SCG3_RAT
ID SCG3_RAT Reviewed; 471 AA.
AC P47868;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Secretogranin-3;
DE AltName: Full=1B1075;
DE AltName: Full=Secretogranin III;
DE Short=SgIII;
DE Flags: Precursor;
GN Name=Scg3;
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].
RX PubMed=7917832; DOI=10.1007/bf02821554;
RA Dopazo A., Lovenberg T.W., Danielson P.E., Ottiger H.-P., Sutcliffe J.G.;
RT "Primary structure of mouse secretogranin III and its absence from
RT deficient mice.";
RL J. Mol. Neurosci. 4:225-233(1993).
RN [2]
RP PRELIMINARY NUCLEOTIDE SEQUENCE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Brain;
RX PubMed=2204688; DOI=10.1523/jneurosci.10-09-03135.1990;
RA Ottiger H.-P., Battenberg E.F., Tsou A.-P., Bloom F.E., Sutcliffe J.G.;
RT "1B1075: a brain- and pituitary-specific mRNA that encodes a novel
RT chromograNIN / SECretogranin-like component of intracellular vesicles.";
RL J. Neurosci. 10:3135-3147(1990).
RN [3]
RP INTERACTION WITH CHGA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP FUNCTION.
RX PubMed=12388744; DOI=10.1091/mbc.02-03-0040;
RA Hosaka M., Watanabe T., Sakai Y., Uchiyama Y., Takeuchi T.;
RT "Identification of a chromogranin A domain that mediates binding to
RT secretogranin III and targeting to secretory granules in pituitary cells
RT and pancreatic beta-cells.";
RL Mol. Biol. Cell 13:3388-3399(2002).
RN [4]
RP SUBCELLULAR LOCATION, LIPID RAFT-BINDING, AND FUNCTION.
RX PubMed=14597614; DOI=10.1074/jbc.m310104200;
RA Hosaka M., Suda M., Sakai Y., Izumi T., Watanabe T., Takeuchi T.;
RT "Secretogranin III binds to cholesterol in the secretory granule membrane
RT as an adapter for chromogranin A.";
RL J. Biol. Chem. 279:3627-3634(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND IDENTIFICATION BY
RP 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: Member of the granin protein family that regulates the
CC biogenesis of secretory granules (PubMed:12388744, PubMed:14597614).
CC Acts as a sorting receptor for intragranular proteins including
CC chromogranin A/CHGA (PubMed:12388744, PubMed:14597614). May also play a
CC role in angiogenesis. Promotes endothelial proliferation, migration and
CC tube formation through MEK/ERK signaling pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q8WXD2, ECO:0000269|PubMed:12388744,
CC ECO:0000269|PubMed:14597614}.
CC -!- SUBUNIT: Interacts with CHGA (PubMed:12388744). Interacts with
CC secretogranin II/SCG2 (By similarity). Interacts (via C-terminus) with
CC CPE (By similarity). {ECO:0000250|UniProtKB:P47867,
CC ECO:0000250|UniProtKB:Q8WXD2, ECO:0000269|PubMed:12388744}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
CC Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000269|PubMed:14597614}; Peripheral membrane protein. Secreted.
CC Note=Associated with the secretory granule membrane through direct
CC binding to cholesterol-enriched lipid rafts.
CC {ECO:0000269|PubMed:14597614}.
CC -!- TISSUE SPECIFICITY: Expression restricted to the brain and pituitary
CC gland. Not detected in the adrenal gland. {ECO:0000269|PubMed:12388744,
CC ECO:0000269|PubMed:2204688}.
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DR EMBL; U02983; AAA56637.1; -; mRNA.
DR RefSeq; NP_446308.1; NM_053856.2.
DR AlphaFoldDB; P47868; -.
DR SMR; P47868; -.
DR STRING; 10116.ENSRNOP00000014491; -.
DR iPTMnet; P47868; -.
DR PhosphoSitePlus; P47868; -.
DR jPOST; P47868; -.
DR PaxDb; P47868; -.
DR GeneID; 116635; -.
DR KEGG; rno:116635; -.
DR UCSC; RGD:621209; rat.
DR CTD; 29106; -.
DR RGD; 621209; Scg3.
DR eggNOG; ENOG502QUJH; Eukaryota.
DR InParanoid; P47868; -.
DR OrthoDB; 692526at2759; -.
DR PhylomeDB; P47868; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
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:P47868; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; TAS:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030667; C:secretory granule membrane; ISO:RGD.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033366; P:protein localization to secretory granule; ISO:RGD.
DR InterPro; IPR026197; SCG3.
DR PANTHER; PTHR17388; PTHR17388; 1.
DR Pfam; PF15467; SGIII; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Cytoplasmic vesicle; Membrane;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..471
FT /note="Secretogranin-3"
FT /id="PRO_0000005463"
FT REGION 24..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47867"
SQ SEQUENCE 471 AA; 53183 MW; 977B3F8885F33223 CRC64;
MGFLWTGSWI LVLVLNSGPI QAFPKPEGSQ DKSLHNRELS AERPLNEQIA EAEADKIKKT
YPSESKPSES NFSSVDNLNL LKAITEKETV EKAKQSIRSS PFDNRLNVDD ADSTKNRKLT
DEYDSTKSGL DRKVQDDPDG LHQLDGTPLT AEDIVHKIAT RIYEENDRGV FDKIVSKLLN
LGLITESQAH TLEDEVAEAL QKLISKEANN YEEAPEKPTS RTENQDGKIP EKVTPVAATQ
DGFTNRENDD TVSNTLTLSN GLERRTNPHR DDDFEELQYF PNFYALLTSI DSEKEAKEKE
TLITIMKTLI DFVKMMVKYG TISPEEGVSY LENLDETIAL QTKNKLEKNT TDSKSKLFPA
PPEKSHEETD STKEEAAKME KEYGSLKDST KDDNSNLGGK TDEAKGKTEA YLEAIRKNIE
WLKKHNKKGN KEDYDLSKMR DFINQQADAY VEKGILDKEE ANAIKRIYSS L
