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SCG3_XENTR
ID   SCG3_XENTR              Reviewed;         463 AA.
AC   F7E728; A4IIY0; A7MC32;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 2.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Secretogranin-3;
DE   AltName: Full=Secretogranin III;
DE            Short=SgIII;
DE   Flags: Precursor;
GN   Name=scg3;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-395 (ISOFORMS 1 AND 2).
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Member of the granin protein family that regulates the
CC       biogenesis of secretory granules (By similarity). Acts as a sorting
CC       receptor for intragranular proteins including chromogranin A/CHGA (By
CC       similarity). May also play a role in angiogenesis. Promotes endothelial
CC       proliferation, migration and tube formation through MEK/ERK signaling
CC       pathway (By similarity). {ECO:0000250|UniProtKB:P47868,
CC       ECO:0000250|UniProtKB:Q8WXD2}.
CC   -!- SUBUNIT: Interacts with CHGA (By similarity). Interacts with
CC       secretogranin II/SCG2 (By similarity). Interacts (via C-terminus) with
CC       CPE (By similarity). {ECO:0000250|UniProtKB:P47867,
CC       ECO:0000250|UniProtKB:Q8WXD2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000250|UniProtKB:P47868}. Cytoplasmic vesicle, secretory vesicle
CC       membrane {ECO:0000250|UniProtKB:P47868}; Peripheral membrane protein.
CC       Secreted {ECO:0000250|UniProtKB:Q8WXD2}. Note=Associated with the
CC       secretory granule membrane through direct binding to cholesterol-
CC       enriched lipid rafts. {ECO:0000250|UniProtKB:P47868}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=F7E728-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F7E728-2; Sequence=VSP_043175;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI36198.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAI52025.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AAMC01056589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01056590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01056591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC136197; AAI36198.1; ALT_SEQ; mRNA.
DR   EMBL; BC152024; AAI52025.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001263622.1; NM_001276693.1.
DR   RefSeq; NP_001263623.1; NM_001276694.1.
DR   AlphaFoldDB; F7E728; -.
DR   SMR; F7E728; -.
DR   STRING; 8364.ENSXETP00000052912; -.
DR   PaxDb; F7E728; -.
DR   GeneID; 100125084; -.
DR   KEGG; xtr:100125084; -.
DR   CTD; 29106; -.
DR   Xenbase; XB-GENE-966935; scg3.
DR   eggNOG; ENOG502QUJH; Eukaryota.
DR   HOGENOM; CLU_031198_1_0_1; -.
DR   InParanoid; F7E728; -.
DR   OrthoDB; 692526at2759; -.
DR   Reactome; R-XTR-114608; Platelet degranulation.
DR   Reactome; R-XTR-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-XTR-8957275; Post-translational protein phosphorylation.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033366; P:protein localization to secretory granule; IBA:GO_Central.
DR   InterPro; IPR026197; SCG3.
DR   PANTHER; PTHR17388; PTHR17388; 1.
DR   Pfam; PF15467; SGIII; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cleavage on pair of basic residues;
KW   Cytoplasmic vesicle; Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..463
FT                   /note="Secretogranin-3"
FT                   /id="PRO_0000417024"
FT   REGION          87..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         353
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_043175"
FT   CONFLICT        234
FT                   /note="E -> G (in Ref. 2; AAI36198)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        392..394
FT                   /note="DKP -> KKK (in Ref. 2; AAI36198/AAI52025)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   463 AA;  52476 MW;  F2883301A1224267 CRC64;
     MGPKYVFITA IIGVFWHVQG FPNPGIKQDK AVHNRELSEE RPLEEQIAEA DTVSRGTSKE
     NQEMLKNDSF ADELGLLMSV AEKEGDVKRS GSVRSSVGGH RGTLDDADST KNLKPAEYFD
     STKSMLDYKY EDDPDGLHQL DGTPLTAEDI VRKIATRIYE ENDRGVFDKI VSKLLNLGLI
     TESQAYTLED EVAEVLQQLI ANEAKNREKE AGDLDYAAVR SDVYDDDKQE GKMETRNKNE
     DRESSETKNE DSFSSKERRN ELSPEEDFDD LQYFPNFNRL IKSLNSENDA KEKKTLITIM
     KTLIDFVKMM VKYGTITPEE GVNYLENLDA MIAVQAKNKL GKSFGSHKSI LSEDKNVDES
     DSTKQEAAKM EKEYEALKDS TKPEPKDAED KDKPKGKAET YLEAIRKNIE WLKEHNKEGN
     KGVSDNDLSK LKDFINQQAD SYVEKGILDK EEANVIKRIY SSL
 
 
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