;
RX PubMed=7744058; DOI=10.1111/j.1432-1033.1995.tb20476.x;
RA Strub J.-M., Garcia-Sablone P., Lonning K., Taupenot L., Hubert P.,
RA van Dorsselaer A., Aunis D., Metz-Boutigue M.-H.;
RT "Processing of chromogranin B in bovine adrenal medulla. Identification of
RT secretolytin, the endogenous C-terminal fragment of residues 614-626 with
RT antibacterial activity.";
RL Eur. J. Biochem. 229:356-368(1995).
RN [8]
RP PROTEIN SEQUENCE OF 21-211; 276-289; 300-409; 427-445; 476-516; 530-542;
RP 567-580 AND 584-646, PHOSPHORYLATION AT SER-168; SER-351; SER-354; SER-584;
RP SER-593 AND SER-598, PYROGLUTAMATE FORMATION AT GLN-476 AND GLN-567,
RP SULFATION AT TYR-441 AND TYR-535, GLYCOSYLATION, STRUCTURE OF
RP CARBOHYDRATES, MASS SPECTROMETRY, AND VARIANT VAL-597.
RX PubMed=15174145; DOI=10.1002/pmic.200300693;
RA Gasnier C., Lugardon K., Ruh O., Strub J.-M., Aunis D., Metz-Boutigue M.H.;
RT "Characterization and location of post-translational modifications on
RT chromogranin B from bovine adrenal medullary chromaffin granules.";
RL Proteomics 4:1789-1801(2004).
RN [9]
RP CHARACTERIZATION OF SECRETOLYTIN.
RX PubMed=8603705; DOI=10.1016/0014-5793(95)01529-9;
RA Strub J.-M., Hubert P., Nullans G., Aunis D., Metz-Boutigue M.-H.;
RT "Antibacterial activity of secretolytin, a chromogranin B-derived peptide
RT (614-626), is correlated with peptide structure.";
RL FEBS Lett. 379:273-278(1996).
CC -!- FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule
CC protein, which may be the precursor for other biologically active
CC peptides. The 16 pairs of basic AA distributed throughout its sequence
CC may be used as proteolytic cleavage sites.
CC -!- FUNCTION: Secretolytin has antibacterial activity.
CC -!- SUBCELLULAR LOCATION: [Secretogranin-1]: Cytoplasmic vesicle, secretory
CC vesicle membrane; Peripheral membrane protein; Lumenal side.
CC Note=Neuroendocrine and endocrine secretory granules. Found to be
CC membrane bound inside the secretory vesicles. The N-terminal region
CC exhibits pH-dependent membrane-binding activity, binds to the membrane
CC at intravesicular pH (5.5) and freed when the pH is near to
CC physiological pH.
CC -!- SUBCELLULAR LOCATION: [Peptide BAM-1745]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Secretolytin]: Secreted.
CC -!- PTM: O-glycosylated by the trisaccharide, GalNAc-Gal-NeuAc, on 2 sites
CC in the N-terminal. May be glycated. {ECO:0000269|PubMed:15174145}.
CC -!- PTM: Extensively phosphorylated. {ECO:0000269|PubMed:15174145}.
CC -!- PTM: Differentially processed on numerous sites throughout the sequence
CC depending on tissue type. {ECO:0000269|PubMed:7744058}.
CC -!- MASS SPECTROMETRY: [Peptide BAM-1745]: Mass=1746; Method=MALDI;
CC Note=Pyroglutamate.; Evidence={ECO:0000269|PubMed:15174145};
CC -!- MASS SPECTROMETRY: [Peptide BAM-1745]: Mass=1746; Method=FAB;
CC Note=Pyroglutamate.; Evidence={ECO:0000269|PubMed:1554736};
CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC {ECO:0000305}.
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DR EMBL; X55027; CAA38846.1; -; mRNA.
DR EMBL; U88551; AAC48720.1; -; mRNA.
DR EMBL; X55489; CAA39109.1; -; mRNA.
DR PIR; S15901; S15901.
DR RefSeq; NP_851349.1; NM_181006.2.
DR AlphaFoldDB; P23389; -.
DR MINT; P23389; -.
DR STRING; 9913.ENSBTAP00000015645; -.
DR iPTMnet; P23389; -.
DR PaxDb; P23389; -.
DR PRIDE; P23389; -.
DR GeneID; 281071; -.
DR KEGG; bta:281071; -.
DR CTD; 1114; -.
DR eggNOG; ENOG502QRBF; Eukaryota.
DR HOGENOM; CLU_026095_0_0_1; -.
DR InParanoid; P23389; -.
DR OrthoDB; 670416at2759; -.
DR TreeFam; TF336596; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IEA:InterPro.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR001819; Chromogranin_AB.
DR InterPro; IPR018054; Chromogranin_CS.
DR InterPro; IPR001990; Granin.
DR PANTHER; PTHR10583; PTHR10583; 1.
DR Pfam; PF01271; Granin; 1.
DR PRINTS; PR00659; CHROMOGRANIN.
DR PROSITE; PS00422; GRANINS_1; 1.
DR PROSITE; PS00423; GRANINS_2; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal; Sulfation.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:15174145,
FT ECO:0000269|PubMed:7744058"
FT CHAIN 21..646
FT /note="Secretogranin-1"
FT /id="PRO_0000005434"
FT CHAIN 476..566
FT /note="Secretogranin-1(476-566)"
FT /id="PRO_0000326263"
FT PEPTIDE 544..554
FT /note="PE-11"
FT /evidence="ECO:0000250|UniProtKB:P16014"
FT /id="PRO_0000432729"
FT PEPTIDE 567..580
FT /note="Peptide BAM-1745"
FT /id="PRO_0000005436"
FT PEPTIDE 584..646
FT /note="CCB peptide"
FT /id="PRO_0000411987"
FT PEPTIDE 634..646
FT /note="Secretolytin"
FT /id="PRO_0000005437"
FT REGION 67..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 161..162
FT /note="Cleavage; major site"
FT SITE 275..276
FT /note="Cleavage; major site"
FT SITE 278..279
FT /note="Cleavage; major site"
FT SITE 324..325
FT /note="Cleavage; major site"
FT SITE 629..630
FT /note="Cleavage; major site"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35314"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000305"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15174145"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16014"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 315
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35314"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15174145"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15174145"
FT MOD_RES 374
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060, ECO:0000255"
FT MOD_RES 441
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305|PubMed:15174145"
FT MOD_RES 476
FT /note="Pyrrolidone carboxylic acid; in secretogranin-1(476-
FT 566)"
FT /evidence="ECO:0000269|PubMed:15174145"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 535
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000305|PubMed:15174145"
FT MOD_RES 567
FT /note="Pyrrolidone carboxylic acid; in peptide BAM-1745"
FT /evidence="ECO:0000269|PubMed:15174145,
FT ECO:0000269|PubMed:1982622"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15174145"
FT MOD_RES 591
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35314"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15174145"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15174145"
FT MOD_RES 634
FT /note="Pyrrolidone carboxylic acid; in Secretolytin;
FT partial"
FT /evidence="ECO:0000269|PubMed:7744058"
FT CARBOHYD 113
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305|PubMed:15174145"
FT CARBOHYD 190
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305|PubMed:15174145"
FT DISULFID 36..57
FT /evidence="ECO:0000250"
FT VARIANT 597
FT /note="M -> V"
FT /evidence="ECO:0000269|PubMed:15174145,
FT ECO:0000269|PubMed:2025642"
FT CONFLICT 64
FT /note="N -> S (in Ref. 1; CAA38846)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="N -> D (in Ref. 2; AAC48720)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..98
FT /note="SEAPGL -> FRSPRAS (in Ref. 3; CAA39109)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="T -> M (in Ref. 2; AAC48720)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="H -> R (in Ref. 2; AAC48720)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="P -> R (in Ref. 2; AAC48720)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="H -> L (in Ref. 3; CAA39109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 73340 MW; 420DB1178FD9E415 CRC64;
MQPAALLGLL GATVVAAVSS MPVDIRNHNE EVVTHCIIEV LSNALLKSSA PPITPECRQV
LKKNGKELKN EEKSENENTR FEVRLLRDPA DTSEAPGLSS REDSGEGDAQ VPTVADTESG
GHSRERAGEP PGSQVAKEAK TRYSKSEGQN REEEMVKYQK RERGEVGSEE RLSEGPGKAQ
TAFLNQRNQT PAKKEELVSR YDTQSARGLE KSHSRERSSQ ESGEETKSQE NWPQELQRHP
EGQEAPGESE EDASPEVDKR HSRPRHHHGR SRPDRSSQEG NPPLEEESHV GTGNSDEEKA
RHPAHFRALE EGAEYGEEVR RHSAAQAPGD LQGARFGGRG RGEHQALRRP SEESLEQENK
RHGLSPDLNM AQGYSEESEE ERGPAPGPSY RARGGEAAAY STLGQTDEKR FLGETHHRVQ
ESQRDKARRR LPGELRNYLD YGEEKGEEAA RGKWQPQGDP RDADENREEA RLRGKQYAPH
HITEKRLGEL LNPFYDPSQW KSSRFERKDP MDDSFLEGEE ENGLTLNEKN FFPEYNYDWW
EKKPFEEDVN WGYEKRNPVP KLDLKRQYDR VAELDQLLHY RKKSAEFPDF YDSEEQMSPQ
HTAENEEEKA GQGVLTEEEE KELENLAAMD LELQKIAEKF SGTRRG
