7B2_MOUSE
ID 7B2_MOUSE Reviewed; 212 AA.
AC P12961; Q8CCZ3; Q9CYP0; Q9D2P6; Q9DB14;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Neuroendocrine protein 7B2;
DE AltName: Full=Secretogranin V;
DE AltName: Full=Secretogranin-5;
DE AltName: Full=Secretory granule endocrine protein I;
DE Contains:
DE RecName: Full=N-terminal peptide;
DE Contains:
DE RecName: Full=C-terminal peptide;
DE Flags: Precursor;
GN Name=Scg5; Synonyms=Sgne-1, Sgne1;
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], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=BALB/cJ; TISSUE=Pancreas;
RX PubMed=2542174; DOI=10.1111/j.1399-3011.1989.tb00681.x;
RA Mbikay M., Grant S.G.N., Sirois F., Tadros H., Skowronski J., Lazure C.,
RA Seidah N.G., Hanahan D., Chretien M.;
RT "cDNA sequence of neuroendocrine protein 7B2 expressed in beta cell tumors
RT of transgenic mice.";
RL Int. J. Pept. Protein Res. 33:39-45(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Embryo, Hippocampus, and Medulla oblongata;
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 MRNA].
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9348280; DOI=10.1083/jcb.139.3.625;
RA Muller L., Zhu X., Lindberg I.;
RT "Mechanism of the facilitation of PC2 maturation by 7B2: involvement in
RT ProPC2 transport and activation but not folding.";
RL J. Cell Biol. 139:625-638(1997).
RN [5]
RP FUNCTION.
RX PubMed=10089884; DOI=10.1016/s0092-8674(00)80579-6;
RA Westphal C.H., Muller L., Zhou A., Zhu X., Bonner-Weir S., Schambelan M.,
RA Steiner D.F., Lindberg I., Leder P.;
RT "The neuroendocrine protein 7B2 is required for peptide hormone processing
RT in vivo and provides a novel mechanism for pituitary Cushing's disease.";
RL Cell 96:689-700(1999).
RN [6]
RP INHIBITION OF PCSK2 BY C-TERMINAL PEPTIDE.
RX PubMed=8016065; DOI=10.1073/pnas.91.13.5784;
RA Martens G.J.M., Braks J.A., Eib D.W., Zhou Y., Lindberg I.;
RT "The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of
RT prohormone convertase PC2.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5784-5787(1994).
RN [7]
RP SULFATION, CLEAVAGE BY FURIN-LIKE CONVERTASE, AND MUTAGENESIS OF ARG-177
RP AND ARG-178.
RX PubMed=8034690; DOI=10.1016/s0021-9258(17)32164-6;
RA Paquet L., Bergeron F., Boudreault A., Seidah N.G., Chretien M., Mbikay M.,
RA Lazure C.;
RT "The neuroendocrine precursor 7B2 is a sulfated protein proteolytically
RT processed by a ubiquitous furin-like convertase.";
RL J. Biol. Chem. 269:19279-19285(1994).
RN [8]
RP REVIEW.
RX PubMed=11439082; DOI=10.1042/0264-6021:3570329;
RA Mbikay M., Seidah N.G., Chretien M.;
RT "Neuroendocrine secretory protein 7B2: structure, expression and
RT functions.";
RL Biochem. J. 357:329-342(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND SER-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
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: Acts as a molecular chaperone for PCSK2/PC2, preventing its
CC premature activation in the regulated secretory pathway. Binds to
CC inactive PCSK2 in the endoplasmic reticulum and facilitates its
CC transport from there to later compartments of the secretory pathway
CC where it is proteolytically matured and activated. Also required for
CC cleavage of PCSK2 but does not appear to be involved in its folding.
CC Plays a role in regulating pituitary hormone secretion. The C-terminal
CC peptide inhibits PCSK2 in vitro. {ECO:0000269|PubMed:10089884,
CC ECO:0000269|PubMed:9348280}.
CC -!- SUBUNIT: Interacts with PCSK2/PC2 early in the secretory pathway.
CC Dissociation occurs at later stages (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC secretory granules.
CC -!- PTM: Proteolytically cleaved in the Golgi by a furin-like convertase to
CC generate bioactive peptides. {ECO:0000269|PubMed:8034690}.
CC -!- PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:8034690}.
CC -!- DISRUPTION PHENOTYPE: Mice have no demonstrable Pcsk2/Pc2 activity, are
CC deficient in processing islet hormones, and display hypoglycemia,
CC hyperproinsulinemia and hypoglucagonemia, similar to Pcsk2 null mice.
CC In contrast to Pcsk2 null mice, they develop Cushing's disease due to
CC excessive secretion of corticotropin from the pituitary and die before
CC 9 weeks, indicating a role for Sgne1 in control of peptide secretion
CC from the pituitary. {ECO:0000269|PubMed:9348280}.
CC -!- SIMILARITY: Belongs to the 7B2 family. {ECO:0000305}.
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DR EMBL; X15830; CAA33835.1; -; mRNA.
DR EMBL; AK005331; BAB23956.1; -; mRNA.
DR EMBL; AK011938; BAB27927.1; -; mRNA.
DR EMBL; AK017481; BAB30765.1; -; mRNA.
DR EMBL; AK019337; BAB31669.1; -; mRNA.
DR EMBL; AK031856; BAC27581.1; -; mRNA.
DR EMBL; BC029021; AAH29021.1; -; mRNA.
DR CCDS; CCDS16561.1; -.
DR PIR; S12477; S12477.
DR RefSeq; NP_033188.3; NM_009162.3.
DR AlphaFoldDB; P12961; -.
DR SMR; P12961; -.
DR BioGRID; 203198; 4.
DR STRING; 10090.ENSMUSP00000024005; -.
DR MEROPS; I21.001; -.
DR iPTMnet; P12961; -.
DR PhosphoSitePlus; P12961; -.
DR PaxDb; P12961; -.
DR PeptideAtlas; P12961; -.
DR PRIDE; P12961; -.
DR ProteomicsDB; 285577; -.
DR Antibodypedia; 2202; 155 antibodies from 26 providers.
DR DNASU; 20394; -.
DR Ensembl; ENSMUST00000024005; ENSMUSP00000024005; ENSMUSG00000023236.
DR GeneID; 20394; -.
DR KEGG; mmu:20394; -.
DR UCSC; uc008lpq.1; mouse.
DR CTD; 6447; -.
DR MGI; MGI:98289; Scg5.
DR VEuPathDB; HostDB:ENSMUSG00000023236; -.
DR eggNOG; KOG4187; Eukaryota.
DR GeneTree; ENSGT00390000009816; -.
DR HOGENOM; CLU_113154_0_0_1; -.
DR InParanoid; P12961; -.
DR OMA; GKWSKSL; -.
DR OrthoDB; 1534994at2759; -.
DR PhylomeDB; P12961; -.
DR TreeFam; TF314328; -.
DR BioGRID-ORCS; 20394; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Scg5; mouse.
DR PRO; PR:P12961; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P12961; protein.
DR Bgee; ENSMUSG00000023236; Expressed in paraventricular nucleus of hypothalamus and 173 other tissues.
DR ExpressionAtlas; P12961; baseline and differential.
DR Genevisible; P12961; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016486; P:peptide hormone processing; IDA:UniProtKB.
DR GO; GO:0046883; P:regulation of hormone secretion; IDA:UniProtKB.
DR InterPro; IPR007945; Secretogranin_V.
DR PANTHER; PTHR12738; PTHR12738; 1.
DR Pfam; PF05281; Secretogranin_V; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Neuropeptide; Phosphoprotein; Reference proteome; Secreted;
KW Signal; Sulfation; Transport.
FT SIGNAL 1..26
FT CHAIN 27..212
FT /note="Neuroendocrine protein 7B2"
FT /id="PRO_0000000044"
FT CHAIN 27..176
FT /note="N-terminal peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000045"
FT PEPTIDE 200..212
FT /note="C-terminal peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000046"
FT REGION 171..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT DISULFID 120..130
FT /evidence="ECO:0000250"
FT MUTAGEN 177
FT /note="R->A: No effect on proteolytic processing. Abolishes
FT proteolytic processing; when associated with G-178."
FT /evidence="ECO:0000269|PubMed:8034690"
FT MUTAGEN 178
FT /note="R->G: Abolishes proteolytic processing; when
FT associated with A-177."
FT /evidence="ECO:0000269|PubMed:8034690"
FT CONFLICT 6
FT /note="V -> G (in Ref. 2; BAB23956)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="P -> H (in Ref. 2; BAB30765)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="Q -> R (in Ref. 2; BAB31669)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="P -> T (in Ref. 2; BAC27581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 23866 MW; 6D8CD046532F9609 CRC64;
MASRLVSAML SGLLFWLMFE WNPAFAYSPR TPDRVSETDI QRLLHGVMEQ LGIARPRVEY
PAHQAMNLVG PQSIEGGAHE GLQHLGPFGN IPNIVAELTG DNIPKDFSED QGYPDPPNPC
PLGKTADDGC LENAPDTAEF SREFQLDQHL FDPEHDYPGL GKWNKKLLYE KMKGGQRRKR
RSVNPYLQGK RLDNVVAKKS VPHFSEEEKE AE
