ID   SCG2_PELRI              Reviewed;         601 AA.
AC   P30945;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Secretogranin-2;
DE   AltName: Full=Secretogranin II;
DE            Short=SgII;
DE   Contains:
DE     RecName: Full=Secretoneurin;
DE              Short=SN;
DE     AltName: Full=Brain peptide;
DE   Flags: Precursor;
OS   Pelophylax ridibundus (Marsh frog) (Rana ridibunda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=8406;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=8830661; DOI=10.1016/0014-5793(96)00976-3;
RA   Anouar Y., Jegou S., Alexandre D., Lihrmann I., Conlon J.M., Vaudry H.;
RT   "Molecular cloning of frog secretogranin II reveals the occurrence of
RT   several highly conserved potential regulatory peptides.";
RL   FEBS Lett. 394:295-299(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 183-215.
RC   TISSUE=Brain;
RX   PubMed=2060624; DOI=10.1016/0014-5793(91)80754-q;
RA   Vaudry H., Conlon J.M.;
RT   "Identification of a peptide arising from the specific post-translation
RT   processing of secretogranin II.";
RL   FEBS Lett. 284:31-33(1991).
CC   -!- FUNCTION: May be important in regulation of neurosecretion.
CC   -!- SUBCELLULAR LOCATION: [Secretogranin-2]: Cytoplasmic vesicle, secretory
CC       vesicle {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Secretoneurin]: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC       {ECO:0000305}.
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DR   EMBL; U68757; AAB17470.1; -; mRNA.
DR   PIR; S74239; S74239.
DR   AlphaFoldDB; P30945; -.
DR   SMR; P30945; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030141; C:secretory granule; IEA:InterPro.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001990; Granin.
DR   InterPro; IPR038858; ScgII.
DR   PANTHER; PTHR15119; PTHR15119; 1.
DR   Pfam; PF01271; Granin; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW   Direct protein sequencing; Secreted; Signal; Sulfation.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000250"
FT   CHAIN           31..601
FT                   /note="Secretogranin-2"
FT                   /id="PRO_0000005459"
FT   PEPTIDE         183..215
FT                   /note="Secretoneurin"
FT                   /id="PRO_0000005460"
FT   REGION          89..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         151
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P13521"
SQ   SEQUENCE   601 AA;  69900 MW;  8D16FDAA1280A712 CRC64;
     MSSQRNYCLA GCLSSCILVI LMSFSDAASF QYYQVPQQDQ EYRMKTLQRL PSPDMLKALE
     YIENLRKQAS RTESLPDYTS YQGAPFLSEQ KDTQALSTDT AKSPTSDDES EWMRAMLEAL
     MQAEKEAKVS PQEKNNLYMD KNIPPELIED YDSNKWSEKR PKAGKFSSRL YDDYSRDNPL
     KRTNEIVEGQ YTPQSLATLQ SVFQELGKLK GQANNKRDRM EEDQKLYKDD EDDLYKANNI
     AYEDVAGGED WNPIEEKVES QTQEELKESK EEVEKTDDME DEIKRSGLLG LQDEEPEKDT
     KEQESENLSN LMNTYLNMWM NRMDKGKQNP DRRSLRFSGK ELDPEAIYQL IDISRNLQIP
     PEDLIDMLRD EDGRKFGGRL ESEKEVDVPL DLDEVTETMT DKTNVYKNKQ GFVRQPTSPV
     LPNIPEGLTV EDMVNLMGAD KLQNRFKQNN GLQRPYPMLS KIKGHKAIWP KESEKRQIEY
     ESRPEKEEEL ADYVVKMLAK YPELLGNNQN KKMPIPYSAG DLQELEKQYE NALRGYVNMR
     GYQDLETVSS SNRRLSTREN DDTQNKQYID EDLLMKVLEY LNQEKAEKAR DHSVKRSMEN
     M