SCG3_BOVIN
ID SCG3_BOVIN Reviewed; 471 AA.
AC A6QLI2; F1MY56;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Secretogranin-3;
DE AltName: Full=Secretogranin III;
DE Short=SgIII;
DE Flags: Precursor;
GN Name=SCG3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DAAA02029009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02029010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02029011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC147974; AAI47975.1; -; mRNA.
DR RefSeq; NP_001095567.1; NM_001102097.1.
DR AlphaFoldDB; A6QLI2; -.
DR STRING; 9913.ENSBTAP00000023512; -.
DR PaxDb; A6QLI2; -.
DR PRIDE; A6QLI2; -.
DR Ensembl; ENSBTAT00000023512; ENSBTAP00000023512; ENSBTAG00000017677.
DR GeneID; 525941; -.
DR KEGG; bta:525941; -.
DR CTD; 29106; -.
DR VEuPathDB; HostDB:ENSBTAG00000017677; -.
DR VGNC; VGNC:34333; SCG3.
DR eggNOG; ENOG502QUJH; Eukaryota.
DR GeneTree; ENSGT00390000005488; -.
DR HOGENOM; CLU_031198_1_0_1; -.
DR InParanoid; A6QLI2; -.
DR OMA; MEKEYEI; -.
DR OrthoDB; 692526at2759; -.
DR TreeFam; TF331266; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000017677; Expressed in adenohypophysis and 81 other tissues.
DR ExpressionAtlas; A6QLI2; baseline and differential.
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 Cleavage on pair of basic residues; Cytoplasmic vesicle; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..471
FT /note="Secretogranin-3"
FT /id="PRO_0000417022"
FT REGION 23..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47867"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47867"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 471 AA; 53751 MW; 267A1E8AA89E70F6 CRC64;
MGFLWTGTWI VVLMLHSSPI QAFPKPAGSQ DKPLHNRELS AERPLNEQIA EAEADEIKKT
YPPENKPGES NYSFVDNLNL LKAITEKEKN EKERQSVKIS PNDNKLNVED VDSTKNRRLI
DDYDSTKSGL DRKFQDDPDG LHQLDGTPLT AEDIVQKIAT RIYEENDRGV FDRIVSKLLN
LGLITESQAH TLEDEVAEVL QKLISKEANN YEEELNKPTS KTESQTGKIP EKVTPMAAIQ
DAFTNGENDE TVSNTLTLTN GLERRTKTYS EDNFEELQYF PNFYALLKSI DSEKEAKEKE
TLITIMKTLI DFVKMMVKYG TISPEEGVSY LENLDETIAL QTKNKLEKNV TDNKSKLFAV
PSEKSHEETD STKEEAAKME KEYGTLKDST KDDDSNPRGK TDEHKGKTEA YLEAIRKNID
WLKKHNKKEN KEDYDLSKMR DFINQQADAY VEKGILDKEE ADAIKRIYSS L
