SOGA1_MOUSE
ID SOGA1_MOUSE Reviewed; 1418 AA.
AC E1U8D0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 3.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Protein SOGA1;
DE AltName: Full=SOGA family member 1;
DE AltName: Full=Suppressor of glucose by autophagy;
DE AltName: Full=Suppressor of glucose, autophagy-associated protein 1;
DE Contains:
DE RecName: Full=N-terminal form;
DE Contains:
DE RecName: Full=C-terminal 80 kDa form;
DE Short=80-kDa SOGA fragment;
GN Name=Soga1; Synonyms=Soga;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION IN AUTOPHAGY INHIBITION,
RP PROTEOLYTIC PROCESSING, CLEAVAGE SITE, SUBUNIT, INDUCTION, TISSUE
RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=20813965; DOI=10.2353/ajpath.2010.100363;
RA Cowerd R.B., Asmar M.M., Alderman J.M., Alderman E.A., Garland A.L.,
RA Busby W.H., Bodnar W.M., Rusyn I., Medoff B.D., Tisch R., Mayer-Davis E.,
RA Swenberg J.A., Zeisel S.H., Combs T.P.;
RT "Adiponectin lowers glucose production by increasing SOGA.";
RL Am. J. Pathol. 177:1936-1945(2010).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulates autophagy by playing a role in the reduction of
CC glucose production in an adiponectin- and insulin-dependent manner.
CC {ECO:0000269|PubMed:20813965}.
CC -!- SUBUNIT: The C-terminal SOGA 25 kDa form occurs as a monomer.
CC {ECO:0000305|PubMed:20813965}.
CC -!- SUBCELLULAR LOCATION: [C-terminal 80 kDa form]: Secreted. Note=Secreted
CC in primary hepatocyte-conditioned media.
CC -!- TISSUE SPECIFICITY: Expressed in liver (at protein level).
CC {ECO:0000269|PubMed:20813965}.
CC -!- INDUCTION: Up-regulated by adiponectin in primary hepatocytes through
CC the insulin signaling pathway. Down-regulated by amino-imidazole
CC carboxamide riboside (AICAR), an AMPK activator that potentiated
CC insulin secretion. {ECO:0000269|PubMed:20813965}.
CC -!- PTM: Proteolytically cleaved into a C-terminal SOGA 25 kDa form that is
CC detected in plasma (By similarity). Proteolytically cleaved in primary
CC hepatocytes into a C-terminal SOGA 80 kDa form. {ECO:0000250,
CC ECO:0000269|PubMed:20813965}.
CC -!- SIMILARITY: Belongs to the SOGA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADC34694.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=DAA34787.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FJ977045; ADC34694.2; ALT_INIT; mRNA.
DR EMBL; BK007093; DAA34787.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; E1U8D0; -.
DR SMR; E1U8D0; -.
DR IntAct; E1U8D0; 4.
DR STRING; 10090.ENSMUSP00000066556; -.
DR iPTMnet; E1U8D0; -.
DR PhosphoSitePlus; E1U8D0; -.
DR MaxQB; E1U8D0; -.
DR PaxDb; E1U8D0; -.
DR PeptideAtlas; E1U8D0; -.
DR PRIDE; E1U8D0; -.
DR ProteomicsDB; 261548; -.
DR MGI; MGI:2444575; Soga1.
DR eggNOG; KOG4787; Eukaryota.
DR InParanoid; E1U8D0; -.
DR ChiTaRS; Soga1; mouse.
DR PRO; PR:E1U8D0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; E1U8D0; protein.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IDA:UniProtKB.
DR InterPro; IPR027882; DUF4482.
DR InterPro; IPR027881; SOGA.
DR Pfam; PF14818; DUF4482; 1.
DR Pfam; PF11365; SOGA; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome; Secreted.
FT CHAIN 1..1418
FT /note="Protein SOGA1"
FT /id="PRO_0000418051"
FT CHAIN 1..686
FT /note="N-terminal form"
FT /id="PRO_0000418052"
FT CHAIN 687..1418
FT /note="C-terminal 80 kDa form"
FT /id="PRO_0000418053"
FT REGION 112..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..76
FT /evidence="ECO:0000255"
FT COILED 105..149
FT /evidence="ECO:0000255"
FT COILED 191..384
FT /evidence="ECO:0000255"
FT COILED 603..663
FT /evidence="ECO:0000255"
FT COILED 787..817
FT /evidence="ECO:0000255"
FT COILED 875..915
FT /evidence="ECO:0000255"
FT SITE 686..687
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94964"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94964"
SQ SEQUENCE 1418 AA; 159186 MW; 4A36FE0AF8E22827 CRC64;
MLEMRDVYME EDVYQLQELR QQLDQASKTC RILQYRLRKA ERRSLRAAQT GQVDGELIRG
LEQDVKVSKD ISMRLHKELE VVEKKRMRLE EENEGLRQRL IETELAKQVL QTELDRPREH
SLKKRGTRSL GKTDKKPTAQ EDSADLKCQL HFAKEESALM CKKLTKLAKE NDSMKEELLK
YRSLYGDLDA ALSAEELADA PHSRETELKV HLKLVEEEAN LLSRRIVELE VENRGLRAEM
DDMKDHGGGG GPEARLAFSS LGGECGESLA ELRRHLQFVE EEAELLRRSS AELEDQNKLL
LNELAKYRSE HELDVTLSED SCSVLSEPSQ EELAAAKLQI GELSGKVKKL QYENRVLLSN
LQRCDLASCQ STRPMLETDA EAGDSAQCVP APLGETLEPH AARLCRAREA EALPGLREQA
ALVSKAIDVL VADANGFSVG LRLCLDNECA DLRLHEAPDN SEGPRDAKLI HAILVRLSVL
QQELNAFTRK ADVALGSSGK EQPEPFPALP ALGSQGPAKE IMLSKDLGSD FQPPDFRDLL
EWEPRIREAF RTGDLESKPD PSRNFRPYRA EDNDSYASEI KDLQLVLAEA HDSLRGLQEQ
LSQERQLRKE EADSFNQKMV QLKEDQQRAL LRREFELQSL SLQRRLEQKF WSQEKNILVQ
ESQQFKHNFL LLFMKLRWFL KRWRQGKVLP SEEDDFLEVN SMKELYLLME EEEMNAQHSD
NKACTGESWT QNTPNECIKT LADMKVTLKE LCWLLQDERR GLTELQQQFA KAKATWETER
AELKGHASQM ELKAGKGASE RPGPDWKAAL QREREEQQHL LAESYSAVME LTRQLQLSER
HWSQEKLQLV ERLQGEKQQV EQQVKELQNR LSQLQKAAEP WVLKHSDMEK QDNSWKEARS
EKTHDKEGVS EAELGGTGLK RTKSVSSMSE FESLLDCSPY LAGGDARNKK LPNGPAFAFV
STEPVEPEKD AKEKAGLSTR DCSHIGSLAC QEPAGRQMQR SYTAPDKTGI RVYYSPPVAR
RLGVPVVHDK EGKILIEPGF LFTTAKPKES AEADGLAESS YSRWLCNFSR QRLDGGSGAS
TSGSGPAFPA LHDFEMSGNM SDDMKEITNC VRQAMRSGSL ERKVKNTSSQ TVGVATVGTQ
TIRTVSVGLQ TDPPRSSLHS KSWSPRSSSL VSVRSKQISS SLDKVHSRIE RPCCSPKYGS
PKLQRRSVSK LDSTKDRSLW NLHQGKQNGS AWARSTTTRD SPVLRNINDG LSSLFSVVEH
SGSTESVWKL GMSEARTKPE PPKYGIVQEF FRNVCGRAPS PTTAAGEESC KKPEPLSPAS
YHQPEGVSRI LNKKAAKAGG SEEVRPTMLS QVGKDGILRD GDGSLILPSE DAVCDCSAQS
LASCFIRPSR NTIRHSPSKC RLHPSESGWG GEERAAPQ
