SCG2_RAT
ID SCG2_RAT Reviewed; 619 AA.
AC P10362;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 128.
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 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=3211750; DOI=10.1093/nar/16.24.11811;
RA Gerdes H.-H., Philipps E., Huttner W.B.;
RT "The primary structure of rat secretogranin II deduced from a cDNA
RT sequence.";
RL Nucleic Acids Res. 16:11811-11811(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8321414; DOI=10.1159/000126388;
RA Kakar S.S., Wei N., Mulchahey J.J., Leboeuf R.D., Neill J.D.;
RT "Regulation of expression of secretogranin II mRNA in female rat pituitary
RT and hypothalamus.";
RL Neuroendocrinology 57:422-431(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] 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 529-568, MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=15257142; DOI=10.1097/01.wnr.0000127634.38052.84;
RA Yajima A., Ikeda M., Miyazaki K., Maeshima T., Narita N., Narita M.;
RT "Manserin, a novel peptide from secretogranin II in the neuroendocrine
RT system.";
RL NeuroReport 15:1755-1759(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-270; SER-434;
RP SER-534 AND SER-558, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: 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 -!- TISSUE SPECIFICITY: [Manserin]: Brain. Expression in the pituitary is
CC restricted to the anterior lobe. Expression in the hypothalamus is
CC observed in the neuronal cells and neurons of arcuate nucleus,
CC supraoptic nucleus and median eminence (at protein level).
CC {ECO:0000269|PubMed:15257142}.
CC -!- MASS SPECTROMETRY: [Manserin]: Mass=4637; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15257142};
CC -!- MISCELLANEOUS: Binds calcium with a low-affinity.
CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC {ECO:0000305}.
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DR EMBL; X13618; CAA31950.1; -; mRNA.
DR EMBL; M93669; AAA42135.1; -; mRNA.
DR PIR; S02180; S02180.
DR RefSeq; NP_073160.1; NM_022669.1.
DR AlphaFoldDB; P10362; -.
DR SMR; P10362; -.
DR IntAct; P10362; 1.
DR STRING; 10116.ENSRNOP00000020219; -.
DR iPTMnet; P10362; -.
DR PhosphoSitePlus; P10362; -.
DR jPOST; P10362; -.
DR PaxDb; P10362; -.
DR PRIDE; P10362; -.
DR GeneID; 24765; -.
DR KEGG; rno:24765; -.
DR UCSC; RGD:3626; rat.
DR CTD; 7857; -.
DR RGD; 3626; Scg2.
DR eggNOG; ENOG502QV5W; Eukaryota.
DR InParanoid; P10362; -.
DR OrthoDB; 587478at2759; -.
DR PhylomeDB; P10362; -.
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:P10362; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031045; C:dense core granule; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISS:HGNC-UCL.
DR GO; GO:0098992; C:neuronal dense core vesicle; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
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; ISS: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:RGD.
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; IPR018054; Chromogranin_CS.
DR InterPro; IPR001990; Granin.
DR InterPro; IPR038858; ScgII.
DR PANTHER; PTHR15119; PTHR15119; 1.
DR Pfam; PF01271; Granin; 1.
DR PROSITE; PS00422; GRANINS_1; 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 CHAIN 31..619
FT /note="Secretogranin-2"
FT /id="PRO_0000005457"
FT PEPTIDE 184..216
FT /note="Secretoneurin"
FT /id="PRO_0000005458"
FT PEPTIDE 529..568
FT /note="Manserin"
FT /evidence="ECO:0000269|PubMed:15257142"
FT /id="PRO_0000432740"
FT REGION 247..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..307
FT /note="Basic and acidic residues"
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:0007744|PubMed:22673903"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03517"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 619 AA; 71031 MW; 27CB75B4F25A38D1 CRC64;
MTESKAYRFG AVLLLIHLIF LVPGTEAASF QRNQLLQKEP DLRLENVQKF PSPEMIRALE
YIEKLRQQAH REESSPDYNP YQGISVPLQL KENGEESHLA ESSRDVLSED EWMRIILEAL
RQAENEPPSA LKENKPYALN LEKNFPVDTP DDYETQQWPE RKLKHMRFPL MYEENSRENP
FKRTNEIVEE QYTPQSLATL ESVFQELGKL TGPSNQKRER VDEEQKLYTD DEDDVYKTNN
IAYEDVVGGE DWSPMEEKIE TQTQEEVRDS KENTEKNEQI NEEMKRSGHL GLPDEGNRKE
SKDQLSEDAS KVITYLRRLV NAVGSGRSQS GQNGDRAARL LERPLDSQSI YQLIEISRNL
QIPPEDLIEM LKAGEKPNGL VEPEQDLELA VDLDDIPEAD IDRPDMFQSK TLSKGGYPKA
PGRGMMEALP DGLSVEDILN VLGMENVANQ KSPYFPNQYS RDKALLRLPY GPGKSRANQI
PKVAWIPDVE SRQAPYDNLN DKDQELGEYL ARMLVKYPEL MNTNQLKRVP SPGSSEDDLQ
EEEQLEQAIK EHLGQGSSQE MEKLAKVSKR IPAGSLKNED TPNRQYLDED MLLKVLEYLN
QEQAEQGREH LAKRAMENM
