ID   SCG2_PONAB              Reviewed;         617 AA.
AC   Q5R4M6;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Secretogranin-2;
DE   AltName: Full=Secretogranin II;
DE            Short=SgII;
DE   Contains:
DE     RecName: Full=Secretoneurin;
DE              Short=SN;
DE   Contains:
DE     RecName: Full=Manserin;
DE   Flags: Precursor;
GN   Name=SCG2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Neuroendocrine protein of the granin family that regulates
CC       the biogenesis of secretory granules. {ECO:0000250|UniProtKB:P13521}.
CC   -!- SUBUNIT: Interacts with Secretogranin III/SCG3.
CC       {ECO:0000250|UniProtKB:P13521}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC       secretory granules. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Binds calcium with a low-affinity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC       {ECO:0000305}.
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DR   EMBL; CR861220; CAH93290.1; -; mRNA.
DR   RefSeq; NP_001127651.1; NM_001134179.1.
DR   AlphaFoldDB; Q5R4M6; -.
DR   SMR; Q5R4M6; -.
DR   STRING; 9601.ENSPPYP00000014779; -.
DR   PRIDE; Q5R4M6; -.
DR   GeneID; 100174732; -.
DR   KEGG; pon:100174732; -.
DR   CTD; 7857; -.
DR   eggNOG; ENOG502QV5W; Eukaryota.
DR   InParanoid; Q5R4M6; -.
DR   OrthoDB; 587478at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030141; C:secretory granule; IEA:InterPro.
DR   InterPro; IPR018054; Chromogranin_CS.
DR   InterPro; IPR001990; Granin.
DR   InterPro; IPR038858; ScgII.
DR   PANTHER; PTHR15119; PTHR15119; 1.
DR   Pfam; PF01271; Granin; 1.
DR   PROSITE; PS00422; GRANINS_1; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cleavage on pair of basic residues; Phosphoprotein;
KW   Reference proteome; Secreted; Signal; Sulfation.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..30
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000352524"
FT   CHAIN           31..617
FT                   /note="Secretogranin-2"
FT                   /id="PRO_0000352525"
FT   PEPTIDE         182..214
FT                   /note="Secretoneurin"
FT                   /id="PRO_0000352526"
FT   PEPTIDE         527..566
FT                   /note="Manserin"
FT                   /evidence="ECO:0000250|UniProtKB:P10362"
FT                   /id="PRO_0000432739"
FT   REGION          68..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         151
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P13521"
FT   MOD_RES         174
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10362"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10362"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P10362"
FT   MOD_RES         532
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03517"
FT   MOD_RES         555
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03517"
FT   MOD_RES         556
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03517"
SQ   SEQUENCE   617 AA;  70872 MW;  7CA6D9A8188242E6 CRC64;
     MAEAKTHWLG AALSLIPLIF LISGAEAASF QRNQLLQKEP DLRLENVKKF PSPEMIRALE
     YIEKLRQQAH KEESSSDYNP YQGVSVPFQQ KENGDESHLP ERDSLSEEDW MRIILEALRQ
     AENEPQSAPK ENKPYALNSE KNFPMDMSDD YETQQWPERK LKHMQFPPMN EENSRDNPFK
     RTNEIVEEQY APQSLATLES VFQELGKLTG PNNQKRERMD EEQKLYTDDE DDIYKANNIA
     YEDVVGGEDW NPVEEKIESQ TQEEVRDSKE NIEKNEQIND EMKRSGQLGI QEEDLRKESK
     DQLSDDVSKV IAYLKRLVNA AGSGRLQNGQ NGERATRLFE KPLDSQSIYQ LIEISRNLQI
     PPEDLIEMLK TGEKPNGSVE PERELDLPVD LDDISEADLD HPDLFQNKML SKSGYPKTPG
     RAGTEALPDG LSVEDILNLL GMESAANQKT SYFPNPYNQE KVLPRLPYGP GRSRSNQLPK
     AAWMPYVENR QMAYENLNDK DQELGEYLAR MLVKYPEIIS SNQVKRVPGQ SSSEDDLQEE
     EQIEQAIKEH LNQGSSQETD KLAPVSKRFP VGPPKNDDTP NRQYLDEDLL MKVLEYLNQE
     KAEKGREHIA KRAMENM