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   29-MAY-2024, entry version 196.
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 {ECO:0000250|UniProtKB:P01165}.
CC       Note=Neuroendocrine and endocrine secretory granules.
CC       {ECO:0000250|UniProtKB:P01165}.
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|UniProtKB:P12961}.
CC   -!- PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:P12961}.
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; 25.
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; 9606-ENSP00000300175; -.
DR   PeptideAtlas; P05408; -.
DR   ProteomicsDB; 51834; -. [P05408-1]
DR   ProteomicsDB; 51835; -. [P05408-2]
DR   Antibodypedia; 2202; 176 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   AGR; HGNC:10816; -.
DR   CTD; 6447; -.
DR   DisGeNET; 6447; -.
DR   GeneCards; SCG5; -.
DR   HGNC; HGNC:10816; SCG5.
DR   HPA; ENSG00000166922; Tissue enhanced (brain, choroid plexus, 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; LGKWNKN; -.
DR   OrthoDB; 3024399at2759; -.
DR   PhylomeDB; P05408; -.
DR   TreeFam; TF314328; -.
DR   PathwayCommons; P05408; -.
DR   SignaLink; P05408; -.
DR   BioGRID-ORCS; 6447; 67 hits in 1149 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 100 other cell types or tissues.
DR   ExpressionAtlas; P05408; baseline and differential.
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; NEUROENDOCRINE PROTEIN 7B2; 1.
DR   PANTHER; PTHR12738:SF0; NEUROENDOCRINE PROTEIN 7B2; 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|UniProtKB:P01165"
FT                   /id="PRO_0000000042"
FT   PEPTIDE         200..212
FT                   /note="C-terminal peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P18844"
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|UniProtKB:P18844"
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
//