SCG3_MOUSE
ID SCG3_MOUSE Reviewed; 471 AA.
AC P47867; Q3UTT1; Q3UZT8; Q8R1D7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Secretogranin-3;
DE AltName: Full=Secretogranin III;
DE Short=SgIII;
DE Flags: Precursor;
GN Name=Scg3;
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] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Embryonic spinal cord, Inner ear, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [5]
RP INTERACTION WITH CHGA, SUBCELLULAR LOCATION, AND 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 [6]
RP FUNCTION, INTERACTION WITH CPE, AND SUBCELLULAR LOCATION.
RX PubMed=16219686; DOI=10.1242/jcs.02608;
RA Hosaka M., Watanabe T., Sakai Y., Kato T., Takeuchi T.;
RT "Interaction between secretogranin III and carboxypeptidase E facilitates
RT prohormone sorting within secretory granules.";
RL J. Cell Sci. 118:4785-4795(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17200173; DOI=10.1210/jc.2006-1808;
RA Tanabe A., Yanagiya T., Iida A., Saito S., Sekine A., Takahashi A.,
RA Nakamura T., Tsunoda T., Kamohara S., Nakata Y., Kotani K., Komatsu R.,
RA Itoh N., Mineo I., Wada J., Funahashi T., Miyazaki S., Tokunaga K.,
RA Hamaguchi K., Shimada T., Tanaka K., Yamada K., Hanafusa T., Oikawa S.,
RA Yoshimatsu H., Sakata T., Matsuzawa Y., Kamatani N., Nakamura Y., Hotta K.;
RT "Functional single-nucleotide polymorphisms in the secretogranin III (SCG3)
RT gene that form secretory granules with appetite-related neuropeptides are
RT associated with obesity.";
RL J. Clin. Endocrinol. Metab. 92:1145-1154(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-365, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
RN [9]
RP FUNCTION.
RX PubMed=28330905; DOI=10.1084/jem.20161802;
RA LeBlanc M.E., Wang W., Chen X., Caberoy N.B., Guo F., Shen C., Ji Y.,
RA Tian H., Wang H., Chen R., Li W.;
RT "Secretogranin III as a disease-associated ligand for antiangiogenic
RT therapy of diabetic retinopathy.";
RL J. Exp. Med. 214:1029-1047(2017).
CC -!- FUNCTION: Member of the granin protein family that regulates the
CC biogenesis of secretory granules (PubMed:16219686). Acts as a sorting
CC receptor for intragranular proteins including chromogranin A/CHGA
CC (PubMed:12388744). May also play a role in angiogenesis
CC (PubMed:28330905). 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:16219686, ECO:0000269|PubMed:28330905}.
CC -!- SUBUNIT: Interacts with CHGA (PubMed:12388744). Interacts with
CC secretogranin II/SCG2 (By similarity). Interacts (via C-terminus) with
CC CPE (PubMed:16219686). {ECO:0000250|UniProtKB:Q8WXD2,
CC ECO:0000269|PubMed:12388744, ECO:0000269|PubMed:16219686}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000269|PubMed:12388744, ECO:0000269|PubMed:16219686}. Cytoplasmic
CC vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:P47868};
CC Peripheral membrane protein {ECO:0000250}. Secreted
CC {ECO:0000269|PubMed:12388744}. Note=Associated with the secretory
CC granule membrane through direct binding to cholesterol-enriched lipid
CC rafts. {ECO:0000250|UniProtKB:P47868}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P47867-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P47867-2; Sequence=VSP_042877;
CC -!- TISSUE SPECIFICITY: Expressed in various brain areas, with highest
CC levels in the arcuate nucleus and the lateral hypothalamic area, as
CC well as the paraventricular nucleus and the ventromedial hypothalamus
CC (at protein level). {ECO:0000269|PubMed:17200173}.
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DR EMBL; U02982; AAA56636.1; -; mRNA.
DR EMBL; AK133655; BAE21767.1; -; mRNA.
DR EMBL; AK139140; BAE23899.1; -; mRNA.
DR EMBL; AK158315; BAE34456.1; -; mRNA.
DR EMBL; AK164089; BAE37620.1; -; mRNA.
DR EMBL; CH466522; EDL26334.1; -; Genomic_DNA.
DR EMBL; BC024785; AAH24785.1; -; mRNA.
DR CCDS; CCDS23347.1; -. [P47867-1]
DR CCDS; CCDS90627.1; -. [P47867-2]
DR RefSeq; NP_001158262.1; NM_001164790.1. [P47867-2]
DR RefSeq; NP_033156.1; NM_009130.3. [P47867-1]
DR AlphaFoldDB; P47867; -.
DR BioGRID; 203091; 2.
DR IntAct; P47867; 1.
DR MINT; P47867; -.
DR STRING; 10090.ENSMUSP00000034699; -.
DR GlyConnect; 2690; 1 N-Linked glycan (1 site).
DR GlyGen; P47867; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; P47867; -.
DR PhosphoSitePlus; P47867; -.
DR CPTAC; non-CPTAC-3875; -.
DR PaxDb; P47867; -.
DR PeptideAtlas; P47867; -.
DR PRIDE; P47867; -.
DR ProteomicsDB; 256748; -. [P47867-1]
DR ProteomicsDB; 256749; -. [P47867-2]
DR Antibodypedia; 1520; 284 antibodies from 31 providers.
DR DNASU; 20255; -.
DR Ensembl; ENSMUST00000034699; ENSMUSP00000034699; ENSMUSG00000032181. [P47867-1]
DR Ensembl; ENSMUST00000213324; ENSMUSP00000149561; ENSMUSG00000032181. [P47867-2]
DR GeneID; 20255; -.
DR KEGG; mmu:20255; -.
DR UCSC; uc009qss.2; mouse. [P47867-1]
DR UCSC; uc009qst.2; mouse. [P47867-2]
DR CTD; 29106; -.
DR MGI; MGI:103032; Scg3.
DR VEuPathDB; HostDB:ENSMUSG00000032181; -.
DR eggNOG; ENOG502QUJH; Eukaryota.
DR GeneTree; ENSGT00390000005488; -.
DR HOGENOM; CLU_031198_1_0_1; -.
DR InParanoid; P47867; -.
DR OMA; MEKEYEI; -.
DR OrthoDB; 692526at2759; -.
DR PhylomeDB; P47867; -.
DR TreeFam; TF331266; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
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; 20255; 3 hits in 72 CRISPR screens.
DR PRO; PR:P47867; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P47867; protein.
DR Bgee; ENSMUSG00000032181; Expressed in cerebellar nuclear complex and 193 other tissues.
DR ExpressionAtlas; P47867; baseline and differential.
DR Genevisible; P47867; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030667; C:secretory granule membrane; IDA:MGI.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033366; P:protein localization to secretory granule; IDA:MGI.
DR InterPro; IPR026197; SCG3.
DR PANTHER; PTHR17388; PTHR17388; 1.
DR Pfam; PF15467; SGIII; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues;
KW Cytoplasmic vesicle; Membrane; Phosphoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..471
FT /note="Secretogranin-3"
FT /id="PRO_0000005462"
FT REGION 24..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..398
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:21183079"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 355..360
FT /note="SKLFPA -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_042877"
SQ SEQUENCE 471 AA; 53326 MW; FC1E9C381AFCA564 CRC64;
MGFLWTGSWI LVLVLNSGPI QAFPKPEGSQ DKSLHNRELS AERPLNEQIA EAEADKIKKA
FPSESKPSES NYSSVDNLNL LRAITEKETV EKERQSIRSP PFDNQLNVED ADSTKNRKLI
DEYDSTKSGL DHKFQDDPDG LHQLDGTPLT AEDIVHKIAT RIYEENDRGV FDKIVSKLLN
LGLITESQAH TLEDEVAEAL QKLISKEANN YEETLDKPTS RTENQDGKIP EKVTPVAAVQ
DGFTNRENDE TVSNTLTLSN GLERRTNPHR EDDFEELQYF PNFYALLTSI DSEKEAKEKE
TLITIMKTLI DFVKMMVKYG TISPEEGVSY LENLDETIAL QTKNKLEKNT TDSKSKLFPA
PPEKSQEETD STKEEAAKME KEYGSLKDST KDDNSNLGGK TDEATGKTEA YLEAIRKNIE
WLKKHNKKGN KEDYDLSKMR DFINQQADAY VEKGILDKEE ANAIKRIYSS L
