SCG1_MOUSE
ID SCG1_MOUSE Reviewed; 677 AA.
AC P16014;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 165.
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=CCB peptide;
DE Contains:
DE RecName: Full=PE-11;
DE Flags: Precursor;
GN Name=Chgb; Synonyms=Scg-1, Scg1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=2320426; DOI=10.1093/nar/18.5.1298;
RA Linard C.G., Mbikay M., Seidah N.G., Chretien M.;
RT "Primary structure of mouse chromogranin B deduced from cDNA sequence.";
RL Nucleic Acids Res. 18:1298-1298(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2335203; DOI=10.1016/0014-5793(90)80194-n;
RA Pohl T.M., Phillips E., Song K., Gerdes H.-H., Huttner W.B., Ruether U.;
RT "The organisation of the mouse chromogranin B (secretogranin I) gene.";
RL FEBS Lett. 262:219-224(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [4]
RP CHARACTERIZATION OF PE-11.
RX PubMed=9422384; DOI=10.1046/j.1471-4159.1998.70010374.x;
RA Laslop A., Weiss C., Savaria D., Eiter C., Tooze S.A., Seidah N.G.,
RA Winkler H.;
RT "Proteolytic processing of chromogranin B and secretogranin II by
RT prohormone convertases.";
RL J. Neurochem. 70:374-383(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-342; SER-493 AND
RP SER-626, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule
CC protein, which may be the precursor for other biologically active
CC peptides.
CC -!- INTERACTION:
CC P16014; P00441: SOD1; Xeno; NbExp=6; IntAct=EBI-990820, EBI-990792;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC secretory granules.
CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC {ECO:0000305}.
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DR EMBL; X53028; CAA37199.1; -; mRNA.
DR EMBL; X51429; CAA35792.1; -; mRNA.
DR EMBL; BC014736; AAH14736.1; -; mRNA.
DR CCDS; CCDS16777.1; -.
DR PIR; S09078; S09078.
DR RefSeq; NP_031720.1; NM_007694.4.
DR AlphaFoldDB; P16014; -.
DR BioGRID; 198697; 7.
DR IntAct; P16014; 2.
DR STRING; 10090.ENSMUSP00000028826; -.
DR GlyGen; P16014; 1 site.
DR iPTMnet; P16014; -.
DR PhosphoSitePlus; P16014; -.
DR CPTAC; non-CPTAC-3496; -.
DR PaxDb; P16014; -.
DR PeptideAtlas; P16014; -.
DR PRIDE; P16014; -.
DR ProteomicsDB; 255357; -.
DR Antibodypedia; 2170; 246 antibodies from 33 providers.
DR DNASU; 12653; -.
DR Ensembl; ENSMUST00000028826; ENSMUSP00000028826; ENSMUSG00000027350.
DR GeneID; 12653; -.
DR KEGG; mmu:12653; -.
DR UCSC; uc008mnf.1; mouse.
DR CTD; 1114; -.
DR MGI; MGI:88395; Chgb.
DR VEuPathDB; HostDB:ENSMUSG00000027350; -.
DR eggNOG; ENOG502QRBF; Eukaryota.
DR GeneTree; ENSGT00940000154206; -.
DR HOGENOM; CLU_026095_0_0_1; -.
DR InParanoid; P16014; -.
DR OMA; WGYEKRS; -.
DR OrthoDB; 670416at2759; -.
DR PhylomeDB; P16014; -.
DR TreeFam; TF336596; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 12653; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Chgb; mouse.
DR PRO; PR:P16014; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P16014; protein.
DR Bgee; ENSMUSG00000027350; Expressed in superior cervical ganglion and 163 other tissues.
DR ExpressionAtlas; P16014; baseline and differential.
DR Genevisible; P16014; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
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; Disulfide bond; Glycoprotein;
KW Phosphoprotein; Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..20
FT CHAIN 21..677
FT /note="Secretogranin-1"
FT /id="PRO_0000005441"
FT PEPTIDE 575..585
FT /note="PE-11"
FT /evidence="ECO:0000305|PubMed:9422384"
FT /id="PRO_0000432731"
FT PEPTIDE 617..677
FT /note="CCB peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000411988"
FT REGION 63..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..278
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35314"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 348
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35314"
FT MOD_RES 365
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 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 472
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 566
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT MOD_RES 624
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35314"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 115
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000305"
FT DISULFID 36..57
FT /evidence="ECO:0000250"
FT CONFLICT 422..424
FT /note="REP -> LGA (in Ref. 1; CAA35792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 677 AA; 77969 MW; C73291E781E4F9B9 CRC64;
MQPAMLLGLL GAAALAAVSS APVDNRDHNE EMVTRCIIEV LSNALSKSSV PTITPECRQV
LKKSGKEVKG EEKGENQNSK FEVRLLRDPA DASGTRWASS REDAGAPVED SQGQTKVGNE
KWTEGGGHSR EGVDDQESLR PSNQQASKEA KIYHSEERVG KEREKEEGKI YPMGEHREDA
GEEKKHIEDS GEKPNTFSNK RSEASAKKKD ESVARADAHS MELEEKTHSR EQSSQESGEE
TRRQEKPQEL TDQDQSQEES QEGEEGEEGE EGEEGEEDSA SEVTKRRPRH HHGRSGSNKS
SYEGHPLSEE RRPSPKESKE ADVATVRLGE KRSHHLAHYR ASEEEPEYGE ESRSYRGLQY
RGRGSEEDRA PRPRSEESQE REYKRNHPDS ELESTANRHG EETEEERSYE GANGRQHRGR
GREPGAHSAL DTREEKRLLD EGHYPVRESP IDTAKRYPQS KWQEQEKNYL NYGEEGDQGR
WWQQEEQLGP EESREEVRFP DRQYEPYPIT EKRKRLGALF NPYFDPLQWK NSDFEKRGNP
DDSFLEDEGE DRNGVTLTEK NSFPEYNYDW WERRPFSEDV NWGYEKRSFA RAPQLDLKRQ
YDGVAELDQL LHYRKKADEF PDFYDSEEQM GPHQEANDEK ARADQRVLTA EEKKELENLA
AMDLELQKIA EKFSQRG
