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Protein

Secretogranin-1

Gene

Chgb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides.

Names & Taxonomyi

Protein namesi
Recommended name:
Secretogranin-1
Alternative name(s):
Chromogranin-B
Short name:
CgB
Glucagonoma peptide
Secretogranin-I
Short name:
SgI
Cleaved into the following 3 chains:
Gene namesi
Name:Chgb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2339. Chgb.

Subcellular locationi

  • Secreted

  • Note: Neuroendocrine and endocrine secretory granules.By similarity

GO - Cellular componenti

  • extracellular region Source: UniProtKB-SubCell
  • secretory granule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 675655Secretogranin-1PRO_0000005446Add
BLAST
Peptidei572 – 58211PE-11By similarityPRO_0000432733Add
BLAST
Peptidei615 – 67561CCB peptide long formPRO_0000411990Add
BLAST
Peptidei615 – 67460CCB peptide short formPRO_0000005447Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 57By similarity
Modified residuei93 – 931PhosphoserineCombined sources
Modified residuei99 – 991PhosphoserineSequence analysis
Modified residuei100 – 1001PhosphoserineSequence analysis
Modified residuei129 – 1291PhosphoserineCombined sources
Modified residuei147 – 1471PhosphoserineCombined sources
Modified residuei171 – 1711SulfotyrosineSequence analysis
Modified residuei190 – 1901PhosphoserineCombined sources
Modified residuei255 – 2551PhosphoserineCombined sources
Modified residuei259 – 2591PhosphoserineCombined sources
Modified residuei291 – 2911PhosphoserineSequence analysis
Modified residuei309 – 3091PhosphoserineBy similarity
Modified residuei333 – 3331PhosphoserineCombined sources
Modified residuei339 – 3391Sulfotyrosine1 Publication
Modified residuei362 – 3621PhosphoserineBy similarity
Modified residuei372 – 3721PhosphoserineBy similarity
Modified residuei375 – 3751PhosphoserineCombined sources
Modified residuei397 – 3971PhosphoserineSequence analysis
Modified residuei466 – 4661SulfotyrosineSequence analysis
Modified residuei469 – 4691SulfotyrosineCurated
Modified residuei490 – 4901PhosphoserineCombined sources
Modified residuei529 – 5291PhosphoserineSequence analysis
Modified residuei540 – 5401PhosphoserineSequence analysis
Modified residuei563 – 5631SulfotyrosineCurated
Modified residuei565 – 5651SulfotyrosineSequence analysis
Modified residuei622 – 6221Sulfotyrosine; partial1 Publication
Modified residuei624 – 6241PhosphoserineCombined sources1 Publication
Modified residuei674 – 6741Arginine amide; in CCB peptide short form1 Publication

Post-translational modificationi

Extensively processed in glucagonoma tissue by limited proteolysis at conserved basic residues. Alternative processing are seen in different tissues. The proglucagon-converting enzymes present in transformed alpha-cells are likely candidates to be involved in tissue-specific processing.

Keywords - PTMi

Amidation, Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, Sulfation

Proteomic databases

PaxDbiO35314.
PRIDEiO35314.

PTM databases

iPTMnetiO35314.
PhosphoSiteiO35314.

Expressioni

Tissue specificityi

Expressed in the brain, adrenal medulla and anterior pituitary. In the brain, localized to the hippocampal formation, the endocrine hypothalamus, the olfactory system, and in anatomically distinct structures in the pons-medulla.1 Publication

Developmental stagei

First expressed in the brain around embryonic days 13-14, and peaks by postnatal day 20.1 Publication

Gene expression databases

GenevisibleiO35314. RN.

Interactioni

Protein-protein interaction databases

IntActiO35314. 1 interaction.
STRINGi10116.ENSRNOP00000028892.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi162 – 1676Poly-Glu

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IVJ3. Eukaryota.
ENOG410ZHMS. LUCA.
GeneTreeiENSGT00730000111312.
HOGENOMiHOG000132984.
HOVERGENiHBG057317.
InParanoidiO35314.
KOiK19991.
OMAiNWGYEKR.
OrthoDBiEOG74N5GF.
PhylomeDBiO35314.
TreeFamiTF336596.

Family and domain databases

InterProiIPR001819. Chromogranin_AB.
IPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]
PANTHERiPTHR10583. PTHR10583. 1 hit.
PfamiPF01271. Granin. 1 hit.
[Graphical view]
PRINTSiPR00659. CHROMOGRANIN.
PROSITEiPS00422. GRANINS_1. 1 hit.
PS00423. GRANINS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35314-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRAMLLGLL GAAALAAVIS APVDNRDHNE EMVTRCIIEV LSNALSKSSA
60 70 80 90 100
PTITPECRQV LRKSGKEVKG EEKGENENSK FEVRLLRDPS DASVGRWASS
110 120 130 140 150
REETGAPVED SPGQAKVDNE EWTGGGGHSR EAVDDQESLH PSNQQVSKEA
160 170 180 190 200
KIRHSEERGG KEEEEEEGKI YPKGEHRGDA GEEKKHTEES GEKHNAFSNK
210 220 230 240 250
RSEASAKKKE ESVARAEAHF VELEKTHSRE QSSQESGEET RRQEKPQELP
260 270 280 290 300
DQDQSEEESE EGEEGEEGAT SEVTKRRPRH HHWRSQSNKP SYEGRRPLSE
310 320 330 340 350
ERKHAAGESK DANVATANLG EKRGHHLAHY RASEEEPDYG EELRSYPGFQ
360 370 380 390 400
APQGLQYQGR GSEEVRAPSP RSEESQEKEY KRNHPDSELE STANRHSEET
410 420 430 440 450
EEERSYEGAK GRQHRGRGRE PGAYPALDSR QEKRLLDEGH DPVHESPVDT
460 470 480 490 500
AKRYPQSKWQ EQEKNYLNYD EEGDQGRWWQ QEEQLEPEES REEVSFPDRQ
510 520 530 540 550
YAPYPTTEKR KRLGALFNPY FDPLQWKNSD FEKKGNPDDS FLDDDGEDGN
560 570 580 590 600
GVTMTEKNFF PEYNYDWWEK RPFSEDVNWG YEKRSFARAP HLDLKRQYDD
610 620 630 640 650
GVAELDQLLH YRKKAAEFPD FYDSEEQMGP HQEAEDEKDR ADQRVLTEEE
660 670
KKELENLAAM DLELQKIAEK FSQRG
Length:675
Mass (Da):77,536
Last modified:February 20, 2007 - v2
Checksum:i042B045B272074FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti358 – 3581Q → R in AAB72089 (PubMed:2641278).Curated
Sequence conflicti461 – 4644EQEK → GQGE in AAB72089 (PubMed:2641278).Curated
Sequence conflicti588 – 5881R → K in AAB72089 (PubMed:2641278).Curated

Mass spectrometryi

Molecular mass is 7270.2446 Da from positions 615 - 675. Determined by MALDI. Sulfated and phosphorylated CCB peptide long form.1 Publication
Molecular mass is 7190.3133 Da from positions 615 - 675. Determined by MALDI. Sulfated or phosphorylated CCB peptide long form.1 Publication
Molecular mass is 7110.2525 Da from positions 615 - 675. Determined by MALDI. CCB peptide long form without any modifications.1 Publication
Molecular mass is 7212.2845 Da from positions 615 - 674. Determined by MALDI. Sulfated and phosphorylated CCB peptide short form.1 Publication
Molecular mass is 7132.2800 Da from positions 615 - 674. Determined by MALDI. Sulfated or phosphorylated CCB peptide short form.1 Publication
Molecular mass is 7052.3410 Da from positions 615 - 674. Determined by MALDI. CCB peptide short form without any modifications.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019974 mRNA. Translation: AAB72089.1.
BC128743 mRNA. Translation: AAI28744.1.
PIRiD49164.
RefSeqiNP_036658.2. NM_012526.2.
UniGeneiRn.11090.

Genome annotation databases

EnsembliENSRNOT00000028892; ENSRNOP00000028892; ENSRNOG00000021269.
GeneIDi24259.
KEGGirno:24259.
UCSCiRGD:2339. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019974 mRNA. Translation: AAB72089.1.
BC128743 mRNA. Translation: AAI28744.1.
PIRiD49164.
RefSeqiNP_036658.2. NM_012526.2.
UniGeneiRn.11090.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35314. 1 interaction.
STRINGi10116.ENSRNOP00000028892.

PTM databases

iPTMnetiO35314.
PhosphoSiteiO35314.

Proteomic databases

PaxDbiO35314.
PRIDEiO35314.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028892; ENSRNOP00000028892; ENSRNOG00000021269.
GeneIDi24259.
KEGGirno:24259.
UCSCiRGD:2339. rat.

Organism-specific databases

CTDi1114.
RGDi2339. Chgb.

Phylogenomic databases

eggNOGiENOG410IVJ3. Eukaryota.
ENOG410ZHMS. LUCA.
GeneTreeiENSGT00730000111312.
HOGENOMiHOG000132984.
HOVERGENiHBG057317.
InParanoidiO35314.
KOiK19991.
OMAiNWGYEKR.
OrthoDBiEOG74N5GF.
PhylomeDBiO35314.
TreeFamiTF336596.

Miscellaneous databases

PROiO35314.

Gene expression databases

GenevisibleiO35314. RN.

Family and domain databases

InterProiIPR001819. Chromogranin_AB.
IPR018054. Chromogranin_CS.
IPR001990. Granin.
[Graphical view]
PANTHERiPTHR10583. PTHR10583. 1 hit.
PfamiPF01271. Granin. 1 hit.
[Graphical view]
PRINTSiPR00659. CHROMOGRANIN.
PROSITEiPS00422. GRANINS_1. 1 hit.
PS00423. GRANINS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence and cellular distribution of rat chromogranin B (secretogranin I) mRNA in the neuroendocrine system."
    Forss-Petter S., Danielson P., Battenberg E., Bloom F., Sutcliffe J.G.
    J. Mol. Neurosci. 1:63-75(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Sprague-Dawley.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Chromogranin-B, a putative precursor of eight novel rat glucagonoma peptides through processing at mono-, di-, or tribasic residues."
    Nielsen E., Welinder B.S., Madsen O.D.
    Endocrinology 129:3147-3156(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Glucagonoma.
  4. "The primary structure of human secretogranin I (chromogranin B): comparison with chromogranin A reveals homologous terminal domains and a large intervening variable region."
    Benedum U.M., Lamouroux A., Konecki D.S., Hille A., Baeuerle P.A., Frank R., Lottspeich F., Mallet J., Huttner W.B.
    EMBO J. 6:1203-1211(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-34; 85-93; 332-339 AND 345-353, SULFATION AT TYR-339.
    Tissue: Pheochromocytoma.
  5. "A sulfated, phosphorylated 7 kDa secreted peptide characterized by direct analysis of cell culture media."
    Taylor S.W., Sun C., Hsieh A., Andon N.L., Ghosh S.S.
    J. Proteome Res. 7:795-802(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: AMIDATION AT ARG-674, SULFATION AT TYR-622, PHOSPHORYLATION AT SER-624, SYNTHESIS OF 615-674, MASS SPECTROMETRY.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-129; SER-147; SER-190; SER-255; SER-259; SER-333; SER-375; SER-490 AND SER-624, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSCG1_RAT
AccessioniPrimary (citable) accession number: O35314
Secondary accession number(s): A1A5N9, Q9QVG8, Q9QVH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: February 20, 2007
Last modified: June 8, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.