SCG1_PIG
ID SCG1_PIG Reviewed; 668 AA.
AC Q9GLG4;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=Peptide SR-17;
DE Contains:
DE RecName: Full=Peptide HQ-34;
DE Contains:
DE RecName: Full=Peptide KR-11;
DE Contains:
DE RecName: Full=CCB peptide;
DE Flags: Precursor;
GN Name=CHGB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000312|EMBL:AAG13399.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 342-356; 475-492 AND
RP 606-668, MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-615 AND SER-620.
RC TISSUE=Adrenal medulla;
RX PubMed=11168356; DOI=10.1046/j.1432-1033.2001.01864.x;
RA Wang Z., Vandenberghe I., Depreitere J., Devreese B., Clerens S.,
RA Nouwen E.J., Van Beeumen J., De Potter W.;
RT "Identification and characterization of novel chromogranin B-derived
RT peptides from porcine chromaffin granules by liquid
RT chromatography/electrospray tandem MS.";
RL Eur. J. Biochem. 268:235-242(2001).
CC -!- FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule
CC protein, which may be the precursor for other biologically active
CC peptides.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC secretory granules.
CC -!- PTM: Peptide SR-17 exists in both monophosphorylated and
CC diphosphorylated forms. {ECO:0000269|PubMed:11168356}.
CC -!- MASS SPECTROMETRY: [Peptide SR-17]: Mass=2034.04; Method=Electrospray;
CC Note=With 1 phosphate group.; Evidence={ECO:0000269|PubMed:11168356};
CC -!- MASS SPECTROMETRY: [Peptide SR-17]: Mass=2115.42; Method=Electrospray;
CC Note=With 2 phosphate groups.; Evidence={ECO:0000269|PubMed:11168356};
CC -!- MASS SPECTROMETRY: [Peptide HQ-34]: Mass=3815.56; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11168356};
CC -!- MASS SPECTROMETRY: [Peptide KR-11]: Mass=1305.34; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11168356};
CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC {ECO:0000305}.
CC -!- CAUTION: PubMed:11168356 reported the oxidation of Met-651 to
CC sulfoxide. This is most probably an artifact of isolation.
CC {ECO:0000305}.
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DR EMBL; AF284349; AAG13399.1; -; mRNA.
DR AlphaFoldDB; Q9GLG4; -.
DR STRING; 9823.ENSSSCP00000007507; -.
DR iPTMnet; Q9GLG4; -.
DR PaxDb; Q9GLG4; -.
DR PRIDE; Q9GLG4; -.
DR Ensembl; ENSSSCT00040071128; ENSSSCP00040030327; ENSSSCG00040052597.
DR Ensembl; ENSSSCT00045063331; ENSSSCP00045044656; ENSSSCG00045036764.
DR Ensembl; ENSSSCT00055056131; ENSSSCP00055044839; ENSSSCG00055028282.
DR eggNOG; ENOG502QRBF; Eukaryota.
DR InParanoid; Q9GLG4; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; NAS:UniProtKB.
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; Direct protein sequencing;
KW Disulfide bond; Phosphoprotein; Reference proteome; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..668
FT /note="Secretogranin-1"
FT /id="PRO_0000005442"
FT PEPTIDE 566..576
FT /note="PE-11"
FT /evidence="ECO:0000250|UniProtKB:P16014"
FT /id="PRO_0000432732"
FT PEPTIDE 606..668
FT /note="CCB peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000411989"
FT PEPTIDE 606..622
FT /note="Peptide SR-17"
FT /id="PRO_0000005443"
FT PEPTIDE 623..656
FT /note="Peptide HQ-34"
FT /id="PRO_0000005444"
FT PEPTIDE 657..667
FT /note="Peptide KR-11"
FT /id="PRO_0000005445"
FT REGION 64..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16014"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060, ECO:0000255"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 557
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT MOD_RES 613
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35314"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11168356"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11168356"
FT DISULFID 36..57
FT /evidence="ECO:0000250"
SQ SEQUENCE 668 AA; 74392 MW; BC8694D09388D5E8 CRC64;
MQPAVLLGFL GATVVAAVSS MPVDNRNHNE EMVAHCIIEV LSNALSKSNA PPITPECRQV
LKKGGKEVKD EEKGANENTR FEVRLLRDPA DTSETQRPSG GREGAEAPSE DTQGPPGADV
EGGGHSREGA GKPRGGPYSS DNPVAKEGKT RHSEKSEGQD REEEEGEKYQ KRERGEEGSE
ERHLQEPGET QTAFLNQGNR ATAKKKEEFE SRYDAHSAGG PAKTHSRERS SQESGEETGS
QDAAPGEPES PPEGQEAPEE SQEDASLEVD KRRWRPRHHH GRSRPDRAPQ EGSPPPEERG
HPREESEESV LGLASPGGQR TRHPTHYPAS EEEAEHGEEV RSSSSVQAPG DLVGARYGGR
GGAEHRAARR PGEESPEQDR RVGASSELRN KGPGHSEESE EERGDEGQRH HRAWAGGPRA
DAPPDPAEEE QFWGEAHRPV PESQVDEARR HPQAKLRNYL NRGEENGEEG APGRWQQPED
LQGPGEHAAE ARLPGKPYAA HRIPEKKRLG ELLNPYYVPP QWESSHFERK DNVGDNFLEG
EDANGVTLNE KTFFPEYSYD WWEKKPFEED VNWGYEERNL APKLDLKRQY DRVAELDQLL
HYRKKSAEFP DFYDSGEHLS PRHAAESEKE RAGQGVLTEE EEKELENLAA MDLELQKIAE
KFSGNRRG
