SCG1_RAT
ID SCG1_RAT Reviewed; 675 AA.
AC O35314; A1A5N9; Q9QVG8; Q9QVH1;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Secretogranin-1;
DE AltName: Full=Chromogranin-B;
DE Short=CgB;
DE AltName: Full=Glucagonoma peptide;
DE AltName: Full=Secretogranin-I;
DE Short=SgI;
DE Contains:
DE RecName: Full=PE-11;
DE Contains:
DE RecName: Full=CCB peptide short form;
DE Contains:
DE RecName: Full=CCB peptide long form;
DE Flags: Precursor;
GN Name=Chgb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley;
RX PubMed=2641278; DOI=10.1007/bf02896890;
RA Forss-Petter S., Danielson P., Battenberg E., Bloom F., Sutcliffe J.G.;
RT "Nucleotide sequence and cellular distribution of rat chromogranin B
RT (secretogranin I) mRNA in the neuroendocrine system.";
RL J. Mol. Neurosci. 1:63-75(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Glucagonoma;
RX PubMed=1954895; DOI=10.1210/endo-129-6-3147;
RA Nielsen E., Welinder B.S., Madsen O.D.;
RT "Chromogranin-B, a putative precursor of eight novel rat glucagonoma
RT peptides through processing at mono-, di-, or tribasic residues.";
RL Endocrinology 129:3147-3156(1991).
RN [4]
RP PROTEIN SEQUENCE OF 21-34; 85-93; 332-339 AND 345-353, AND SULFATION AT
RP TYR-339.
RC TISSUE=Pheochromocytoma;
RX PubMed=3608978; DOI=10.1002/j.1460-2075.1987.tb02355.x;
RA Benedum U.M., Lamouroux A., Konecki D.S., Hille A., Baeuerle P.A.,
RA Frank R., Lottspeich F., Mallet J., Huttner W.B.;
RT "The primary structure of human secretogranin I (chromogranin B):
RT comparison with chromogranin A reveals homologous terminal domains and a
RT large intervening variable region.";
RL EMBO J. 6:1203-1211(1987).
RN [5]
RP AMIDATION AT ARG-674, SULFATION AT TYR-622, PHOSPHORYLATION AT SER-624,
RP SYNTHESIS OF 615-674, AND MASS SPECTROMETRY.
RX PubMed=18181560; DOI=10.1021/pr7006686;
RA Taylor S.W., Sun C., Hsieh A., Andon N.L., Ghosh S.S.;
RT "A sulfated, phosphorylated 7 kDa secreted peptide characterized by direct
RT analysis of cell culture media.";
RL J. Proteome Res. 7:795-802(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-129; SER-147;
RP SER-190; SER-255; SER-259; SER-333; SER-375; SER-490 AND SER-624, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, adrenal medulla and
CC anterior pituitary. In the brain, localized to the hippocampal
CC formation, the endocrine hypothalamus, the olfactory system, and in
CC anatomically distinct structures in the pons-medulla.
CC {ECO:0000269|PubMed:2641278}.
CC -!- DEVELOPMENTAL STAGE: First expressed in the brain around embryonic days
CC 13-14, and peaks by postnatal day 20. {ECO:0000269|PubMed:2641278}.
CC -!- PTM: Extensively processed in glucagonoma tissue by limited proteolysis
CC at conserved basic residues. Alternative processing are seen in
CC different tissues. The proglucagon-converting enzymes present in
CC transformed alpha-cells are likely candidates to be involved in tissue-
CC specific processing.
CC -!- MASS SPECTROMETRY: [CCB peptide long form]: Mass=7270.2446;
CC Method=MALDI; Note=Sulfated and phosphorylated CCB peptide long form.;
CC Evidence={ECO:0000269|PubMed:18181560};
CC -!- MASS SPECTROMETRY: [CCB peptide long form]: Mass=7190.3133;
CC Method=MALDI; Note=Sulfated or phosphorylated CCB peptide long form.;
CC Evidence={ECO:0000269|PubMed:18181560};
CC -!- MASS SPECTROMETRY: [CCB peptide long form]: Mass=7110.2525;
CC Method=MALDI; Note=CCB peptide long form without any modifications.;
CC Evidence={ECO:0000269|PubMed:18181560};
CC -!- MASS SPECTROMETRY: [CCB peptide short form]: Mass=7212.2845;
CC Method=MALDI; Note=Sulfated and phosphorylated CCB peptide short form.;
CC Evidence={ECO:0000269|PubMed:18181560};
CC -!- MASS SPECTROMETRY: [CCB peptide short form]: Mass=7132.2800;
CC Method=MALDI; Note=Sulfated or phosphorylated CCB peptide short form.;
CC Evidence={ECO:0000269|PubMed:18181560};
CC -!- MASS SPECTROMETRY: [CCB peptide short form]: Mass=7052.3410;
CC Method=MALDI; Note=CCB peptide short form without any modifications.;
CC Evidence={ECO:0000269|PubMed:18181560};
CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC {ECO:0000305}.
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DR EMBL; AF019974; AAB72089.1; -; mRNA.
DR EMBL; BC128743; AAI28744.1; -; mRNA.
DR PIR; D49164; D49164.
DR RefSeq; NP_036658.2; NM_012526.2.
DR AlphaFoldDB; O35314; -.
DR SMR; O35314; -.
DR IntAct; O35314; 2.
DR MINT; O35314; -.
DR STRING; 10116.ENSRNOP00000028892; -.
DR iPTMnet; O35314; -.
DR PhosphoSitePlus; O35314; -.
DR jPOST; O35314; -.
DR PaxDb; O35314; -.
DR PRIDE; O35314; -.
DR GeneID; 24259; -.
DR KEGG; rno:24259; -.
DR UCSC; RGD:2339; rat.
DR CTD; 1114; -.
DR RGD; 2339; Chgb.
DR VEuPathDB; HostDB:ENSRNOG00000021269; -.
DR eggNOG; ENOG502QRBF; Eukaryota.
DR HOGENOM; CLU_026095_0_0_1; -.
DR InParanoid; O35314; -.
DR OMA; WGYEKRS; -.
DR OrthoDB; 670416at2759; -.
DR PhylomeDB; O35314; -.
DR TreeFam; TF336596; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:O35314; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000021269; Expressed in cerebellum and 15 other tissues.
DR Genevisible; O35314; RN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
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 Amidation; 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:0000269|PubMed:3608978"
FT CHAIN 21..675
FT /note="Secretogranin-1"
FT /id="PRO_0000005446"
FT PEPTIDE 572..582
FT /note="PE-11"
FT /evidence="ECO:0000250|UniProtKB:P16014"
FT /id="PRO_0000432733"
FT PEPTIDE 615..675
FT /note="CCB peptide long form"
FT /id="PRO_0000411990"
FT PEPTIDE 615..674
FT /note="CCB peptide short form"
FT /id="PRO_0000005447"
FT REGION 64..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..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 147..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 339
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:3608978"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05060"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 469
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 563
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23389"
FT MOD_RES 622
FT /note="Sulfotyrosine; partial"
FT /evidence="ECO:0000269|PubMed:18181560"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18181560,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 674
FT /note="Arginine amide; in CCB peptide short form"
FT /evidence="ECO:0000269|PubMed:18181560"
FT DISULFID 36..57
FT /evidence="ECO:0000250"
FT CONFLICT 358
FT /note="Q -> R (in Ref. 1; AAB72089)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..464
FT /note="EQEK -> GQGE (in Ref. 1; AAB72089)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="R -> K (in Ref. 1; AAB72089)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 77536 MW; 042B045B272074FC CRC64;
MQRAMLLGLL GAAALAAVIS APVDNRDHNE EMVTRCIIEV LSNALSKSSA PTITPECRQV
LRKSGKEVKG EEKGENENSK FEVRLLRDPS DASVGRWASS REETGAPVED SPGQAKVDNE
EWTGGGGHSR EAVDDQESLH PSNQQVSKEA KIRHSEERGG KEEEEEEGKI YPKGEHRGDA
GEEKKHTEES GEKHNAFSNK RSEASAKKKE ESVARAEAHF VELEKTHSRE QSSQESGEET
RRQEKPQELP DQDQSEEESE EGEEGEEGAT SEVTKRRPRH HHWRSQSNKP SYEGRRPLSE
ERKHAAGESK DANVATANLG EKRGHHLAHY RASEEEPDYG EELRSYPGFQ APQGLQYQGR
GSEEVRAPSP RSEESQEKEY KRNHPDSELE STANRHSEET EEERSYEGAK GRQHRGRGRE
PGAYPALDSR QEKRLLDEGH DPVHESPVDT AKRYPQSKWQ EQEKNYLNYD EEGDQGRWWQ
QEEQLEPEES REEVSFPDRQ YAPYPTTEKR KRLGALFNPY FDPLQWKNSD FEKKGNPDDS
FLDDDGEDGN GVTMTEKNFF PEYNYDWWEK RPFSEDVNWG YEKRSFARAP HLDLKRQYDD
GVAELDQLLH YRKKAAEFPD FYDSEEQMGP HQEAEDEKDR ADQRVLTEEE KKELENLAAM
DLELQKIAEK FSQRG
