STBD1_RAT
ID STBD1_RAT Reviewed; 333 AA.
AC Q5FVN1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Starch-binding domain-containing protein 1 {ECO:0000303|PubMed:20810658};
DE AltName: Full=Genethonin-1 {ECO:0000303|PubMed:20810658};
DE AltName: Full=Glycophagy cargo receptor stbd1 {ECO:0000305};
GN Name=Stbd1 {ECO:0000303|PubMed:20810658};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP SUBCELLULAR LOCATION, DOMAIN, GLYCOGEN-BINDING, AND FUNCTION.
RX PubMed=20810658; DOI=10.1074/jbc.m110.150839;
RA Jiang S., Heller B., Tagliabracci V.S., Zhai L., Irimia J.M.,
RA DePaoli-Roach A.A., Wells C.D., Skurat A.V., Roach P.J.;
RT "Starch binding domain-containing protein 1/genethonin 1 is a novel
RT participant in glycogen metabolism.";
RL J. Biol. Chem. 285:34960-34971(2010).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-162; SER-201;
RP SER-208; SER-216 AND SER-219, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts as a cargo receptor for glycogen. Delivers its cargo to
CC an autophagic pathway called glycophagy, resulting in the transport of
CC glycogen to lysosomes. {ECO:0000250|UniProtKB:O95210,
CC ECO:0000269|PubMed:20810658}.
CC -!- SUBUNIT: Interacts with the ATG8 family proteins GABARAP and GABARAPL1
CC (By similarity). Interacts with several glycogen-associated proteins,
CC such as GYS2 (liver glycogen synthase), GDE (glycogen debranching
CC enzyme), GBE1 (glycogen branching enzyme 1) and EPM2A (Laforin) (By
CC similarity). {ECO:0000250|UniProtKB:O95210}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:20810658}; Single-pass type III membrane protein
CC {ECO:0000250|UniProtKB:O95210}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O95210}; Single-pass type III membrane protein
CC {ECO:0000250|UniProtKB:O95210}. Cell membrane, sarcolemma, T-tubule
CC {ECO:0000250|UniProtKB:O95210}. Note=Also detected near the junctional
CC sarcoplasmic reticulum (By similarity). Concentrates at perinuclear
CC structures (PubMed:20810658). {ECO:0000250|UniProtKB:O95210,
CC ECO:0000269|PubMed:20810658}.
CC -!- DOMAIN: The LIR motif (LC3-interacting region) is required for the
CC interaction with the ATG8 family protein GABARAPL1.
CC {ECO:0000250|UniProtKB:O95210}.
CC -!- DOMAIN: The C-terminal CBM20 domain is required for the interaction
CC with glycogen. {ECO:0000269|PubMed:20810658}.
CC -!- PTM: Ubiquitinated, which leads to proteasomal degradation.
CC {ECO:0000250|UniProtKB:O95210}.
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DR EMBL; BC089867; AAH89867.1; -; mRNA.
DR RefSeq; NP_001014010.1; NM_001013988.1.
DR AlphaFoldDB; Q5FVN1; -.
DR SMR; Q5FVN1; -.
DR IntAct; Q5FVN1; 1.
DR STRING; 10116.ENSRNOP00000003020; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR iPTMnet; Q5FVN1; -.
DR PhosphoSitePlus; Q5FVN1; -.
DR PaxDb; Q5FVN1; -.
DR Ensembl; ENSRNOT00000119917; ENSRNOP00000078314; ENSRNOG00000002218.
DR GeneID; 305234; -.
DR KEGG; rno:305234; -.
DR UCSC; RGD:1311800; rat.
DR CTD; 8987; -.
DR RGD; 1311800; Stbd1.
DR eggNOG; ENOG502SE11; Eukaryota.
DR GeneTree; ENSGT00390000007731; -.
DR HOGENOM; CLU_070592_0_0_1; -.
DR InParanoid; Q5FVN1; -.
DR OMA; NGGVTRW; -.
DR OrthoDB; 1378991at2759; -.
DR PhylomeDB; Q5FVN1; -.
DR TreeFam; TF338505; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q5FVN1; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002218; Expressed in quadriceps femoris and 18 other tissues.
DR Genevisible; Q5FVN1; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISS:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:GO_Central.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030315; C:T-tubule; ISO:RGD.
DR GO; GO:0038024; F:cargo receptor activity; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:2001069; F:glycogen binding; ISS:GO_Central.
DR GO; GO:0030247; F:polysaccharide binding; ISO:RGD.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; ISS:GO_Central.
DR GO; GO:0061723; P:glycophagy; ISS:GO_Central.
DR GO; GO:0046907; P:intracellular transport; ISO:RGD.
DR GO; GO:0061753; P:substrate localization to autophagosome; IEA:Ensembl.
DR CDD; cd05813; CBM20_genethonin_1; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR034838; CBM20_genethonin_1.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00686; CBM_20; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 1: Evidence at protein level;
KW Autophagy; Carbohydrate metabolism; Cell membrane; Endoplasmic reticulum;
KW Glycogen metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..333
FT /note="Starch-binding domain-containing protein 1"
FT /id="PRO_0000238962"
FT TOPO_DOM 1..6
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 233..332
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT REGION 31..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 181..187
FT /note="LIR"
FT /evidence="ECO:0000250|UniProtKB:O95210"
FT COMPBIAS 120..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95210"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95210"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95210"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C7E7"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 333 AA; 35494 MW; 65D081FB65EC04BD CRC64;
MGAVWSALLV GGGLAGALIL WLLRGDSGAP GKDGGAEPLK DAPPGEAAAP GGGPGGGGSG
GLSPEPSDRE LVSKAEHLRE SNGHLISESK DLGNLTEAQR LQNVGNAREY VPVGKVPDTH
SRANSETSRN QSPESRVGEW RLPKGHETAV KVAGSVAEKL PSSSPLMDRA EAASLAQSAG
HEDWEVVSRH SSWGSVGLGG SLEASRLSLN QGMDESRNSL VGGGWEVDGK VVSVKPRQVS
IQFKVHYSTS TDVQFIAVTG DHESLGGWNT YIPLHYCKDG LWSHSVFLPA DTVVEWKFVL
VENKEVTRWE ECSNRRLQTG HEDKVVHGWW GIH
