SCG2_PIG
ID SCG2_PIG Reviewed; 616 AA.
AC Q5FZP5;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 51.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-208; ASP-557; LEU-573 AND
RP THR-597.
RX PubMed=18278550; DOI=10.1007/s10528-008-9153-y;
RA Du H.L., Chen J., Zhang Y.S., Zhang X.Q.;
RT "Molecular cloning, mapping, and polymorphism of the porcine SCG2 gene.";
RL Biochem. Genet. 46:369-379(2008).
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; AY870646; AAW63723.1; -; mRNA.
DR RefSeq; NP_001012299.1; NM_001012299.1.
DR AlphaFoldDB; Q5FZP5; -.
DR SMR; Q5FZP5; -.
DR STRING; 9823.ENSSSCP00000027906; -.
DR PaxDb; Q5FZP5; -.
DR PeptideAtlas; Q5FZP5; -.
DR PRIDE; Q5FZP5; -.
DR GeneID; 497237; -.
DR KEGG; ssc:497237; -.
DR CTD; 7857; -.
DR eggNOG; ENOG502QV5W; Eukaryota.
DR InParanoid; Q5FZP5; -.
DR OrthoDB; 587478at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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_0000352314"
FT CHAIN 31..616
FT /note="Secretogranin-2"
FT /id="PRO_0000352315"
FT PEPTIDE 181..213
FT /note="Secretoneurin"
FT /evidence="ECO:0000250"
FT /id="PRO_0000352316"
FT PEPTIDE 526..565
FT /note="Manserin"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT /id="PRO_0000432738"
FT REGION 68..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P13521"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03517"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03517"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03517"
FT VARIANT 208
FT /note="T -> A"
FT /evidence="ECO:0000269|PubMed:18278550"
FT VARIANT 557
FT /note="E -> D"
FT /evidence="ECO:0000269|PubMed:18278550"
FT VARIANT 573
FT /note="P -> L"
FT /evidence="ECO:0000269|PubMed:18278550"
FT VARIANT 597
FT /note="N -> T"
FT /evidence="ECO:0000269|PubMed:18278550"
SQ SEQUENCE 616 AA; 70999 MW; D945210BB730FC9C CRC64;
MAEAKTHWLG ASLSLILLIF LLATAEAASF QRNQLLQKEP DLRLENVQRF ASPEMIRALE
YIEKLRQQAH KEESSPDYNP YQGVSVPLQQ KENSDLPESS RDSLSEDEWM KILLEALRQA
ENEPQSSLKE NKPYTLNSEK NFPMDMPDDY ETQQWPERKL EHMRFPPMYE ENSRDNPFKR
TNEIVEEQYT PQSLATLESV FQELGKLTGP NNQKRERVDE EQKLYTDDED DIYKANNIAY
EDVVGGEDWN PVEEKIESQT QEEVRDSKEN IEKNEQINDE MKRSGQMGLQ DEDLRKEGKD
QLSEDVSKVI AYLKRLVNAV GSGKSQNGQN GERANRLFEK PLDSQSIYQL IELSRNLQIP
PEDLIDMLKT GEKPNASVEP EQELEIPVDL DDISEVDLDH PDLFQNKMLS KNGYSKTPGR
AVSEALPDGL SVEDILNLLG MENAANQKPP YFPNQYNREK ILPRLPYGPG RAKANQLPKA
VWMPDVENRQ MAYDNLNDKD QELGEYLARM LVKYPEIMNS NQVKRVPSQG SSEDDLQEEN
QIEQAIKERL NQHSSQETDK LALVSKRLPV ATPKSDDAPN RQYLDEDLLM KVLEYLNQEK
AEKGREHIAK RAMENM
