7B2_HUMAN
ID 7B2_HUMAN Reviewed; 212 AA.
AC P05408; P01164; Q6FHD0; Q9BS38;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Neuroendocrine protein 7B2;
DE AltName: Full=Pituitary polypeptide;
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=SGNE1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Pituitary;
RX PubMed=3134253; DOI=10.1016/0014-5793(88)81324-3;
RA Martens G.J.M.;
RT "Cloning and sequence analysis of human pituitary cDNA encoding the novel
RT polypeptide 7B2.";
RL FEBS Lett. 234:160-164(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 125-140
RP (ISOFORM 1), AND PROTEIN SEQUENCE OF 126-132 (ISOFORM 2).
RC TISSUE=Pituitary;
RX PubMed=1989596; DOI=10.1016/0006-291x(91)90499-w;
RA Paquet L., Lazure C., Seidah N.G., Chretien M., Mbikay M.;
RT "The production by alternate splicing of two mRNAs differing by one codon
RT could be an intrinsic property of neuroendocrine protein 7B2 gene
RT expression in man.";
RL Biochem. Biophys. Res. Commun. 174:156-162(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jackson R.S.;
RT "Human neuroendocrine protein 7B2 genomic organization.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pancreas;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-92.
RX PubMed=8617287; DOI=10.1111/j.1432-1033.1996.00060.x;
RA Braks J.A., Broers C.A., Danger J.M., Martens G.J.M.;
RT "Structural organization of the gene encoding the neuroendocrine chaperone
RT 7B2.";
RL Eur. J. Biochem. 236:60-67(1996).
RN [8]
RP PROTEIN SEQUENCE OF 27-103.
RX PubMed=6625600; DOI=10.1016/0003-9861(83)90063-2;
RA Seidah N.G., Hsi K.L., de Serres G., Rochemont J., Hamelin J., Antakly T.,
RA Cantin M., Chretien M.;
RT "Isolation and NH2-terminal sequence of a highly conserved human and
RT porcine pituitary protein belonging to a new superfamily.
RT Immunocytochemical localization in pars distalis and pars nervosa of the
RT pituitary and in the supraoptic nucleus of the hypothalamus.";
RL Arch. Biochem. Biophys. 225:525-534(1983).
RN [9]
RP FUNCTION, AND INTERACTION WITH PCSK2.
RX PubMed=7913882; DOI=10.1016/0092-8674(94)90296-8;
RA Braks J.A., Martens G.J.M.;
RT "7B2 is a neuroendocrine chaperone that transiently interacts with
RT prohormone convertase PC2 in the secretory pathway.";
RL Cell 78:263-273(1994).
RN [10]
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).
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:7913882}.
CC -!- SUBUNIT: Interacts with PCSK2/PC2 early in the secretory pathway.
CC Dissociation occurs at later stages. {ECO:0000269|PubMed:7913882}.
CC -!- INTERACTION:
CC P05408; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-722635, EBI-16439278;
CC P05408; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-722635, EBI-741480;
CC P05408; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-722635, EBI-10173939;
CC P05408; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-722635, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC secretory granules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P05408-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P05408-2; Sequence=VSP_011754;
CC -!- PTM: Proteolytically cleaved in the Golgi by a furin-like convertase to
CC generate bioactive peptides. {ECO:0000250}.
CC -!- PTM: Sulfated on tyrosine residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 7B2 family. {ECO:0000305}.
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DR EMBL; Y00757; CAA68726.1; -; mRNA.
DR EMBL; AJ290438; CAB90397.1; -; Genomic_DNA.
DR EMBL; AJ290439; CAB90397.1; JOINED; Genomic_DNA.
DR EMBL; AJ290440; CAB90397.1; JOINED; Genomic_DNA.
DR EMBL; AJ290441; CAB90397.1; JOINED; Genomic_DNA.
DR EMBL; AJ290442; CAB90397.1; JOINED; Genomic_DNA.
DR EMBL; CR541824; CAG46623.1; -; mRNA.
DR EMBL; CH471125; EAW92262.1; -; Genomic_DNA.
DR EMBL; BC005349; AAH05349.1; -; mRNA.
DR EMBL; BC093053; AAH93053.1; -; mRNA.
DR CCDS; CCDS45207.1; -. [P05408-1]
DR CCDS; CCDS45208.1; -. [P05408-2]
DR PIR; S01008; PUHU.
DR RefSeq; NP_001138229.1; NM_001144757.2. [P05408-1]
DR RefSeq; NP_003011.1; NM_003020.4. [P05408-2]
DR AlphaFoldDB; P05408; -.
DR SMR; P05408; -.
DR BioGRID; 112345; 24.
DR IntAct; P05408; 8.
DR MINT; P05408; -.
DR STRING; 9606.ENSP00000300175; -.
DR MEROPS; I21.001; -.
DR iPTMnet; P05408; -.
DR PhosphoSitePlus; P05408; -.
DR BioMuta; SCG5; -.
DR DMDM; 23830842; -.
DR EPD; P05408; -.
DR MassIVE; P05408; -.
DR PaxDb; P05408; -.
DR PeptideAtlas; P05408; -.
DR PRIDE; P05408; -.
DR ProteomicsDB; 51834; -. [P05408-1]
DR ProteomicsDB; 51835; -. [P05408-2]
DR Antibodypedia; 2202; 155 antibodies from 26 providers.
DR DNASU; 6447; -.
DR Ensembl; ENST00000300175.9; ENSP00000300175.4; ENSG00000166922.9. [P05408-1]
DR Ensembl; ENST00000413748.6; ENSP00000388560.2; ENSG00000166922.9. [P05408-2]
DR Ensembl; ENST00000614359.1; ENSP00000482615.1; ENSG00000277614.1. [P05408-1]
DR Ensembl; ENST00000632219.1; ENSP00000488109.1; ENSG00000281931.1. [P05408-1]
DR Ensembl; ENST00000632674.1; ENSP00000488509.1; ENSG00000281931.1. [P05408-2]
DR GeneID; 6447; -.
DR KEGG; hsa:6447; -.
DR MANE-Select; ENST00000300175.9; ENSP00000300175.4; NM_001144757.3; NP_001138229.1.
DR UCSC; uc001zgz.3; human. [P05408-1]
DR CTD; 6447; -.
DR DisGeNET; 6447; -.
DR GeneCards; SCG5; -.
DR HGNC; HGNC:10816; SCG5.
DR HPA; ENSG00000166922; Tissue enhanced (pancreas, pituitary gland).
DR MIM; 173120; gene.
DR neXtProt; NX_P05408; -.
DR OpenTargets; ENSG00000166922; -.
DR PharmGKB; PA35724; -.
DR VEuPathDB; HostDB:ENSG00000166922; -.
DR eggNOG; KOG4187; Eukaryota.
DR GeneTree; ENSGT00390000009816; -.
DR InParanoid; P05408; -.
DR OMA; GKWSKSL; -.
DR PhylomeDB; P05408; -.
DR TreeFam; TF314328; -.
DR PathwayCommons; P05408; -.
DR SignaLink; P05408; -.
DR BioGRID-ORCS; 6447; 66 hits in 1071 CRISPR screens.
DR ChiTaRS; SCG5; human.
DR GeneWiki; SCG5; -.
DR GenomeRNAi; 6447; -.
DR Pharos; P05408; Tbio.
DR PRO; PR:P05408; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P05408; protein.
DR Bgee; ENSG00000166922; Expressed in islet of Langerhans and 99 other tissues.
DR ExpressionAtlas; P05408; baseline and differential.
DR Genevisible; P05408; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; ISS:UniProtKB.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016486; P:peptide hormone processing; ISS:UniProtKB.
DR GO; GO:0046883; P:regulation of hormone secretion; ISS:UniProtKB.
DR InterPro; IPR007945; Secretogranin_V.
DR PANTHER; PTHR12738; PTHR12738; 1.
DR Pfam; PF05281; Secretogranin_V; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Neuropeptide; Phosphoprotein;
KW Reference proteome; Secreted; Signal; Sulfation; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:6625600"
FT CHAIN 27..212
FT /note="Neuroendocrine protein 7B2"
FT /id="PRO_0000000041"
FT CHAIN 27..176
FT /note="N-terminal peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000042"
FT PEPTIDE 200..212
FT /note="C-terminal peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000043"
FT REGION 174..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12961"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12961"
FT DISULFID 120..130
FT /evidence="ECO:0000250"
FT VAR_SEQ 126
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1989596, ECO:0000303|PubMed:3134253,
FT ECO:0000303|Ref.4"
FT /id="VSP_011754"
FT CONFLICT 151
FT /note="F -> S (in Ref. 6; AAH05349)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 23730 MW; A459702055C0FE84 CRC64;
MVSRMVSTML SGLLFWLASG WTPAFAYSPR TPDRVSEADI QRLLHGVMEQ LGIARPRVEY
PAHQAMNLVG PQSIEGGAHE GLQHLGPFGN IPNIVAELTG DNIPKDFSED QGYPDPPNPC
PVGKTADDGC LENTPDTAEF SREFQLHQHL FDPEHDYPGL GKWNKKLLYE KMKGGERRKR
RSVNPYLQGQ RLDNVVAKKS VPHFSDEDKD PE
