SCG2_BOVIN
ID SCG2_BOVIN Reviewed; 613 AA.
AC P20616; Q3ZBY6;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Secretogranin-2;
DE AltName: Full=Chromogranin-C;
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; Synonyms=CHGC;
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 [MRNA].
RX PubMed=2345170; DOI=10.1016/s0021-9258(19)38833-7;
RA Fischer-Colbrie R., Gutierrez J., Hsu C.M., Iacangelo A., Eiden L.E.;
RT "Sequence analysis, tissue distribution and regulation by cell
RT depolarization, and second messengers of bovine secretogranin II
RT (chromogranin C) mRNA.";
RL J. Biol. Chem. 265:9208-9213(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 181-213.
RX PubMed=9654353; DOI=10.1016/s0304-3940(98)00345-0;
RA Leitner B., Schneitler C., Klocker H., Volknandt W., Zimmermann H.,
RA Winkler H., Fischer-Colbrie R.;
RT "Formation and sequence analysis of secretoneurin, a neuropeptide derived
RT from secretogranin II, in mammalian, bird, reptile, amphibian and fish
RT brains.";
RL Neurosci. Lett. 248:105-108(1998).
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.
CC -!- MISCELLANEOUS: Binds calcium with a low-affinity.
CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC {ECO:0000305}.
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DR EMBL; J05468; AAA30760.1; -; mRNA.
DR EMBL; BC103034; AAI03035.1; -; mRNA.
DR PIR; A35296; A35296.
DR RefSeq; NP_776601.1; NM_174176.3.
DR AlphaFoldDB; P20616; -.
DR SMR; P20616; -.
DR STRING; 9913.ENSBTAP00000028766; -.
DR PaxDb; P20616; -.
DR PRIDE; P20616; -.
DR Ensembl; ENSBTAT00000028766; ENSBTAP00000028766; ENSBTAG00000021588.
DR GeneID; 281477; -.
DR KEGG; bta:281477; -.
DR CTD; 7857; -.
DR VEuPathDB; HostDB:ENSBTAG00000021588; -.
DR VGNC; VGNC:34332; SCG2.
DR eggNOG; ENOG502QV5W; Eukaryota.
DR GeneTree; ENSGT00390000010895; -.
DR HOGENOM; CLU_031294_0_0_1; -.
DR InParanoid; P20616; -.
DR OMA; KYPEIIN; -.
DR OrthoDB; 587478at2759; -.
DR TreeFam; TF334018; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000021588; Expressed in adenohypophysis and 79 other tissues.
DR ExpressionAtlas; P20616; baseline.
DR GO; GO:0005615; C:extracellular space; ISS:HGNC-UCL.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0042056; F:chemoattractant activity; ISS:HGNC-UCL.
DR GO; GO:0005125; F:cytokine activity; ISS:HGNC-UCL.
DR GO; GO:0001525; P:angiogenesis; ISS:HGNC-UCL.
DR GO; GO:0048245; P:eosinophil chemotaxis; ISS:HGNC-UCL.
DR GO; GO:0050930; P:induction of positive chemotaxis; ISS:HGNC-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:HGNC-UCL.
DR GO; GO:0000165; P:MAPK cascade; ISS:HGNC-UCL.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISS:HGNC.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0050918; P:positive chemotaxis; ISS:HGNC.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:HGNC-UCL.
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_0000005449"
FT CHAIN 31..613
FT /note="Secretogranin-2"
FT /id="PRO_0000005450"
FT PEPTIDE 181..213
FT /note="Secretoneurin"
FT /id="PRO_0000005451"
FT PEPTIDE 523..562
FT /note="Manserin"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT /id="PRO_0000432734"
FT REGION 67..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..580
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 124..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 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03517"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03517"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03517"
FT CONFLICT 109
FT /note="W -> S (in Ref. 2; AAI03035)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="S -> P (in Ref. 1; AAA30760)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="E -> G (in Ref. 2; AAI03035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 70346 MW; F10E64255B09E617 CRC64;
MAEAKTHWLG AVLSLIPLIF LLSEAEAASF QRNQLLQKEP DLRLENVQRF PSPEMIRALE
YIEKLRQQAH KEESSPDYNP YQGVSVPLQQ KENGDLPESS RDSLSEDEWM KIIAEALRQA
ENEPQSAPKE NKPYTLNSEK NFPMDMPDDY ETQQWAERKL KHMRFPPMYE ENSRDNPFKR
TNEIVEEQYT PQNLATLESV FQELGKLTGP NSQKRERADE EQKLYTDDED DIYKANNIAY
EDVVGGEDWN PVEEKIESQT QEEVRDSKEN ADKTEQINDE MKRSGQLGLQ DEDLRKESKD
QLSDDVSKVI TYLKRLVNAA GSGRSQNGQT GERAIRLFEK PLDPQSIYQL IEISRNLQIP
PEDLIDMLKT GEKPVEPEQE LEIPVEPEDI SEVDLDHPDL FQNKMLSKNG YPKAPGHAVA
EALSEGLSVE DILNLLGMES AANPKPPYFP NQYNREKVLS RLPYGPGRSK ANQLPKAVWM
PDVENRQMAY ENLNDKDQEL GEYLARMLVK YPEIMNANPA KRVPSQGSTE DDRQDENQIE
QALKEHLSQH SSQETDKLAS VSKRLPVGTP KSDDTPNRPY LDEDLLVKVL EYLNQEKAEK
GREHIAKRAM ENM
