SCG2_MOUSE
ID SCG2_MOUSE Reviewed; 617 AA.
AC Q03517; Q80Y79; Q9CW80;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Secretogranin-2;
DE AltName: Full=Chromogranin-C;
DE AltName: Full=Secretogranin II;
DE Short=SgII;
DE Contains:
DE RecName: Full=Secretoneurin;
DE Short=SN;
DE Contains:
DE RecName: Full=Manserin;
DE Flags: Precursor;
GN Name=Scg2; Synonyms=Chgc, Scg-2;
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 [GENOMIC DNA].
RX PubMed=1468571; DOI=10.1016/0014-5793(92)81509-k;
RA Schimmel A., Braeunling O., Ruether U., Huttner W.B., Gerdes H.-H.;
RT "The organisation of the mouse secretogranin II gene.";
RL FEBS Lett. 314:375-380(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-516.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 OF 184-216.
RX PubMed=9654353; DOI=10.1016/s0304-3940(98)00345-0;
RA Leitner B., Schneitler C., Klocker H., Volknandt W., Zimmermann H.,
RA Winkler H., Fischer-Colbrie R.;
RT "Formation and sequence analysis of secretoneurin, a neuropeptide derived
RT from secretogranin II, in mammalian, bird, reptile, amphibian and fish
RT brains.";
RL Neurosci. Lett. 248:105-108(1998).
RN [4]
RP PROTEIN SEQUENCE OF 452-463, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532; SER-555 AND SER-556, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, 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: Neuroendocrine protein of the granin family that regulates
CC the biogenesis of secretory granules. {ECO:0000250|UniProtKB:P13521}.
CC -!- SUBUNIT: Interacts with Secretogranin III/SCG3.
CC {ECO:0000250|UniProtKB:P13521}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC secretory granules.
CC -!- MISCELLANEOUS: Binds calcium with a low-affinity.
CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X68837; CAA48727.1; -; Genomic_DNA.
DR EMBL; AK002953; BAB22476.2; -; mRNA.
DR CCDS; CCDS15089.1; -.
DR PIR; S27389; S27389.
DR RefSeq; NP_033155.1; NM_009129.2.
DR AlphaFoldDB; Q03517; -.
DR SMR; Q03517; -.
DR BioGRID; 203090; 4.
DR STRING; 10090.ENSMUSP00000062556; -.
DR iPTMnet; Q03517; -.
DR PhosphoSitePlus; Q03517; -.
DR EPD; Q03517; -.
DR MaxQB; Q03517; -.
DR PaxDb; Q03517; -.
DR PeptideAtlas; Q03517; -.
DR PRIDE; Q03517; -.
DR ProteomicsDB; 255358; -.
DR Antibodypedia; 2205; 338 antibodies from 34 providers.
DR Ensembl; ENSMUST00000049972; ENSMUSP00000062556; ENSMUSG00000050711.
DR GeneID; 20254; -.
DR KEGG; mmu:20254; -.
DR UCSC; uc007bqr.1; mouse.
DR CTD; 7857; -.
DR MGI; MGI:103033; Scg2.
DR VEuPathDB; HostDB:ENSMUSG00000050711; -.
DR eggNOG; ENOG502QV5W; Eukaryota.
DR GeneTree; ENSGT00390000010895; -.
DR InParanoid; Q03517; -.
DR OMA; KYPEIIN; -.
DR OrthoDB; 587478at2759; -.
DR PhylomeDB; Q03517; -.
DR TreeFam; TF334018; -.
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; 20254; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Scg2; mouse.
DR PRO; PR:Q03517; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q03517; protein.
DR Bgee; ENSMUSG00000050711; Expressed in medial preoptic region and 149 other tissues.
DR ExpressionAtlas; Q03517; baseline and differential.
DR Genevisible; Q03517; MM.
DR GO; GO:0031045; C:dense core granule; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:HGNC-UCL.
DR GO; GO:0098992; C:neuronal dense core vesicle; IDA:SynGO.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0042056; F:chemoattractant activity; ISS:HGNC-UCL.
DR GO; GO:0005125; F:cytokine activity; ISS:HGNC-UCL.
DR GO; GO:0001525; P:angiogenesis; IDA:HGNC-UCL.
DR GO; GO:0048245; P:eosinophil chemotaxis; ISS:HGNC-UCL.
DR GO; GO:0050930; P:induction of positive chemotaxis; ISS:HGNC-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:HGNC-UCL.
DR GO; GO:0000165; P:MAPK cascade; ISS:HGNC-UCL.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISS:HGNC.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0050918; P:positive chemotaxis; ISS:HGNC.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:HGNC-UCL.
DR InterPro; IPR001990; Granin.
DR InterPro; IPR038858; ScgII.
DR PANTHER; PTHR15119; PTHR15119; 1.
DR Pfam; PF01271; Granin; 1.
PE 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT CHAIN 31..617
FT /note="Secretogranin-2"
FT /id="PRO_0000005455"
FT PEPTIDE 184..216
FT /note="Secretoneurin"
FT /id="PRO_0000005456"
FT PEPTIDE 527..566
FT /note="Manserin"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT /id="PRO_0000432737"
FT REGION 261..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 153
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P13521"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 238
FT /note="T -> A (in Ref. 2; BAB22476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 70644 MW; 42D0D5D5546F4BDD CRC64;
MAGAKAYRLG AVLLLIHLIF LISGAEAASF QRNQLLQKEP DLRLENVQKF PSPEMIRALE
YIEKLRQQAH REESSPDYNP YQGVSVPLQL KENGEESHLA ESSRDALSED EWMRIILEAL
RQAENEPPSA PKENKPYALN LEKNFPVDTP DDYETQQWPE RKLKHMRFPL MYEENSRENP
FKRTNEIVEE QYTPQSLATL ESVFQELGKL TGPSNQKRER VDEEQKLYTD DEDDVYKTNN
IAYEDVVGGE DWSPIEEKIE TQTQEEVRDS KENTEKNEQI NEEMKRSGQL GLPDEENRRE
SKDQLSEDAS KVITYLRRLV NAVGSGRSQS GPNGDRAARL LQKPLDSQSI YQLIEISRNL
QIPPEDLIEM LKAGEKPNGL VEPEQDLELA VDLDDIPEAD LDRPDMFQSK MLSKGGYPKA
PGRGMVEALP DGLSVEDILN VLGMENVVNQ KSPYFPNQYS QDKALMRLPY GPGKSRANQI
PKVAWIPDVE SRQAPYENLN DQELGEYLAR MLVKYPELLN TNQLKRVPSP VSSEDDLQEE
EQLEQAIKEH LGPGSSQEME RLAKVSKRIP VGSLKNEDTP NRQYLDEDML LKVLEYLNQE
QAEQGREHLA KRAMENM
